Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation

Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence,...

Full description

Saved in:
Bibliographic Details
Published inFrontiers in microbiology Vol. 8; p. 832
Main Authors Yang, Jie, Li, Wenjuan, Ng, Tzi Bun, Deng, Xiangzhen, Lin, Juan, Ye, Xiuyun
Format Journal Article
LanguageEnglish
Published Switzerland Frontiers Media S.A 16.05.2017
Subjects
antibiotics
bioremediation
expression regulation
laccase
Microbiology
PPCPs
production
bioremediation
PPCPs
production
antibiotics
expression regulation
laccase
Online AccessGet full text

Cover

Abstract Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, , and included a discussion with regards to regulation of laccase expression.
AbstractList Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, Cerrena, and included a discussion with regards to regulation of laccase expression.
Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, Cerrena , and included a discussion with regards to regulation of laccase expression.
Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas. There have been over two dozen reviews on laccases since 2010 covering various aspects of this group of versatile enzymes, from their occurrence, biochemical properties, and expression to immobilization and applications. This review is not intended to be all-encompassing; instead, we highlighted some of the latest developments in basic and applied laccase research with an emphasis on laccase-mediated bioremediation of pharmaceuticals, especially antibiotics. Pharmaceuticals are a broad class of emerging organic contaminants that are recalcitrant and prevalent. The recent surge in the relevant literature justifies a short review on the topic. Since low laccase yields in natural and genetically modified hosts constitute a bottleneck to industrial-scale applications, we also accentuated a genus of laccase-producing white-rot fungi, , and included a discussion with regards to regulation of laccase expression.
Author Lin, Juan
Deng, Xiangzhen
Yang, Jie
Ye, Xiuyun
Li, Wenjuan
Ng, Tzi Bun
AuthorAffiliation 1 Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University Fujian, China
2 Faculty of Medicine, School of Biomedical Sciences, The Chinese University of Hong Kong Shatin, Hong Kong
AuthorAffiliation_xml – name: 1 Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou University Fujian, China
– name: 2 Faculty of Medicine, School of Biomedical Sciences, The Chinese University of Hong Kong Shatin, Hong Kong
Author_xml – sequence: 1
  givenname: Jie
  surname: Yang
  fullname: Yang, Jie
  organization: Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou UniversityFujian, China
– sequence: 2
  givenname: Wenjuan
  surname: Li
  fullname: Li, Wenjuan
  organization: Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou UniversityFujian, China
– sequence: 3
  givenname: Tzi Bun
  surname: Ng
  fullname: Ng, Tzi Bun
  organization: Faculty of Medicine, School of Biomedical Sciences, The Chinese University of Hong KongShatin, Hong Kong
– sequence: 4
  givenname: Xiangzhen
  surname: Deng
  fullname: Deng, Xiangzhen
  organization: Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou UniversityFujian, China
– sequence: 5
  givenname: Juan
  surname: Lin
  fullname: Lin, Juan
  organization: Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou UniversityFujian, China
– sequence: 6
  givenname: Xiuyun
  surname: Ye
  fullname: Ye, Xiuyun
  organization: Fujian Key Laboratory of Marine Enzyme Engineering, Fuzhou UniversityFujian, China
BackLink https://www.ncbi.nlm.nih.gov/pubmed/28559880$$D View this record in MEDLINE/PubMed
BookMark eNpVkUFv1DAQhS1UREvpnRPKkQO72GM7G3NAKlWBSitRIZA4YU3syTZVEgc7Qe2_x82WqvXBHj2_-TzWe8kOhjAQY68FX0tZmfdN37p6DVxs1pxXEp6xI1GWaiU5_Dp4VB-yk5SueV6KQ95fsEOotDZVxY_Y7y06h4nSh-IyBj-7qQ3Du-L8ZoyUUq6L77SbO9zLOPjidBy71i1CKtqhuLzC2KOjecpqV3xqg6ddRL84XrHnDXaJTu7PY_bz8_mPs6-r7bcvF2en25VTJUyrRpNxYlM5J8BLFPlP0nAEhd4rI_2mrngFNRfKOao3EjyCriSV3vBaoZPH7GLP9QGv7RjbHuOtDdjaRQhxZzHmATuy0GiFygujnVbQoCkNOekAyAgApMz6uGeNc92TdzRMEbsn0Kc3Q3tld-Gv1UqC1jwD3t4DYvgzU5ps3yZHXYcDhTlZYbgCqQXobOV7q4shpUjNwzOC27uU7ZKyvUvZLinnljePx3to-J-p_AdKK6dF
CitedBy_id crossref_primary_10_1007_s00253_018_9469_4
crossref_primary_10_1016_j_scitotenv_2018_03_366
crossref_primary_10_3390_app10093152
crossref_primary_10_1038_s41598_018_33435_6
crossref_primary_10_1007_s43393_023_00163_6
crossref_primary_10_1021_acsami_1c14663
crossref_primary_10_1007_s42535_022_00480_6
crossref_primary_10_1021_acs_est_1c08042
crossref_primary_10_3389_fbioe_2019_00165
crossref_primary_10_1186_s13068_019_1596_3
crossref_primary_10_1007_s13205_022_03404_y
crossref_primary_10_1039_D3NR01625K
crossref_primary_10_1016_j_enzmictec_2023_110308
crossref_primary_10_1007_s00253_022_12087_7
crossref_primary_10_1186_s12896_021_00698_3
crossref_primary_10_3390_pr10101968
crossref_primary_10_1007_s11356_020_11078_3
crossref_primary_10_1186_s13568_020_01118_z
crossref_primary_10_1016_j_envres_2021_110878
crossref_primary_10_1088_1755_1315_471_1_012012
crossref_primary_10_3389_fmicb_2023_1078382
crossref_primary_10_1038_s41598_021_98979_6
crossref_primary_10_1016_j_scitotenv_2023_169598
crossref_primary_10_3390_w14244068
crossref_primary_10_3390_molecules26133813
crossref_primary_10_3390_w15122262
crossref_primary_10_1016_j_envres_2022_112882
crossref_primary_10_1093_jimb_kuad014
crossref_primary_10_3389_fphys_2020_591569
crossref_primary_10_1007_s10123_018_00045_1
crossref_primary_10_3390_microorganisms7120665
crossref_primary_10_1007_s11356_021_13578_2
crossref_primary_10_3389_fbioe_2020_00222
crossref_primary_10_1093_femsle_fnac124
crossref_primary_10_3390_w15213770
crossref_primary_10_1007_s42452_020_2832_y
crossref_primary_10_3390_foods13040566
crossref_primary_10_1016_j_scitotenv_2018_04_051
crossref_primary_10_1039_D0CY00724B
crossref_primary_10_1016_j_enzmictec_2020_109694
crossref_primary_10_1002_cbic_202000775
crossref_primary_10_1007_s12192_018_0874_5
crossref_primary_10_3390_molecules26216556
crossref_primary_10_1007_s00253_018_9404_8
crossref_primary_10_3389_fbioe_2023_1264135
crossref_primary_10_1080_07388551_2021_1895053
crossref_primary_10_1007_s10562_022_04134_9
crossref_primary_10_1007_s43393_024_00246_y
crossref_primary_10_1007_s11356_021_13283_0
crossref_primary_10_1007_s00449_021_02638_z
crossref_primary_10_1016_j_cep_2020_108237
crossref_primary_10_1016_j_chemosphere_2023_138392
crossref_primary_10_1016_j_jhazmat_2021_125520
crossref_primary_10_1093_femsec_fiz186
crossref_primary_10_1016_j_funbio_2022_11_005
crossref_primary_10_1016_j_ecoenv_2023_115202
crossref_primary_10_1007_s12033_021_00396_7
crossref_primary_10_3390_microorganisms7110527
crossref_primary_10_1016_j_jhazmat_2020_124632
crossref_primary_10_1016_j_biortech_2019_121655
crossref_primary_10_1007_s42770_024_01247_8
crossref_primary_10_1016_j_ijbiomac_2018_04_079
crossref_primary_10_1007_s00253_022_12311_4
crossref_primary_10_1007_s10311_020_01081_y
crossref_primary_10_1007_s13399_022_03192_8
crossref_primary_10_3390_catal10040459
crossref_primary_10_2174_1389203720666191011105624
crossref_primary_10_1021_acs_langmuir_3c00362
crossref_primary_10_3390_biom14030369
crossref_primary_10_3390_catal8060223
crossref_primary_10_1016_j_dyepig_2020_108749
crossref_primary_10_1016_j_ijbiomac_2019_05_168
crossref_primary_10_1016_j_biotechadv_2021_107809
crossref_primary_10_1080_10408398_2020_1848788
crossref_primary_10_1038_s41598_019_45118_x
crossref_primary_10_1002_pol_20200647
crossref_primary_10_1016_j_jpba_2019_04_030
crossref_primary_10_1016_j_watres_2021_117861
crossref_primary_10_1016_j_biteb_2021_100723
crossref_primary_10_1128_AEM_00055_21
crossref_primary_10_3390_pr10102004
crossref_primary_10_1002_jobm_201900084
crossref_primary_10_1186_s13068_021_01937_7
crossref_primary_10_1007_s11274_020_02941_z
crossref_primary_10_1007_s00449_019_02160_3
crossref_primary_10_1038_s41598_022_06111_z
crossref_primary_10_3390_life14020230
crossref_primary_10_3390_catal9121023
crossref_primary_10_3390_molecules29050989
crossref_primary_10_1007_s00203_022_03170_8
crossref_primary_10_1021_acs_est_1c05803
crossref_primary_10_1021_acs_jpclett_2c03126
crossref_primary_10_1016_j_ram_2020_04_007
crossref_primary_10_3390_molecules27051581
crossref_primary_10_1016_j_funbio_2018_02_006
crossref_primary_10_1186_s40643_021_00484_1
crossref_primary_10_3390_su14020935
crossref_primary_10_1007_s12033_020_00281_9
crossref_primary_10_1016_j_enzmictec_2019_109507
crossref_primary_10_1186_s12864_023_09606_9
crossref_primary_10_1128_spectrum_03405_23
crossref_primary_10_1016_j_jenvman_2020_111087
crossref_primary_10_1016_j_ijbiomac_2023_124658
crossref_primary_10_3390_microorganisms8030369
crossref_primary_10_1007_s10532_021_09933_2
crossref_primary_10_1016_j_desal_2022_116198
crossref_primary_10_1016_j_jhazmat_2021_127123
crossref_primary_10_2166_wqrj_2023_003
crossref_primary_10_1007_s12010_019_03141_8
crossref_primary_10_1002_pi_6127
crossref_primary_10_1016_j_ijbiomac_2024_131109
crossref_primary_10_1038_s41598_017_16771_x
crossref_primary_10_1002_ajoc_202200564
crossref_primary_10_1016_j_scitotenv_2019_01_322
crossref_primary_10_1016_j_tibtech_2018_01_011
crossref_primary_10_3389_fmicb_2021_682679
crossref_primary_10_3390_jof9030308
crossref_primary_10_1007_s11274_020_02942_y
crossref_primary_10_1080_01490451_2022_2032883
crossref_primary_10_1186_s12934_024_02443_9
crossref_primary_10_3389_fmicb_2021_802544
crossref_primary_10_3390_jof7100835
crossref_primary_10_3390_microorganisms7080264
crossref_primary_10_1007_s00253_018_9543_y
crossref_primary_10_1016_j_jhazmat_2022_129674
crossref_primary_10_3390_antibiotics12030440
crossref_primary_10_3390_biom13121716
crossref_primary_10_1016_j_enzmictec_2023_110331
crossref_primary_10_1186_s13568_024_01668_6
crossref_primary_10_3390_molecules27144436
crossref_primary_10_1016_j_jtice_2017_12_028
crossref_primary_10_3389_fmicb_2022_878360
crossref_primary_10_1016_j_scitotenv_2024_170498
crossref_primary_10_1016_j_tifs_2021_06_052
crossref_primary_10_1021_acs_biomac_3c00202
crossref_primary_10_3389_fbioe_2021_710035
crossref_primary_10_3390_jof6040340
crossref_primary_10_1080_10643389_2023_2224612
crossref_primary_10_1007_s00018_021_03793_y
crossref_primary_10_1080_10242422_2020_1856820
crossref_primary_10_1016_j_chemosphere_2022_135685
crossref_primary_10_1007_s00396_021_04867_w
crossref_primary_10_1021_acs_est_9b02219
crossref_primary_10_1016_j_hazadv_2024_100410
crossref_primary_10_3390_microorganisms8060871
crossref_primary_10_1007_s00253_023_12582_5
crossref_primary_10_1016_j_biortech_2019_02_008
crossref_primary_10_1039_D0NR00361A
crossref_primary_10_1016_j_jece_2017_12_006
crossref_primary_10_1080_09593330_2023_2219851
crossref_primary_10_1186_s40643_023_00703_x
crossref_primary_10_1007_s13399_022_03510_0
crossref_primary_10_1007_s00253_018_9227_7
crossref_primary_10_1134_S1064229322070146
crossref_primary_10_3389_fmicb_2023_1200108
crossref_primary_10_1007_s13399_020_00929_1
crossref_primary_10_3390_jof8010022
crossref_primary_10_1002_jctb_6807
crossref_primary_10_1007_s00253_019_10147_z
crossref_primary_10_3390_ijms20082008
crossref_primary_10_3389_fpls_2022_912293
crossref_primary_10_1016_j_ijbiomac_2020_11_169
crossref_primary_10_4103_bbrj_bbrj_266_23
crossref_primary_10_1002_advs_202300210
crossref_primary_10_1016_j_jhazmat_2019_121890
Cites_doi 10.4161/bbug.1.4.11438
10.1155/2015/829708
10.1007/s00449-009-0389-7
10.1016/j.jbiosc.2012.10.025
10.1016/j.chemosphere.2016.02.064
10.1016/j.jhazmat.2010.05.103
10.1021/acs.jafc.6b02187
10.1021/acs.est.6b01641
10.1016/j.biotechadv.2007.07.002
10.1007/s00253-010-2934-3
10.1074/jbc.M600577200
10.1111/j.1574-6968.2009.01619.x
10.1016/j.enzmictec.2012.10.003
10.1128/AEM.00218-12
10.3892/ol.2016.4220
10.1007/s11270-016-3064-z
10.1371/journal.pone.0147997
10.1016/j.crvi.2011.06.001
10.1016/j.watres.2009.09.058
10.1016/j.biotechadv.2012.02.013
10.1016/j.chemosphere.2013.12.059
10.1016/j.ibiod.2015.04.027
10.1016/j.enzmictec.2010.07.005
10.1016/j.chemosphere.2016.05.031
10.1007/s12010-009-8676-y
10.1155/2014/163242
10.1016/j.ab.2015.10.004
10.1007/s00018-014-1823-9
10.1016/j.biortech.2016.05.077
10.1016/j.biortech.2009.10.087
10.1186/s13068-015-0331-y
10.1128/AEM.00635-12
10.1104/pp.15.00359
10.1016/j.nbt.2012.12.004
10.3109/07388551.2014.949617
10.1016/j.jiec.2015.06.037
10.1007/s00253-002-1169-3
10.1111/febs.13224
10.1111/1751-7915.12277
10.1007/s12010-008-8279-z
10.1016/j.bej.2015.06.008
10.1038/srep35787
10.1007/s00449-015-1476-6
10.1016/j.watres.2011.11.063
10.1016/j.micres.2013.08.004
10.4061/2010/918761
10.1016/j.ibiod.2014.12.004
10.1080/10643380902945706
10.1007/s12033-015-9910-1
10.1016/j.fbr.2013.07.001
10.4014/jmb.1604.04011
10.1007/s10311-015-0516-4
10.1016/j.seppur.2015.09.072
10.1016/j.bcab.2012.03.003
10.1016/j.copbio.2015.03.006
10.1016/j.biortech.2015.10.054
10.1007/s00253-014-5810-8
10.3109/07388551.2012.725390
10.1007/s11356-016-6139-x
10.1016/j.funbio.2012.05.005
10.1016/j.ibiod.2015.11.029
10.1371/journal.pone.0025724
10.1128/AEM.07880-11
10.1016/j.watres.2010.12.027
10.1016/j.chroma.2014.09.089
10.1007/s10532-008-9237-8
10.2174/138920211795564377
10.1111/j.1742-4658.2006.05247.x
10.1016/j.biortech.2012.10.085
10.2174/1876520301205010001
10.1016/j.biortech.2016.07.094
10.1016/j.jbiotec.2009.06.011
10.1111/j.1574-4976.2005.00010.x
10.1128/AEM.67.5.2088-2094.2001
10.1016/j.jtice.2014.03.021
10.1016/j.biortech.2014.03.116
10.1093/protein/gzs082
10.1016/j.biortech.2017.01.064
10.1016/j.molcatb.2016.07.015
10.1016/j.scitotenv.2013.10.004
10.1007/s00018-014-1822-x
10.1016/j.jhazmat.2012.02.008
10.1002/jobm.200900155
10.1007/s00253-012-3980-9
10.1007/s11157-015-9364-8
10.1039/c3ra46014b
10.1007/s00253-006-0430-6
10.1007/s00294-006-0074-1
10.1016/j.jbiotec.2015.06.401
10.1007/s11356-015-4248-6
10.1007/s00018-014-1825-7
10.13346/j.mycosystema.130231
10.1007/s00253-014-6177-6
10.1007/s00253-005-0015-9
10.1016/j.jhazmat.2009.10.133
10.1016/j.biortech.2012.01.172
10.3389/fmicb.2016.00707
10.1007/s10295-008-0471-1
10.1016/j.tibtech.2014.12.007
10.1007/s00253-004-1663-x
10.1016/j.crvi.2014.12.001
10.1016/j.scitotenv.2014.08.116
10.1016/j.tibtech.2013.04.002
10.1007/s00253-005-0128-1
10.1016/j.gene.2014.09.028
10.3390/toxins8090245
10.1016/j.enzmictec.2005.07.005
10.1007/s12257-015-0278-7
10.1016/j.cej.2014.06.060
10.1016/j.jhazmat.2009.11.112
10.1016/j.bbrc.2015.11.096
10.1016/j.biortech.2011.12.111
10.1021/es202272w
10.1016/j.ibiod.2016.03.004
10.1016/j.tibtech.2011.04.005
10.1186/s13568-015-0151-2
10.1007/s00253-014-6219-0
10.1016/j.biotechadv.2011.05.013
10.1080/09593330.2015.1069897
10.1016/j.bej.2010.06.005
10.1016/j.chemosphere.2008.10.040
10.1186/1475-2859-10-78
10.1016/j.ibmb.2010.02.006
10.1016/j.scitotenv.2014.04.009
10.1007/s12010-012-9769-6
10.1002/jpln.200390023
10.1074/jbc.M300861200
10.1080/10826068.2010.488967
10.1016/j.biortech.2016.08.004
10.1016/j.molcatb.2014.06.006
10.1016/j.nbt.2013.06.004
10.1016/j.biortech.2011.10.041
10.1007/s10532-010-9426-0
10.1007/s10482-013-9883-7
10.1080/19443994.2015.1063462
10.1016/j.biotechadv.2013.04.005
10.1093/jxb/erl022
10.1016/j.ijbiomac.2016.10.079
10.1039/C4EM00627E
10.1016/j.biotechadv.2010.05.002
10.3390/ijms161226111
10.1186/2191-0855-3-63
10.1016/j.enzmictec.2007.03.003
10.1016/j.ibiod.2015.12.003
10.1007/s00284-010-9794-z
10.1016/j.watres.2015.01.012
10.1002/btpr.2173
10.1016/j.biortech.2016.01.014
10.1016/j.enzmictec.2016.03.001
10.1007/s00284-006-0068-8
10.1007/s11274-016-2032-5
10.3109/10242422.2012.646032
10.1016/j.ibiod.2016.04.027
10.1186/s13068-015-0235-x
10.1016/j.jhazmat.2010.01.005
10.1016/j.biortech.2012.09.039
10.1016/j.biortech.2013.08.032
10.1186/s13568-015-0173-9
10.4061/2011/376015
10.2174/138920211795564331
10.1016/j.jenvman.2016.04.008
10.1016/j.biochi.2015.07.015
10.1016/j.biortech.2013.01.173
10.1016/j.ecoleng.2014.11.039
10.1016/j.jmgm.2013.04.011
10.1016/j.memsci.2014.11.044
10.3109/03009734.2014.896438
10.1007/s00018-014-1824-8
10.1016/j.gene.2015.03.020
10.1016/j.cattod.2014.02.051
10.1007/s00253-013-4797-x
10.3109/07388551.2012.694409
10.1016/j.molcatb.2013.12.016
10.1002/adsc.201300960
10.1039/c0em00068j
10.1002/elsc.200700017
10.1111/j.1469-8137.2009.02774.x
10.1016/j.biortech.2016.08.088
10.1134/S0003683807050055
10.1016/j.jhazmat.2016.10.019
10.1016/j.scitotenv.2014.06.035
10.1002/bab.1026
10.1615/IntJMedMushr.v15.i2.90
10.1007/s11274-007-9390-y
10.1038/srep34309
10.1016/j.cej.2014.09.072
10.1016/j.jbiotec.2009.06.020
10.1039/c3ra40818c
10.1016/j.jbiotec.2014.06.027
10.1016/j.jhazmat.2014.08.062
10.1371/journal.pone.0058294
10.2166/wst.2013.684
10.1016/j.ijbiomac.2016.10.037
10.1016/j.dib.2016.01.029
10.1007/s00253-015-7113-0
10.1002/bit.10297
10.1016/j.micres.2015.06.005
10.1128/AEM.70.11.6379-6384.2004
10.1002/cctc.201200611
10.1016/j.chemosphere.2009.01.052
10.1016/j.biotechadv.2014.12.007
10.3389/fmicb.2015.01558
10.1371/journal.pone.0079307
10.1016/j.biortech.2010.09.080
10.1002/jobm.200900382
10.1016/j.memsci.2016.08.056
10.1186/s40201-016-0248-9
10.1111/1751-7915.12422
10.1080/19443994.2013.877851
10.1016/j.jbiotec.2016.02.029
10.1126/science.1221748
10.1016/j.chemosphere.2016.01.019
10.1016/j.molcatb.2010.11.002
10.1007/s11356-016-7003-8
10.1016/j.jtice.2016.04.025
10.1016/j.tibtech.2009.11.001
10.1016/j.funbio.2012.11.005
10.1016/j.enzmictec.2010.11.007
10.1007/s00253-011-3554-2
10.1016/j.scitotenv.2014.01.132
10.1016/j.biortech.2013.02.093
10.2965/jwet.2010.125
10.1007/s00294-003-0452-x
10.1371/journal.pone.0065633
10.1007/s11356-015-4893-9
10.1007/s13205-015-0316-3
10.1371/journal.pone.0093912
10.1016/j.jhazmat.2012.02.056
10.1007/s00294-014-0460-z
10.1007/s10295-010-0757-y
10.1016/j.eti.2016.04.001
10.1016/j.fbr.2016.06.003
10.1080/09593330.2014.931468
10.1016/j.jenvman.2016.07.049
10.1016/j.enzmictec.2016.04.004
10.1016/j.ibiod.2014.10.018
10.1016/j.jhazmat.2016.05.064
10.1371/journal.pone.0073282
10.1016/j.chemosphere.2008.11.086
10.1093/femsle/fnv072
10.1016/S0032-9592(02)00023-7
10.1007/s00018-009-0169-1
10.1111/j.1365-2672.2008.03998.x
10.1016/j.jbiotec.2011.11.021
10.1016/j.chemosphere.2014.05.072
10.1016/j.ibiod.2014.05.017
10.3390/molecules21081017
10.1016/j.gene.2014.09.018
10.1016/j.jhazmat.2014.06.070
10.1007/s11270-015-2514-3
10.1016/j.memsci.2015.12.043
10.1007/s00425-006-0300-6
10.1016/j.ibiod.2013.12.017
10.1371/journal.pone.0127714
10.1111/j.1751-7915.2011.00273.x
10.1016/j.ijbiomac.2015.05.015
10.1016/j.chemosphere.2016.01.022
10.1007/S10267-009-0002-6
10.1016/j.biortech.2015.09.100
10.1021/es3044592
10.1016/j.jenvman.2016.05.035
10.1007/S10267-011-0122-7
10.1007/s11274-014-1624-1
10.1007/s12257-012-0125-z
10.1016/j.ibiod.2016.03.017
10.1016/j.biortech.2013.08.113
10.1007/s00253-016-7288-z
10.1016/j.biortech.2014.05.125
10.1016/j.bej.2012.05.010
10.1016/j.jhazmat.2015.12.062
10.1002/prot.24575
10.1007/s00018-014-1826-6
10.1007/s11157-011-9257-4
10.1007/s00425-010-1298-3
10.1016/j.chemosphere.2009.10.009
10.1023/A:1026070122451
10.1007/s00253-005-0188-2
ContentType Journal Article
Copyright Copyright © 2017 Yang, Li, Ng, Deng, Lin and Ye. 2017 Yang, Li, Ng, Deng, Lin and Ye
Copyright_xml – notice: Copyright © 2017 Yang, Li, Ng, Deng, Lin and Ye. 2017 Yang, Li, Ng, Deng, Lin and Ye
DBID NPM
AAYXX
CITATION
7X8
5PM
DOA
DOI 10.3389/fmicb.2017.00832
DatabaseName PubMed
CrossRef
MEDLINE - Academic
PubMed Central (Full Participant titles)
Directory of Open Access Journals
DatabaseTitle PubMed
CrossRef
MEDLINE - Academic
DatabaseTitleList

MEDLINE - Academic
PubMed
Database_xml – sequence: 1
  dbid: DOA
  name: Directory of Open Access Journals
  url: https://www.doaj.org/
  sourceTypes: Open Website
– sequence: 2
  dbid: NPM
  name: PubMed
  url: https://proxy.k.utb.cz/login?url=http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?db=PubMed
  sourceTypes: Index Database
DeliveryMethod fulltext_linktorsrc
Discipline Biology
EISSN 1664-302X
EndPage 832
ExternalDocumentID oai_doaj_org_article_2f54a4d195c542fa969ec3c22e9122ae
10_3389_fmicb_2017_00832
28559880
Genre Journal Article
Review
GrantInformation_xml – fundername: National Natural Science Foundation of China
  grantid: 31671795
GroupedDBID 53G
5VS
9T4
AAFWJ
AAKDD
ACGFO
ACGFS
ACXDI
ADBBV
ADRAZ
AENEX
ALMA_UNASSIGNED_HOLDINGS
AOIJS
BAWUL
BCNDV
DIK
ECGQY
GROUPED_DOAJ
GX1
HYE
IAO
IEA
IHR
IPNFZ
KQ8
M48
M~E
NPM
O5R
O5S
OK1
PGMZT
RIG
RNS
RPM
AAYXX
AFPKN
CITATION
7X8
5PM
ID FETCH-LOGICAL-c462t-f5e9c178cc12d3a1017390a24add493d7b8082b014cceb732da2583e6d90b4ac3
IEDL.DBID RPM
ISSN 1664-302X
IngestDate Tue Oct 22 15:13:16 EDT 2024
Tue Sep 17 21:13:40 EDT 2024
Sat Oct 26 01:15:22 EDT 2024
Thu Sep 26 17:10:04 EDT 2024
Tue Oct 15 23:55:55 EDT 2024
IsDoiOpenAccess true
IsOpenAccess true
IsPeerReviewed true
IsScholarly true
Keywords bioremediation
PPCPs
production
antibiotics
expression regulation
laccase
Language English
License This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) or licensor are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.
LinkModel DirectLink
MergedId FETCHMERGED-LOGICAL-c462t-f5e9c178cc12d3a1017390a24add493d7b8082b014cceb732da2583e6d90b4ac3
Notes ObjectType-Article-2
SourceType-Scholarly Journals-1
ObjectType-Feature-3
content type line 23
ObjectType-Review-1
Edited by: Octavio Luiz Franco, Universidade Católica de Brasília, Brazil
Reviewed by: Susana Rodriguez-Couto, Ikerbasque, Spain; Gerardo Díaz-Godínez, Autonomous University of Tlaxcala, Mexico
This article was submitted to Antimicrobials, Resistance and Chemotherapy, a section of the journal Frontiers in Microbiology
OpenAccessLink https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5432550/
PMID 28559880
PQID 1904235125
PQPubID 23479
PageCount 1
ParticipantIDs doaj_primary_oai_doaj_org_article_2f54a4d195c542fa969ec3c22e9122ae
pubmedcentral_primary_oai_pubmedcentral_nih_gov_5432550
proquest_miscellaneous_1904235125
crossref_primary_10_3389_fmicb_2017_00832
pubmed_primary_28559880
PublicationCentury 2000
PublicationDate 2017-05-16
PublicationDateYYYYMMDD 2017-05-16
PublicationDate_xml – month: 05
  year: 2017
  text: 2017-05-16
  day: 16
PublicationDecade 2010
PublicationPlace Switzerland
PublicationPlace_xml – name: Switzerland
PublicationTitle Frontiers in microbiology
PublicationTitleAlternate Front Microbiol
PublicationYear 2017
Publisher Frontiers Media S.A
Publisher_xml – name: Frontiers Media S.A
References 26698313 - Mol Biotechnol. 2016 Feb;58(2):93-116
26399693 - Biotechnol Prog. 2015 Nov-Dec;31(6):1443-63
23340718 - Antonie Van Leeuwenhoek. 2013 May;103(5):1029-39
22398306 - Biotechnol Adv. 2013 Dec;31(8):1808-25
26104901 - Environ Sci Pollut Res Int. 2015 Nov;22(21):16868-74
18830647 - J Ind Microbiol Biotechnol. 2009 Jan;36(1):45-51
26476168 - Bioresour Technol. 2016 Jan;200:81-9
26631965 - Biochem Biophys Res Commun. 2016 Jan 8;469(2):306-12
25739840 - Environ Sci Pollut Res Int. 2016 Mar;23 (5):4024-35
19459959 - FEMS Microbiol Lett. 2009 Jul;296(1):84-90
27521787 - Bioresour Technol. 2016 Nov;219:500-9
23332833 - Fungal Biol. 2013 Jan;117(1):52-61
26921914 - Chemosphere. 2016 May;150:559-65
25577278 - Cell Mol Life Sci. 2015 Mar;72(5):923-40
24867811 - Sci Total Environ. 2014 Jul 15;487:748-55
27552641 - J Environ Manage. 2016 Nov 1;182:620-40
23069616 - Bioresour Technol. 2012 Dec;125:344-7
19513857 - Appl Biochem Biotechnol. 2010 Mar;160(6):1760-88
22257859 - Bioresour Technol. 2012 Jun;113:259-64
14600788 - Curr Genet. 2004 Feb;45(1):9-18
23639526 - Trends Biotechnol. 2013 Jun;31(6):335-41
12578838 - J Biol Chem. 2003 Apr 18;278(16):14565-77
25649492 - FEBS J. 2015 Apr;282(7):1190-213
24589758 - Sci Total Environ. 2014 May 15;481:90-9
26165135 - Environ Technol. 2016;37(3):335-43
23474614 - Appl Microbiol Biotechnol. 2013 Apr;97(8):3293-300
16650005 - FEBS J. 2006 May;273(10):2308-26
21048873 - Enzyme Res. 2010 Sep 30;2010:918761
26849129 - PLoS One. 2016 Feb 05;11(2):e0147997
15528495 - Appl Environ Microbiol. 2004 Nov;70(11):6379-84
12664149 - Appl Microbiol Biotechnol. 2003 Feb;60(6):700-7
27242729 - Front Microbiol. 2016 May 18;7:707
27272922 - Environ Sci Pollut Res Int. 2016 Sep;23 (17 ):16904-25
23557372 - Int J Med Mushrooms. 2013;15(2):199-210
25572294 - Cell Mol Life Sci. 2015 Mar;72(5):911-22
27775052 - Sci Rep. 2016 Oct 24;6:35787
23199732 - Enzyme Microb Technol. 2013 Jan 10;52(1):1-12
25407463 - Curr Genet. 2015 May;61(2):127-40
27696775 - Microb Biotechnol. 2016 Oct 3;:null
19112598 - Biodegradation. 2009 Jul;20(4):441-66
26874626 - Chemosphere. 2016 Apr;149:373-82
25926529 - FEMS Microbiol Lett. 2015 Jun;362(11):null
25573330 - C R Biol. 2015 Feb;338(2):121-5
24411841 - Chemosphere. 2014 Jul;107:145-62
25244136 - Environ Technol. 2014 Nov-Dec;35(21-24):3082-91
11319086 - Appl Environ Microbiol. 2001 May;67(5):2088-94
20471466 - Biotechnol Adv. 2010 Nov-Dec;28(6):694-705
23586863 - Biotechnol Appl Biochem. 2012 Jul-Aug;59(4):295-306
19945218 - J Hazard Mater. 2010 Apr 15;176(1-3):1089-92
25776201 - Gene. 2015 Jun 1;563(2):142-9
26955647 - Data Brief. 2016 Jan 29;7:1-7
24710109 - PLoS One. 2014 Apr 07;9(4):e93912
27679939 - Sci Rep. 2016 Sep 29;6:34309
19539671 - J Biotechnol. 2009 Aug 10;143(1):69-78
19882175 - Bioprocess Biosyst Eng. 2010 Jun;33(5):639-46
22112763 - Enzyme Microb Technol. 2011 Jan 5;48(1):1-6
25217998 - Sci Total Environ. 2014 Dec 1;500-501:235-42
22733235 - Appl Biochem Biotechnol. 2012 Sep;168(2):256-65
19062071 - Chemosphere. 2009 Feb;74(6):765-72
26924241 - J Biotechnol. 2016 Apr 10;223:42-9
22178304 - Water Res. 2012 Mar 15;46(4):955-64
23081836 - Protein Eng Des Sel. 2012 Nov;25(11):761-9
14574106 - Antonie Van Leeuwenhoek. 2003;84(4):289-99
23499178 - Bioresour Technol. 2013 Aug;141:97-108
24244475 - PLoS One. 2013 Nov 11;8(11):e79307
27231878 - Chemosphere. 2016 Aug;157:200-7
25545886 - Biotechnol Adv. 2015 Jan-Feb;33(1):25-40
23384282 - Environ Sci Technol. 2013 Jul 2;47(13):6916-24
22078734 - C R Biol. 2011 Nov;334(11):781-8
15480638 - Appl Microbiol Biotechnol. 2004 Dec;66(2):194-9
26780358 - Appl Microbiol Biotechnol. 2016 Jun;100(11):4885-99
26475566 - Anal Biochem. 2016 Jan 15;493:27-9
27591519 - Bioresour Technol. 2016 Nov;220:333-40
25198436 - Crit Rev Biotechnol. 2016;36(1):70-86
20082372 - J Basic Microbiol. 2010 Feb;50(1):98-103
27563923 - Toxins (Basel). 2016 Aug 23;8(9):null
26514808 - Plant Physiol. 2015 Dec;169(4):2391-408
18581264 - Appl Biochem Biotechnol. 2009 May;157(2):174-209
26411895 - Microbiol Res. 2015 Oct;179:54-63
16804053 - J Exp Bot. 2006;57(11):2563-9
27240236 - Bioresour Technol. 2016 Sep;216:203-10
23196221 - Bioresour Technol. 2013 Jan;128:49-57
23623853 - Biotechnol Adv. 2013 Nov;31(6):838-50
22022440 - PLoS One. 2011;6(10):e25724
24785303 - Sci Total Environ. 2014 Jul 15;487:830-9
26003302 - Int J Biol Macromol. 2015 Aug;79:459-68
21966248 - Curr Genomics. 2011 Apr;12(2):104-12
19243515 - New Phytol. 2009;182(3):736-50
26497303 - Bioprocess Biosyst Eng. 2016 Jan;39(1):1-36
23992799 - Bioresour Technol. 2013 Oct;146:807-11
24034986 - Bioresour Technol. 2013 Nov;147:667-71
24710963 - Proteins. 2014 Jun;82(6):887-96
25441070 - J Chromatogr A. 2014 Nov 21;1369:43-51
24984233 - Sci Total Environ. 2014 Sep 15;493:626-31
21981827 - Microb Cell Fact. 2011 Oct 08;10:78
23732301 - J Mol Graph Model. 2013 Jul;44:1-8
26536880 - Appl Microbiol Biotechnol. 2016 Mar;100(5):2381-99
20532947 - J Ind Microbiol Biotechnol. 2010 Oct;37(10):1091-6
22745431 - Science. 2012 Jun 29;336(6089):1715-9
25359481 - Appl Microbiol Biotechnol. 2014 Dec;98(24):9931-52
22260423 - Environ Sci Technol. 2012 Feb 21;46(4):2102-11
21237478 - Water Res. 2011 Feb;45(5):1921-32
21791030 - Microb Biotechnol. 2012 May;5(3):318-32
27776862 - J Hazard Mater. 2017 Jan 15;322(Pt B):525-531
20619797 - J Hazard Mater. 2010 Sep 15;181(1-3):1175-8
23526973 - PLoS One. 2013;8(3):e58294
24055313 - Microbiol Res. 2014 May-Jun;169(5-6):453-62
25600621 - Trends Biotechnol. 2015 Mar;33(3):155-62
21624453 - Biotechnol Adv. 2012 Sep-Oct;30(5):933-53
26196690 - Biochimie. 2015 Sep;116:154-64
19844659 - Cell Mol Life Sci. 2010 Feb;67(3):369-85
25655319 - Water Res. 2015 Apr 15;73:118-31
19854464 - Water Res. 2010 Jan;44(1):298-308
20938541 - J Environ Monit. 2010 Nov;12(11):1956-78
19913277 - Chemosphere. 2010 Jan;78(4):474-81
25572295 - Cell Mol Life Sci. 2015 Mar;72(5):869-83
26886217 - World J Microbiol Biotechnol. 2016 Mar;32(3):52
26793186 - Front Microbiol. 2016 Jan 12;6:1558
20972884 - Biodegradation. 2011 Jun;22(3):539-50
26826938 - J Hazard Mater. 2016 Apr 15;307:350-8
22706050 - Appl Environ Microbiol. 2012 Aug;78(16):5845-54
24959348 - Enzyme Res. 2014;2014:163242
25234727 - Gene. 2014 Nov 15;552(1):146-54
21046396 - Curr Microbiol. 2011 Mar;62(3):871-5
22377476 - Bioresour Technol. 2012 May;111:36-41
27475331 - Bioresour Technol. 2016 Nov;219:53-63
26695948 - AMB Express. 2015 Dec;5(1):81
27085152 - J Environ Manage. 2016 Jul 15;177:93-100
19232429 - Chemosphere. 2009 May;75(8):1003-7
16779554 - Planta. 2006 Oct;224(5):1185-96
25824278 - Microb Biotechnol. 2015 Nov;8(6):918-29
27241287 - Enzyme Microb Technol. 2016 Aug;90:1-18
26784443 - Chemosphere. 2016 Apr;148:1-7
24535613 - World J Microbiol Biotechnol. 2014 Jul;30(7):2005-13
26803903 - Bioresour Technol. 2016 Jun;210:108-16
19963293 - Trends Biotechnol. 2010 Feb;28(2):63-72
16283298 - Appl Microbiol Biotechnol. 2006 Jul;71(4):493-501
27414990 - Environ Sci Technol. 2016 Aug 16;50(16):8799-808
27262275 - J Hazard Mater. 2016 Nov 5;317:81-9
22862916 - Fungal Biol. 2012 Aug;116(8):883-9
19120619 - J Appl Microbiol. 2009 Jan;106(1):249-57
12115407 - Biotechnol Bioeng. 2002 Aug 20;79(4):438-49
25218263 - J Hazard Mater. 2014 Sep 15;280:662-70
16740638 - J Biol Chem. 2006 Aug 11;281(32):22933-42
27765568 - Int J Biol Macromol. 2017 Jan;94(Pt A):535-543
25590782 - Environ Sci Process Impacts. 2015 Feb;17(2):326-42
16472305 - FEMS Microbiol Rev. 2006 Mar;30(2):215-42
27527131 - Molecules. 2016 Aug 04;21(8)
24152339 - AMB Express. 2013 Oct 24;3(1):63
24997355 - J Biotechnol. 2014 Dec 10;191:214-20
24972175 - Chemosphere. 2015 Jan;119:90-8
21887507 - Appl Microbiol Biotechnol. 2011 Nov;92(3):467-77
24039902 - PLoS One. 2013 Sep 05;8(9):e73282
25586560 - Cell Mol Life Sci. 2015 Mar;72(5):897-910
28199921 - Bioresour Technol. 2017 May;231:85-93
26817474 - Environ Sci Pollut Res Int. 2016 May;23 (9):8929-39
23508144 - Water Sci Technol. 2013;67(6):1216-23
21327057 - Bioeng Bugs. 2010 Jul-Aug;1(4):252-62
19559737 - J Biotechnol. 2009 Oct 12;144(1):37-42
17706395 - Biotechnol Adv. 2007 Nov-Dec;25(6):558-69
26379777 - Biotechnol Biofuels. 2015 Sep 15;8:145
25595303 - Cell Mol Life Sci. 2015 Mar;72(5):885-96
27793681 - Int J Biol Macromol. 2017 Feb;95:920-927
23340383 - N Biotechnol. 2013 Sep 25;30(6):814-23
26998114 - Oncol Lett. 2016 Mar;11(3):2009-2018
23051065 - Crit Rev Biotechnol. 2013 Dec;33(4):404-18
24980029 - Bioresour Technol. 2014 Sep;167:169-77
26519700 - Bioresour Technol. 2016 Jan;200:477-84
23561949 - Bioresour Technol. 2013 Aug;141:152-9
22436341 - J Hazard Mater. 2012 May 15;215-216:227-32
27233048 - J Environ Manage. 2016 Sep 15;180:228-37
25064257 - J Hazard Mater. 2014 Aug 30;279:203-11
26020270 - PLoS One. 2015 May 28;10(5):e0127714
16622678 - Appl Microbiol Biotechnol. 2006 Nov;73(1):89-94
21811672 - Enzyme Res. 2011;2011:376015
28330085 - 3 Biotech. 2016 Jun;6(1):15
17334840 - Curr Microbiol. 2007 Apr;54(4):260-5
22712546 - Crit Rev Biotechnol. 2013 Sep;33(3):260-92
19948398 - Bioresour Technol. 2010 Apr;101(7):2331-50
22071243 - Bioresour Technol. 2012 Jan;103(1):498-501
24736211 - Bioresour Technol. 2014 Jun;162:45-52
27233125 - Enzyme Microb Technol. 2016 Jul;89:31-8
26113215 - J Biotechnol. 2015 Sep 10;209:76-84
22467498 - Appl Environ Microbiol. 2012 Jun;78(11):4037-45
20117880 - J Hazard Mater. 2010 May 15;177(1-3):924-8
23755261 - PLoS One. 2013 Jun 03;8(6):e65633
23200414 - J Biosci Bioeng. 2013 Apr;115(4):394-9
23831273 - N Biotechnol. 2013 Sep 25;30(6):803-13
22395908 - Appl Microbiol Biotechnol. 2013 Jan;97(2):705-17
21108128 - Prep Biochem Biotechnol. 2010;40(4):242-55
20031320 - J Hazard Mater. 2010 Apr 15;176(1-3):836-42
27499219 - J Agric Food Chem. 2016 Aug 24;64(33):6397-406
15983808 - Appl Microbiol Biotechnol. 2006 Feb;69(6):682-8
22112901 - Enzyme Microb Technol. 2011 Mar 7;48(3):195-208
22390957 - J Hazard Mater. 2012 Apr 30;213-214:347-54
27182441 - J Environ Health Sci Eng. 2016 May 13;14:7
20219675 - Insect Biochem Mol Biol. 2010 Mar;40(3):179-88
27291680 - J Microbiol Biotechnol. 2016 Sep 28;26(9):1570-8
26633374 - Int J Mol Sci. 2015 Dec 01;16(12):28498-509
25883681 - Biotechnol Bio
Pezzella (B179) 2013; 97
Hoegger (B84) 2004; 45
Yang (B270) 2012; 78
Dittmer (B52) 2010; 40
Kilaru (B105); 50
Osma (B172) 2010; 2010
Oulton (B175) 2010; 12
Kim (B107) 2014; 552
Crowe (B44) 2001; 67
Beloqui (B24) 2006; 281
Pan (B176) 2014; 162
Zhang (B276) 2010; 176
Lu (B133) 2015; 16
Onesios (B171) 2009; 20
Li (B121) 2016; 220
Janusz (B93) 2007; 23
Muraguchi (B157) 2011; 52
Forootanfar (B70) 2015; 31
Cabana (B29) 2007; 7
Yang (B269); 67
Yang (B263); 21
Yousefi-Ahmadipour (B272) 2016; 133
Nguyen (B165); 95
Becker (B23) 2016; 219
Arsenault (B10) 2011; 2011
Nishibori (B169) 2013; 115
Sinirlioglu (B216) 2013; 146
Martinkova (B142) 2016; 149
Cai (B30) 2006; 57
Gu (B77) 2014; 9
Rivera-Hoyos (B192) 2013; 27
Hofmann (B85) 2016; 100
Sakamoto (B200) 2015; 5
Wang (B245) 2017; 95
Shi (B208) 2014; 279
Xu (B256) 2014; 255
Ba (B15) 2013; 33
Liebeton (B124) 2014; 191
Rodríguez-Couto (B194) 2012; 5
Liu (B126) 2016; 157
Baldrian (B20) 2006; 30
Daâssi (B45) 2016; 110
Llorca (B129) 2015; 119
Mizerska-Dudka (B154) 2015; 79
Ding (B51) 2016; 307
Wen (B248) 2009; 75
Mikolasch (B152) 2012; 59
Larsson (B117) 2014; 119
Sun (B227) 2014; 30
Margot (B139); 3
Majeau (B134) 2010; 101
Touahar (B232) 2014; 481
Morozova (B156) 2007; 43
Marco-Urrea (B137); 176
Sun (B226) 2011; 62
Piscitelli (B180) 2011; 12
Lettera (B119) 2011; 334
Guo (B80) 2014; 493
Pollegioni (B183) 2015; 282
Antošovǎ (B6) 2016; 58
Thiele-Bruhn (B231) 2003; 166
Ausec (B14) 2011; 6
Si (B210) 2013; 128
Wu (B253) 2013; 33
Postemsky (B185) 2017; 231
Yang (B268); 141
Fang (B63) 2015; 8
Ashrafi (B13) 2015; 57
Hoegger (B83) 2006; 273
Chen (B39) 2016; 50
Hong (B87) 2007; 54
Rühl (B199) 2013; 103
Castanera (B32) 2013; 8
Singh (B212) 2011; 10
Alcalde (B4) 2015; 33
Wang (B243) 2016; 182
Chandra (B35) 2015; 17
D'Souza (B54) 2006; 38
Melo (B148) 2016; 37
Ramírez-Cavazos (B187) 2014; 108
Maqbool (B135) 2016; 23
Jelic (B94) 2012; 46
Kandasamy (B103) 2016; 7
Strong (B222) 2011; 41
Lu (B132) 2010; 51
Upadhyay (B236) 2016; 6
Librando (B123) 2013; 44
Sjaarda (B218) 2015; 8
Vasina (B239) 2015; 116
Zeng (B273) 2016; 148
Chhabra (B40) 2009; 143
Rahmani (B186) 2015; 97
Arca-Ramos (B7) 2016; 23
Debaste (B48) 2014; 52
Arimoto (B8) 2015; 5
Matuszewska (B147) 2016; 11
Otto (B174) 2015; 362
Chen (B38) 2012; 25
Sen (B204) 2016; 30
Yang (B262); 6
Abejón (B1); 156
Kajita (B102) 2004; 66
Kurniawati (B116) 2007; 41
Vasiliadou (B238) 2016; 180
Loi (B131) 2016; 8
Castanera (B33) 2012; 78
Jeon (B96) 2012; 5
Suetomi (B224) 2015; 61
Gulkowska (B78) 2012; 46
Domaradzka (B53) 2015; 14
Singh (B214) 2015; 22
Ramos (B188) 2011; 10
Xiao (B255) 2003; 60
Tran (B234) 2010; 8
Hata (B81) 2010; 181
Mate (B145) 2015; 33
Reiss (B190) 2013; 8
Yang (B260) 2016; 150
Yadav (B259) 2015; 13
Yang (B267); 7
Risso (B191) 2014; 82
Garcia (B72) 2011; 45
Asgher (B11) 2014; 101
Blánquez (B26) 2016; 32
Wong (B252) 2009; 157
del Vecchio (B49) 2012; 30
Martins (B143) 2015; 72
Migliore (B150) 2012
Si (B209) 2013; 15
Fang (B62) 2011; 89
Xu (B258) 2016; 26
Flores (B68) 2009; 106
Chang (B36) 2015; 75
Cho (B41) 2014; 552
Mikolasch (B151) 2016; 100
Nguyen (B161); 210
Hu (B88) 2009; 36
Kudanga (B110) 2011; 48
Valderrama (B237) 2003; 84
Jones (B101) 2015; 72
Nguyen (B166); 88
Balcazar-Lopez (B19) 2016; 11
Fang (B64) 2012; 111
Alves (B5) 2004; 70
Ji (B97); 520
Singh (B215) 2015; 104
Balasubramanian (B18) 2016; 6
Jeon (B95) 2013; 31
Kües (B111) 2015; 33
Mate (B146) 2016
Schwarz (B203) 2015; 2015
Rodríguez-Couto (B195) 2007; 25
Zhang (B275) 2015; 179
Courty (B43) 2009; 182
Arora (B9) 2010; 160
Nair (B159) 2013; 30
Kittl (B108) 2012; 157
Kümmerer (B115) 2009; 75
Popa (B184) 2014; 35
Rodgers (B193) 2010; 28
Marco-Urrea (B138) 2009; 74
Yang (B265) 2015; 10
Zhang (B274) 2006; 73
Maryskova (B144) 2016; 89
Santhanam (B201) 2011; 29
Huang (B89) 2016; 64
Catherine (B34) 2016; 5
Kumar (B113) 2016; 200
Sheldon (B206) 2011; 92
Lisova (B125) 2010; 50
Abejón (B2); 73
Fernández-Fernández (B66) 2013; 31
Senthivelan (B205) 2016; 21
Forootanfar (B71) 2016; 14
Giardina (B75) 2010; 67
Michniewicz (B149) 2006; 69
Wei (B247) 2010; 50
Xu (B257) 2015; 262
Kilaru (B106); 71
Pezzella (B178) 2015; 72
Singh (B213) 2015; 99
Mir-Tutusaus (B153) 2014
Ni (B168) 2013; 31
Kumar (B114) 2014; 487
Shi (B207) 2016; 317
Ji (B98); 502
Iracheta-Cárdenas (B91) 2016; 177
Mogharabi (B155) 2014; 356
Llorca (B128) 2014; 1369
Ergün (B59) 2016; 39
Hong (B86) 2002; 79
Fillat (B67) 2012; 67
Songulashvili (B220) 2012; 116
Yang (B271) 2013; 8
Coconi-Linares (B42) 2015; 209
Margot (B141); 30
Kües (B112) 2011; 12
Bao (B21) 2013; 8
Rodriguez-Rodriguez (B197) 2012
de Cazes (B46) 2015; 476
Le (B118) 2016; 216
Sun (B225) 2016; 227
Cañas (B31) 2010; 28
Songulashvili (B221) 2015; 338
Boonnorat (B27) 2016; 219
Jiang (B99) 2009; 296
Liu (B127) 2010; 33
Betancor (B25) 2013; 5
Garcia-Morales (B73) 2015; 226
Piscitelli (B181) 2010; 1
Ba (B17); 280
Suda (B223) 2012; 103
Al-Adhami (B3) 2002; 37
Liang (B122) 2006; 224
Rodríguez-Delgado (B196) 2016; 108
Zheng (B277) 2016; 110
Olajuyigbe (B170) 2017; 94
Floudas (B69) 2012; 336
Yang (B261) 2017; 322
Nguyen (B167); 200
Karaki (B104) 2016; 90
Nakade (B160) 2013; 117
Solé (B219) 2012; 78
Turlapati (B235) 2011; 233
Wang (B241) 2012; 17
Janusz (B92) 2013; 52
Demarche (B50) 2012; 30
Chang (B37) 2016; 23
Ba (B16); 487
Elisashvili (B58) 2010; 37
Eibes (B56) 2011; 22
Jin (B100) 2016; 6
Pogni (B182) 2015; 72
Nguyen (B164); 167
Li (B120) 2011; 48
Murugesan (B158) 2010; 44
Tahmasbi (B229) 2016; 108
Husain (B90) 2012; 33
de Cazes (B47) 2014; 236
Wang (B244) 2015; 8
Fernandez-Alejandre (B65) 2016; 223
Beaudoin (B22) 2003; 278
Xiao (B254) 2006; 71
Marco-Urrea (B136); 78
Weng (B251) 2013; 141
Ashe (B12) 2016; 113
Nguyen (B163) 2015; 99
Tran (B233) 2013; 147
Viswanath (B240) 2014; 2014
Yang (B264); 65
Ostadhadi-Dehkordi (B173) 2012; 125
Rao (B189) 2014; 107
Yang (B266); 493
Rogalski (B198) 2010; 40
Weng (B250) 2012; 113
Nguyen (B162); 45
Fan (B60) 2014; 169
Fang (B61) 2015; 169
Sitarz (B217) 2016; 36
Wang (B242) 2012; 168
Singh (B211) 2016; 469
Gasser (B74) 2014; 98
Wang (B246) 2015; 563
Cabana (B28) 2011; 102
Hibi (B82) 2012; 1
Talekar (B230) 2013; 3
Dwivedi (B55) 2011; 68
Grover (B76) 2013; 97
Margot (B140) 2015; 103
Pardo (B177) 2015; 72
Sathishkumar (B202) 2014; 4
Wen (B249) 2010; 177
Kudanga (B109) 2014; 98
Lloret (B130) 2010; 51
Sutar (B228) 2015; 31
Gulkowska (B79) 2013; 47
Elisashvili (B57) 2009; 144
References_xml – volume: 1
  start-page: 252
  year: 2010
  ident: B181
  article-title: Heterologous laccase production and its role in industrial applications
  publication-title: Bioeng. Bugs
  doi: 10.4161/bbug.1.4.11438
  contributor:
    fullname: Piscitelli
– volume: 2015
  start-page: 1
  year: 2015
  ident: B203
  article-title: Enzymatic transformation and bonding of sulfonamide antibiotics to model humic substances
  publication-title: J. Chem.
  doi: 10.1155/2015/829708
  contributor:
    fullname: Schwarz
– volume: 33
  start-page: 639
  year: 2010
  ident: B127
  article-title: Improvement of laccase production and its properties by low-energy ion implantation
  publication-title: Bioprocess Biosyst. Eng.
  doi: 10.1007/s00449-009-0389-7
  contributor:
    fullname: Liu
– volume: 115
  start-page: 394
  year: 2013
  ident: B169
  article-title: Comparison of laccase production levels in Pichia pastoris and Cryptococcus sp. S-2
  publication-title: J. Biosci. Bioeng.
  doi: 10.1016/j.jbiosc.2012.10.025
  contributor:
    fullname: Nishibori
– volume: 150
  start-page: 559
  year: 2016
  ident: B260
  article-title: Biodegradation of sulfonamide antibiotics in sludge
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2016.02.064
  contributor:
    fullname: Yang
– volume: 181
  start-page: 1175
  year: 2010
  ident: B81
  article-title: Elimination of carbamazepine by repeated treatment with laccase in the presence of 1-hydroxybenzotriazole
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2010.05.103
  contributor:
    fullname: Hata
– volume: 64
  start-page: 6397
  year: 2016
  ident: B89
  article-title: Rice (Oryza sativa) laccases involved in modification and detoxification of herbicides atrazine and isoproturon residues in plants
  publication-title: J. Agric. Food. Chem.
  doi: 10.1021/acs.jafc.6b02187
  contributor:
    fullname: Huang
– volume: 50
  start-page: 8799
  year: 2016
  ident: B39
  article-title: Cell surface display fungal laccase as a renewable biocatalyst for degradation of persistent micropollutants bisphenol A and sulfamethoxazole
  publication-title: Environ. Sci. Technol.
  doi: 10.1021/acs.est.6b01641
  contributor:
    fullname: Chen
– volume: 25
  start-page: 558
  year: 2007
  ident: B195
  article-title: Laccase production at reactor scale by filamentous fungi
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2007.07.002
  contributor:
    fullname: Rodríguez-Couto
– volume: 89
  start-page: 1103
  year: 2011
  ident: B62
  article-title: A bacterial laccase from marine microbial metagenome exhibiting chloride tolerance and dye decolorization ability
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-010-2934-3
  contributor:
    fullname: Fang
– volume: 281
  start-page: 22933
  year: 2006
  ident: B24
  article-title: Novel polyphenol oxidase mined from a metagenome expression library of bovine rumen: biochemical properties, structural analysis, and phylogenetic relationships
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M600577200
  contributor:
    fullname: Beloqui
– volume: 296
  start-page: 84
  year: 2009
  ident: B99
  article-title: A copper-responsive factor gene CUF1 is required for copper induction of laccase in Cryptococcus neoformans
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1111/j.1574-6968.2009.01619.x
  contributor:
    fullname: Jiang
– volume: 52
  start-page: 1
  year: 2013
  ident: B92
  article-title: Fungal laccase, manganese peroxidase and lignin peroxidase: gene expression and regulation
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2012.10.003
  contributor:
    fullname: Janusz
– volume: 78
  start-page: 5845
  year: 2012
  ident: B270
  article-title: Expression of the laccase gene from a white rot fungus in Pichia pastoris can enhance the resistance of this yeast to H2O2-mediated oxidative stress by stimulating the glutathione-based antioxidative system
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.00218-12
  contributor:
    fullname: Yang
– volume: 11
  start-page: 2009
  year: 2016
  ident: B147
  article-title: Laccase purified from Cerrena unicolor exerts antitumor activity against leukemic cells
  publication-title: Oncol. Lett.
  doi: 10.3892/ol.2016.4220
  contributor:
    fullname: Matuszewska
– volume: 227
  start-page: 358
  year: 2016
  ident: B225
  article-title: Laccase-catalyzed oxidative coupling reaction of triclosan in aqueous solution
  publication-title: Water Air Soil Pollut.
  doi: 10.1007/s11270-016-3064-z
  contributor:
    fullname: Sun
– volume: 11
  start-page: e0147997
  year: 2016
  ident: B19
  article-title: Xenobiotic compounds degradation by heterologous expression of a Trametes sanguineus laccase in Trichoderma atroviride
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0147997
  contributor:
    fullname: Balcazar-Lopez
– volume: 334
  start-page: 781
  year: 2011
  ident: B119
  article-title: Low impact strategies to improve ligninolytic enzyme production in filamentous fungi: the case of laccase in Pleurotus ostreatus
  publication-title: C. R. Biol.
  doi: 10.1016/j.crvi.2011.06.001
  contributor:
    fullname: Lettera
– volume: 44
  start-page: 298
  year: 2010
  ident: B158
  article-title: Enhanced transformation of triclosan by laccase in the presence of redox mediators
  publication-title: Water Res.
  doi: 10.1016/j.watres.2009.09.058
  contributor:
    fullname: Murugesan
– volume: 31
  start-page: 1808
  year: 2013
  ident: B66
  article-title: Recent developments and applications of immobilized laccase
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2012.02.013
  contributor:
    fullname: Fernández-Fernández
– volume: 107
  start-page: 145
  year: 2014
  ident: B189
  article-title: Enzymes as useful tools for environmental purposes
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2013.12.059
  contributor:
    fullname: Rao
– volume: 104
  start-page: 21
  year: 2015
  ident: B215
  article-title: Enzymatic decolorization and degradation of azo dyes – a review
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2015.04.027
  contributor:
    fullname: Singh
– volume: 48
  start-page: 1
  year: 2011
  ident: B120
  article-title: The effect of carbon source succession on laccase activity in the co-culture process of Ganoderma lucidum and a yeast
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2010.07.005
  contributor:
    fullname: Li
– volume: 157
  start-page: 200
  year: 2016
  ident: B126
  article-title: Complete biodegradation of chlorpyrifos by engineered Pseudomonas putida cells expressing surface-immobilized laccases
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2016.05.031
  contributor:
    fullname: Liu
– volume: 160
  start-page: 1760
  year: 2010
  ident: B9
  article-title: Ligninolytic fungal laccases and their biotechnological applications
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-009-8676-y
  contributor:
    fullname: Arora
– volume: 2014
  start-page: 1
  year: 2014
  ident: B240
  article-title: Fungal laccases and their applications in bioremediation
  publication-title: Enzyme Res.
  doi: 10.1155/2014/163242
  contributor:
    fullname: Viswanath
– volume: 493
  start-page: 27
  ident: B266
  article-title: Destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels with fungal laccase
  publication-title: Anal. Biochem.
  doi: 10.1016/j.ab.2015.10.004
  contributor:
    fullname: Yang
– volume: 72
  start-page: 923
  year: 2015
  ident: B178
  article-title: How to enjoy laccases
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-014-1823-9
  contributor:
    fullname: Pezzella
– volume: 216
  start-page: 203
  year: 2016
  ident: B118
  article-title: Degradation of synthetic pollutants in real wastewater using laccase encapsulated in core-shell magnetic copper alginate beads
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2016.05.077
  contributor:
    fullname: Le
– volume: 101
  start-page: 2331
  year: 2010
  ident: B134
  article-title: Laccases for removal of recalcitrant and emerging pollutants
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2009.10.087
  contributor:
    fullname: Majeau
– volume: 8
  start-page: 145
  year: 2015
  ident: B244
  article-title: Lignin engineering through laccase modification: a promising field for energy plant improvement
  publication-title: Biotechnol. Biofuels
  doi: 10.1186/s13068-015-0331-y
  contributor:
    fullname: Wang
– volume: 78
  start-page: 4732
  year: 2012
  ident: B219
  article-title: Differential regulation by organic compounds and heavy metals of multiple laccase genes in the aquatic hyphomycete Clavariopsis aquatica
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.00635-12
  contributor:
    fullname: Solé
– volume: 169
  start-page: 2391
  year: 2015
  ident: B61
  article-title: An intracellular laccase is responsible for epicatechin-mediated anthocyanin degradation in litchi fruit pericarp
  publication-title: Plant Physiol.
  doi: 10.1104/pp.15.00359
  contributor:
    fullname: Fang
– volume: 30
  start-page: 814
  year: 2013
  ident: B159
  article-title: Formulation and characterization of an immobilized laccase biocatalyst and its application to eliminate organic micropollutants in wastewater
  publication-title: N. Biotechnol.
  doi: 10.1016/j.nbt.2012.12.004
  contributor:
    fullname: Nair
– volume: 36
  start-page: 70
  year: 2016
  ident: B217
  article-title: Structure, functionality and tuning up of laccases for lignocellulose and other industrial applications
  publication-title: Crit. Rev. Biotechnol.
  doi: 10.3109/07388551.2014.949617
  contributor:
    fullname: Sitarz
– volume: 31
  start-page: 276
  year: 2015
  ident: B228
  article-title: Ultrasound assisted Laccase catalyzed degradation of Ciprofloxacin hydrochloride
  publication-title: J. Ind. Eng. Chem.
  doi: 10.1016/j.jiec.2015.06.037
  contributor:
    fullname: Sutar
– volume: 60
  start-page: 700
  year: 2003
  ident: B255
  article-title: Purification, molecular characterization and reactivity with aromatic compounds of a laccase from basidiomycete Trametes sp. strain AH28-2
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-002-1169-3
  contributor:
    fullname: Xiao
– volume: 282
  start-page: 1190
  year: 2015
  ident: B183
  article-title: Lignin-degrading enzymes
  publication-title: FEBS J.
  doi: 10.1111/febs.13224
  contributor:
    fullname: Pollegioni
– volume: 8
  start-page: 918
  year: 2015
  ident: B218
  article-title: Induction of lcc2 expression and activity by Agaricus bisporus provides defence against Trichoderma aggressivum toxic extracts
  publication-title: Microb. Biotechnol.
  doi: 10.1111/1751-7915.12277
  contributor:
    fullname: Sjaarda
– volume: 157
  start-page: 174
  year: 2009
  ident: B252
  article-title: Structure and action mechanism of ligninolytic enzymes
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-008-8279-z
  contributor:
    fullname: Wong
– volume: 103
  start-page: 47
  year: 2015
  ident: B140
  article-title: Sulfamethoxazole and isoproturon degradation and detoxification by a laccase-mediator system: influence of treatment conditions and mechanistic aspects
  publication-title: Biochem. Eng. J.
  doi: 10.1016/j.bej.2015.06.008
  contributor:
    fullname: Margot
– volume: 6
  start-page: 35787
  year: 2016
  ident: B100
  article-title: Conditions optimizing and application of laccase-mediator system (LMS) for the Laccase-catalyzed pesticide degradation
  publication-title: Sci. Rep.
  doi: 10.1038/srep35787
  contributor:
    fullname: Jin
– volume: 39
  start-page: 1
  year: 2016
  ident: B59
  article-title: Lignocellulose degrading extremozymes produced by Pichia pastoris: current status and future prospects
  publication-title: Bioprocess Biosyst. Eng.
  doi: 10.1007/s00449-015-1476-6
  contributor:
    fullname: Ergün
– volume: 46
  start-page: 955
  year: 2012
  ident: B94
  article-title: Degradation of carbamazepine by Trametes versicolor in an air pulsed fluidized bed bioreactor and identification of intermediates
  publication-title: Water Res.
  doi: 10.1016/j.watres.2011.11.063
  contributor:
    fullname: Jelic
– volume: 169
  start-page: 453
  year: 2014
  ident: B60
  article-title: Cloning, expression and phylogenetic analysis of a divergent laccase multigene family in Auricularia auricula-judae
  publication-title: Microbiol. Res.
  doi: 10.1016/j.micres.2013.08.004
  contributor:
    fullname: Fan
– volume: 2010
  start-page: 1
  year: 2010
  ident: B172
  article-title: Uses of laccases in the food industry
  publication-title: Enzyme Res.
  doi: 10.4061/2010/918761
  contributor:
    fullname: Osma
– volume: 99
  start-page: 115
  year: 2015
  ident: B163
  article-title: Degradation of a broad spectrum of trace organic contaminants by an enzymatic membrane reactor: complementary role of membrane retention and enzymatic degradation
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2014.12.004
  contributor:
    fullname: Nguyen
– volume: 41
  start-page: 373
  year: 2011
  ident: B222
  article-title: Laccase: a review of its past and its future in bioremediation
  publication-title: Crit. Rev. Environ. Sci. Technol.
  doi: 10.1080/10643380902945706
  contributor:
    fullname: Strong
– volume: 58
  start-page: 93
  year: 2016
  ident: B6
  article-title: Yeast hosts for the production of recombinant laccases: a review
  publication-title: Mol. Biotechnol.
  doi: 10.1007/s12033-015-9910-1
  contributor:
    fullname: Antošovǎ
– volume: 27
  start-page: 67
  year: 2013
  ident: B192
  article-title: Fungal laccases
  publication-title: Fungal Biol. Rev.
  doi: 10.1016/j.fbr.2013.07.001
  contributor:
    fullname: Rivera-Hoyos
– volume: 26
  start-page: 1570
  year: 2016
  ident: B258
  article-title: Selection of high laccase-producing Coriolopsis gallica strain T906: mutation breeding, strain characterization, and features of the extracellular laccases
  publication-title: J. Microbiol. Biotechnol.
  doi: 10.4014/jmb.1604.04011
  contributor:
    fullname: Xu
– volume: 13
  start-page: 309
  year: 2015
  ident: B259
  article-title: Applications of ligninolytic enzymes to pollutants, wastewater, dyes, soil, coal, paper and polymers
  publication-title: Environ. Chem. Lett.
  doi: 10.1007/s10311-015-0516-4
  contributor:
    fullname: Yadav
– volume: 156
  start-page: 183
  ident: B1
  article-title: Design, economic evaluation and optimization of enzymatic membrane reactors for antibiotics degradation in wastewaters
  publication-title: Sep. Purif. Technol.
  doi: 10.1016/j.seppur.2015.09.072
  contributor:
    fullname: Abejón
– volume: 1
  start-page: 220
  year: 2012
  ident: B82
  article-title: Extracellular oxidases of Cerrena sp. complementarily functioning in artificial dye decolorization including laccase, manganese peroxidase, and novel versatile peroxidases
  publication-title: Biocatal. Agric. Biotechnol.
  doi: 10.1016/j.bcab.2012.03.003
  contributor:
    fullname: Hibi
– volume: 33
  start-page: 268
  year: 2015
  ident: B111
  article-title: Fungal enzymes for environmental management
  publication-title: Curr. Opin. Biotechnol.
  doi: 10.1016/j.copbio.2015.03.006
  contributor:
    fullname: Kües
– volume: 200
  start-page: 477
  ident: B167
  article-title: Laccase-syringaldehyde-mediated degradation of trace organic contaminants in an enzymatic membrane reactor: removal efficiency and effluent toxicity
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2015.10.054
  contributor:
    fullname: Nguyen
– volume: 98
  start-page: 6525
  year: 2014
  ident: B109
  article-title: Laccase applications in biofuels production: current status and future prospects
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-014-5810-8
  contributor:
    fullname: Kudanga
– volume: 33
  start-page: 404
  year: 2013
  ident: B15
  article-title: Laccase immobilization and insolubilization: from fundamentals to applications for the elimination of emerging contaminants in wastewater treatment
  publication-title: Crit. Rev. Biotechnol.
  doi: 10.3109/07388551.2012.725390
  contributor:
    fullname: Ba
– volume: 23
  start-page: 8929
  year: 2016
  ident: B7
  article-title: Recyclable cross-linked laccase aggregates coupled to magnetic silica microbeads for elimination of pharmaceuticals from municipal wastewater
  publication-title: Environ. Sci. Pollut. Res.
  doi: 10.1007/s11356-016-6139-x
  contributor:
    fullname: Arca-Ramos
– volume: 116
  start-page: 883
  year: 2012
  ident: B220
  article-title: Immobilized laccase of Cerrena unicolor for elimination of endocrine disruptor micropollutants
  publication-title: Fungal Biol.
  doi: 10.1016/j.funbio.2012.05.005
  contributor:
    fullname: Songulashvili
– volume: 108
  start-page: 1
  year: 2016
  ident: B229
  article-title: Biocatalytic conversion and detoxification of imipramine by the laccase-mediated system
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2015.11.029
  contributor:
    fullname: Tahmasbi
– volume: 6
  start-page: e25724
  year: 2011
  ident: B14
  article-title: Bioinformatic analysis reveals high diversity of bacterial genes for laccase-like enzymes
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0025724
  contributor:
    fullname: Ausec
– volume: 78
  start-page: 4037
  year: 2012
  ident: B33
  article-title: Transcriptional and enzymatic profiling of Pleurotus ostreatus laccase genes in submerged and solid-state fermentation cultures
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.07880-11
  contributor:
    fullname: Castanera
– volume: 45
  start-page: 1921
  year: 2011
  ident: B72
  article-title: Laccase-catalyzed oxidation of oxybenzone in municipal wastewater primary effluent
  publication-title: Water Res.
  doi: 10.1016/j.watres.2010.12.027
  contributor:
    fullname: Garcia
– volume: 1369
  start-page: 43
  year: 2014
  ident: B128
  article-title: Sample preservation for the analysis of antibiotics in water
  publication-title: J. Chromatogr. A
  doi: 10.1016/j.chroma.2014.09.089
  contributor:
    fullname: Llorca
– volume: 20
  start-page: 441
  year: 2009
  ident: B171
  article-title: Biodegradation and removal of pharmaceuticals and personal care products in treatment systems: a review
  publication-title: Biodegradation
  doi: 10.1007/s10532-008-9237-8
  contributor:
    fullname: Onesios
– volume: 12
  start-page: 72
  year: 2011
  ident: B112
  article-title: Multiple multi-copper oxidase gene families in basidiomycetes – what for?
  publication-title: Curr. Genomics
  doi: 10.2174/138920211795564377
  contributor:
    fullname: Kües
– volume: 273
  start-page: 2308
  year: 2006
  ident: B83
  article-title: Phylogenetic comparison and classification of laccase and related multicopper oxidase protein sequences
  publication-title: FEBS J.
  doi: 10.1111/j.1742-4658.2006.05247.x
  contributor:
    fullname: Hoegger
– volume: 128
  start-page: 49
  year: 2013
  ident: B210
  article-title: Purification, biochemical characterization and dye decolorization capacity of an alkali-resistant and metal-tolerant laccase from Trametes pubescens
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2012.10.085
  contributor:
    fullname: Si
– volume: 5
  start-page: 1
  year: 2012
  ident: B194
  article-title: Laccases for denim bleaching: an eco-friendly alternative
  publication-title: Open Text. J.
  doi: 10.2174/1876520301205010001
  contributor:
    fullname: Rodríguez-Couto
– volume: 219
  start-page: 53
  year: 2016
  ident: B27
  article-title: Effects of hydraulic retention time and carbon to nitrogen ratio on micro-pollutant biodegradation in membrane bioreactor for leachate treatment
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2016.07.094
  contributor:
    fullname: Boonnorat
– volume: 143
  start-page: 69
  year: 2009
  ident: B40
  article-title: Laccase/mediator assisted degradation of triarylmethane dyes in a continuous membrane reactor
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2009.06.011
  contributor:
    fullname: Chhabra
– volume: 30
  start-page: 215
  year: 2006
  ident: B20
  article-title: Laccases-occurrence and properties
  publication-title: FEMS Microbiol. Rev.
  doi: 10.1111/j.1574-4976.2005.00010.x
  contributor:
    fullname: Baldrian
– volume: 67
  start-page: 2088
  year: 2001
  ident: B44
  article-title: Induction of laccase activity in Rhizoctonia solani by antagonistic Pseudomonas fluorescens strains and a range of chemical treatments
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.67.5.2088-2094.2001
  contributor:
    fullname: Crowe
– volume: 45
  start-page: 1855
  ident: B162
  article-title: Enhancement of trace organic contaminant degradation by crude enzyme extract from Trametes versicolor culture: effect of mediator type and concentration
  publication-title: J. Taiwan Inst. Chem. Eng.
  doi: 10.1016/j.jtice.2014.03.021
  contributor:
    fullname: Nguyen
– volume: 162
  start-page: 45
  year: 2014
  ident: B176
  article-title: Induction of a laccase Lcc9 from Coprinopsis cinerea by fungal coculture and its application on indigo dye decolorization
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2014.03.116
  contributor:
    fullname: Pan
– volume: 25
  start-page: 761
  year: 2012
  ident: B38
  article-title: Biochemical characterization of a novel laccase from the basidiomycete fungus Cerrena sp. WR1
  publication-title: Protein Eng. Des. Sel.
  doi: 10.1093/protein/gzs082
  contributor:
    fullname: Chen
– volume: 231
  start-page: 85
  year: 2017
  ident: B185
  article-title: Pilot-scale bioconversion of rice and sunflower agro-residues into medicinal mushrooms and laccase enzymes through solid-state fermentation with Ganoderma lucidum
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2017.01.064
  contributor:
    fullname: Postemsky
– volume: 133
  start-page: 77
  year: 2016
  ident: B272
  article-title: Laccase-catalyzed treatment of ketoconazole, identification of biotransformed metabolites, determination of kinetic parameters, and evaluation of micro-toxicity
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2016.07.015
  contributor:
    fullname: Yousefi-Ahmadipour
– volume: 487
  start-page: 748
  ident: B16
  article-title: Synthesis and characterization of combined cross-linked laccase and tyrosinase aggregates transforming acetaminophen as a model phenolic compound in wastewaters
  publication-title: Sci. Total Environ.
  doi: 10.1016/j.scitotenv.2013.10.004
  contributor:
    fullname: Ba
– volume: 72
  start-page: 911
  year: 2015
  ident: B143
  article-title: Laccases of prokaryotic origin: enzymes at the interface of protein science and protein technology
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-014-1822-x
  contributor:
    fullname: Martins
– start-page: 213
  year: 2012
  ident: B197
  article-title: Continuous degradation of a mixture of sulfonamides by Trametes versicolor and identification of metabolites from sulfapyridine and sulfathiazole
  publication-title: J. Hazard. Mater
  doi: 10.1016/j.jhazmat.2012.02.008
  contributor:
    fullname: Rodriguez-Rodriguez
– volume: 50
  start-page: 98
  year: 2010
  ident: B247
  article-title: Gongronella sp. induces overproduction of laccase in Panus rudis
  publication-title: J. Basic Microbiol.
  doi: 10.1002/jobm.200900155
  contributor:
    fullname: Wei
– volume: 97
  start-page: 705
  year: 2013
  ident: B179
  article-title: Transcriptional analysis of Pleurotus ostreatus laccase genes
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-012-3980-9
  contributor:
    fullname: Pezzella
– volume: 14
  start-page: 229
  year: 2015
  ident: B53
  article-title: Biodegradation and biotransformation of polycyclic non-steroidal anti-inflammatory drugs
  publication-title: Rev. Environ. Sci. Biotechnol.
  doi: 10.1007/s11157-015-9364-8
  contributor:
    fullname: Domaradzka
– volume: 4
  start-page: 11689
  year: 2014
  ident: B202
  article-title: Laccase mediated diclofenac transformation and cytotoxicity assessment on mouse fibroblast 3T3-L1 preadipocytes
  publication-title: RSC Adv.
  doi: 10.1039/c3ra46014b
  contributor:
    fullname: Sathishkumar
– volume: 73
  start-page: 89
  year: 2006
  ident: B274
  article-title: Efficient production of laccases by Trametes sp. AH28-2 in cocultivation with a Trichoderma strain
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-006-0430-6
  contributor:
    fullname: Zhang
– volume: 50
  start-page: 45
  ident: B105
  article-title: The laccase multi-gene family in Coprinopsis cinerea has seventeen different members that divide into two distinct subfamilies
  publication-title: Curr. Genet.
  doi: 10.1007/s00294-006-0074-1
  contributor:
    fullname: Kilaru
– volume: 209
  start-page: 76
  year: 2015
  ident: B42
  article-title: Recombinant expression of four oxidoreductases in Phanerochaete chrysosporium improves degradation of phenolic and non-phenolic substrates
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2015.06.401
  contributor:
    fullname: Coconi-Linares
– volume: 23
  start-page: 4024
  year: 2016
  ident: B37
  article-title: Immobilization of fungal laccase onto a nonionic surfactant-modified clay material: application to PAH degradation
  publication-title: Environ. Sci. Pollut. Res.
  doi: 10.1007/s11356-015-4248-6
  contributor:
    fullname: Chang
– volume: 72
  start-page: 885
  year: 2015
  ident: B182
  article-title: Spectroscopic and computational characterization of laccases and their substrate radical intermediates
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-014-1825-7
  contributor:
    fullname: Pogni
– volume: 33
  start-page: 323
  year: 2013
  ident: B253
  article-title: The bioinformatic analyses and the gene expression induced by Cu2+ of 11 laccase homologous genes from Volvariella volvacea
  publication-title: Mycosystema
  doi: 10.13346/j.mycosystema.130231
  contributor:
    fullname: Wu
– volume: 98
  start-page: 9931
  year: 2014
  ident: B74
  article-title: Laccases to take on the challenge of emerging organic contaminants in wastewater
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-014-6177-6
  contributor:
    fullname: Gasser
– volume: 69
  start-page: 682
  year: 2006
  ident: B149
  article-title: The white-rot fungus Cerrena unicolor strain 137 produces two laccase isoforms with different physico-chemical and catalytic properties
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-005-0015-9
  contributor:
    fullname: Michniewicz
– volume: 176
  start-page: 1089
  year: 2010
  ident: B276
  article-title: In vitro degradation of carbamazepine and diclofenac by crude lignin peroxidase
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2009.10.133
  contributor:
    fullname: Zhang
– volume: 111
  start-page: 36
  year: 2012
  ident: B64
  article-title: A new marine bacterial laccase with chloride-enhancing, alkaline-dependent activity and dye decolorization ability
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2012.01.172
  contributor:
    fullname: Fang
– volume: 7
  start-page: 707
  year: 2016
  ident: B103
  article-title: High level secretion of laccase (LccH) from a newly isolated white-rot basidiomycete, Hexagonia hirta MSF2
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2016.00707
  contributor:
    fullname: Kandasamy
– volume: 36
  start-page: 45
  year: 2009
  ident: B88
  article-title: Laccase-mediator system in the decolorization of different types of recalcitrant dyes
  publication-title: J. Ind. Microbiol. Biotechnol.
  doi: 10.1007/s10295-008-0471-1
  contributor:
    fullname: Hu
– volume: 33
  start-page: 155
  year: 2015
  ident: B4
  article-title: Engineering the ligninolytic enzyme consortium
  publication-title: Trends Biotechnol.
  doi: 10.1016/j.tibtech.2014.12.007
  contributor:
    fullname: Alcalde
– volume: 66
  start-page: 194
  year: 2004
  ident: B102
  article-title: Overproduction of recombinant laccase using a homologous expression system in Coriolus versicolor
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-004-1663-x
  contributor:
    fullname: Kajita
– volume: 338
  start-page: 121
  year: 2015
  ident: B221
  article-title: Production of a high level of laccase by submerged fermentation at 120-L scale of Cerrena unicolor C-139 grown on wheat bran
  publication-title: C. R. Biol.
  doi: 10.1016/j.crvi.2014.12.001
  contributor:
    fullname: Songulashvili
– start-page: 500
  year: 2014
  ident: B153
  article-title: Degradation of selected agrochemicals by the white rot fungus Trametes versicolor
  publication-title: Sci. Total Environ
  doi: 10.1016/j.scitotenv.2014.08.116
  contributor:
    fullname: Mir-Tutusaus
– volume: 31
  start-page: 335
  year: 2013
  ident: B95
  article-title: Laccase-mediated oxidation of small organics: bifunctional roles for versatile applications
  publication-title: Trends Biotechnol.
  doi: 10.1016/j.tibtech.2013.04.002
  contributor:
    fullname: Jeon
– volume: 71
  start-page: 200
  ident: B106
  article-title: Expression of laccase gene lcc1 in Coprinopsis cinerea under control of various basidiomycetous promoters
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-005-0128-1
  contributor:
    fullname: Kilaru
– volume: 552
  start-page: 146
  year: 2014
  ident: B107
  article-title: Overexpression of CaDSR6 increases tolerance to drought and salt stresses in transgenic Arabidopsis plants
  publication-title: Gene
  doi: 10.1016/j.gene.2014.09.028
  contributor:
    fullname: Kim
– volume: 8
  start-page: E245
  year: 2016
  ident: B131
  article-title: Aflatoxin B1 and M1 degradation by Lac2 from Pleurotus pulmonarius and redox mediators
  publication-title: Toxins
  doi: 10.3390/toxins8090245
  contributor:
    fullname: Loi
– volume: 38
  start-page: 504
  year: 2006
  ident: B54
  article-title: Enhanced production of laccase by a marine fungus during treatment of colored effluents and synthetic dyes
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2005.07.005
  contributor:
    fullname: D'Souza
– volume: 21
  start-page: 19
  year: 2016
  ident: B205
  article-title: Recent trends in fungal laccase for various industrial applications: an eco-friendly approach - a review
  publication-title: Biotechnol. Bioprocess Eng.
  doi: 10.1007/s12257-015-0278-7
  contributor:
    fullname: Senthivelan
– volume: 255
  start-page: 63
  year: 2014
  ident: B256
  article-title: Triclosan removal by laccase immobilized on mesoporous nanofibers: strong adsorption and efficient degradation
  publication-title: Chem. Eng. J.
  doi: 10.1016/j.cej.2014.06.060
  contributor:
    fullname: Xu
– volume: 176
  start-page: 836
  ident: B137
  article-title: Degradation of the drug sodium diclofenac by Trametes versicolor pellets and identification of some intermediates by NMR
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2009.11.112
  contributor:
    fullname: Marco-Urrea
– volume: 469
  start-page: 306
  year: 2016
  ident: B211
  article-title: Molecular modeling and simulation studies of recombinant laccase from Yersinia enterocolitica suggests significant role in the biotransformation of non-steroidal anti-inflammatory drugs
  publication-title: Biochem. Biophys. Res. Commun.
  doi: 10.1016/j.bbrc.2015.11.096
  contributor:
    fullname: Singh
– volume: 113
  start-page: 259
  year: 2012
  ident: B250
  article-title: The implication of mediators for enhancement of laccase oxidation of sulfonamide antibiotics
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2011.12.111
  contributor:
    fullname: Weng
– volume: 46
  start-page: 2102
  year: 2012
  ident: B78
  article-title: Reactions of a sulfonamide antimicrobial with model humic constituents: assessing pathways and stability of covalent bonding
  publication-title: Environ. Sci. Technol.
  doi: 10.1021/es202272w
  contributor:
    fullname: Gulkowska
– volume: 110
  start-page: 69
  year: 2016
  ident: B277
  article-title: Immobilization of laccase onto chitosan beads to enhance its capability to degrade synthetic dyes
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2016.03.004
  contributor:
    fullname: Zheng
– volume: 29
  start-page: 480
  year: 2011
  ident: B201
  article-title: Expression of industrially relevant laccases: prokaryotic style
  publication-title: Trends Biotechnol.
  doi: 10.1016/j.tibtech.2011.04.005
  contributor:
    fullname: Santhanam
– volume: 5
  start-page: 63
  year: 2015
  ident: B200
  article-title: Grouping of multicopper oxidases in Lentinula edodes by sequence similarities and expression patterns
  publication-title: AMB Express
  doi: 10.1186/s13568-015-0151-2
  contributor:
    fullname: Sakamoto
– volume: 99
  start-page: 155
  year: 2015
  ident: B213
  article-title: Critical factors affecting laccase-mediated biobleaching of pulp in paper industry
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-014-6219-0
  contributor:
    fullname: Singh
– volume: 30
  start-page: 933
  year: 2012
  ident: B50
  article-title: Harnessing the power of enzymes for environmental stewardship
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2011.05.013
  contributor:
    fullname: Demarche
– volume: 37
  start-page: 335
  year: 2016
  ident: B148
  article-title: A comparison between the oxidation with laccase and horseradish peroxidase for triclosan conversion
  publication-title: Environ. Technol.
  doi: 10.1080/09593330.2015.1069897
  contributor:
    fullname: Melo
– volume: 51
  start-page: 124
  year: 2010
  ident: B130
  article-title: Laccase-catalyzed degradation of anti-inflammatories and estrogens
  publication-title: Biochem. Eng. J.
  doi: 10.1016/j.bej.2010.06.005
  contributor:
    fullname: Lloret
– volume: 74
  start-page: 765
  year: 2009
  ident: B138
  article-title: Ability of white-rot fungi to remove selected pharmaceuticals and identification of degradation products of ibuprofen by Trametes versicolor
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2008.10.040
  contributor:
    fullname: Marco-Urrea
– volume: 10
  start-page: 78
  year: 2011
  ident: B188
  article-title: The Aspergillus niger multicopper oxidase family: analysis and overexpression of laccase-like encoding genes
  publication-title: Microb. Cell Fact.
  doi: 10.1186/1475-2859-10-78
  contributor:
    fullname: Ramos
– volume: 40
  start-page: 179
  year: 2010
  ident: B52
  article-title: Insect multicopper oxidases: diversity, properties, and physiological roles
  publication-title: Insect Biochem. Mol. Biol.
  doi: 10.1016/j.ibmb.2010.02.006
  contributor:
    fullname: Dittmer
– volume: 487
  start-page: 830
  year: 2014
  ident: B114
  article-title: Magnetic cross-linked laccase aggregates — bioremediation tool for decolorization of distinct classes of recalcitrant dyes
  publication-title: Sci. Total Environ.
  doi: 10.1016/j.scitotenv.2014.04.009
  contributor:
    fullname: Kumar
– volume: 168
  start-page: 256
  year: 2012
  ident: B242
  article-title: Heat shock treatment improves Trametes versicolor laccase production
  publication-title: Appl. Biochem. Biotechnol.
  doi: 10.1007/s12010-012-9769-6
  contributor:
    fullname: Wang
– volume: 166
  start-page: 145
  year: 2003
  ident: B231
  article-title: Pharmaceutical antibiotic compounds in soils – a review
  publication-title: J. Plant Nutr. Soil Sci.
  doi: 10.1002/jpln.200390023
  contributor:
    fullname: Thiele-Bruhn
– volume: 278
  start-page: 14565
  year: 2003
  ident: B22
  article-title: The Schizosaccharomyces pombe Cuf1 is composed of functional modules from two distinct classes of copper metalloregulatory transcription factors
  publication-title: J. Biol. Chem.
  doi: 10.1074/jbc.M300861200
  contributor:
    fullname: Beaudoin
– volume: 40
  start-page: 242
  year: 2010
  ident: B198
  article-title: Purification of extracellular laccase from Cerrena unicolor
  publication-title: Prep. Biochem. Biotechnol.
  doi: 10.1080/10826068.2010.488967
  contributor:
    fullname: Rogalski
– volume: 219
  start-page: 500
  year: 2016
  ident: B23
  article-title: Removal of antibiotics in wastewater by enzymatic treatment with fungal laccase - Degradation of compounds does not always eliminate toxicity
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2016.08.004
  contributor:
    fullname: Becker
– volume: 108
  start-page: 32
  year: 2014
  ident: B187
  article-title: Purification and characterization of two thermostable laccases from Pycnoporus sanguineus and potential role in degradation of endocrine disrupting chemicals
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2014.06.006
  contributor:
    fullname: Ramírez-Cavazos
– volume: 30
  start-page: 803
  ident: B141
  article-title: Influence of treatment conditions on the oxidation of micropollutants by Trametes versicolor laccase
  publication-title: N. Biotechnol.
  doi: 10.1016/j.nbt.2013.06.004
  contributor:
    fullname: Margot
– volume: 103
  start-page: 498
  year: 2012
  ident: B223
  article-title: Treatment of tetracycline antibiotics by laccase in the presence of 1-hydroxybenzotriazole
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2011.10.041
  contributor:
    fullname: Suda
– volume: 22
  start-page: 539
  year: 2011
  ident: B56
  article-title: Oxidation of pharmaceutically active compounds by a ligninolytic fungal peroxidase
  publication-title: Biodegradation
  doi: 10.1007/s10532-010-9426-0
  contributor:
    fullname: Eibes
– volume: 103
  start-page: 1029
  year: 2013
  ident: B199
  article-title: Lcc1 and Lcc5 are the main laccases secreted in liquid cultures of Coprinopsis cinerea strains
  publication-title: Antonie van Leeuwenhoek
  doi: 10.1007/s10482-013-9883-7
  contributor:
    fullname: Rühl
– volume: 57
  start-page: 14478
  year: 2015
  ident: B13
  article-title: Optimization of the enzymatic elimination of flumequine by laccase-mediated system using response surface methodology
  publication-title: Desalin. Water Treat.
  doi: 10.1080/19443994.2015.1063462
  contributor:
    fullname: Ashrafi
– volume: 31
  start-page: 838
  year: 2013
  ident: B168
  article-title: Lignocellulose-degrading enzymes from termites and their symbiotic microbiota
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2013.04.005
  contributor:
    fullname: Ni
– volume: 57
  start-page: 2563
  year: 2006
  ident: B30
  article-title: Mutant identification and characterization of the laccase gene family in Arabidopsis
  publication-title: J. Exp. Bot.
  doi: 10.1093/jxb/erl022
  contributor:
    fullname: Cai
– volume: 95
  start-page: 920
  year: 2017
  ident: B245
  article-title: Purification, characterization, and cloning of an extracellular laccase with potent dye decolorizing ability from white rot fungus Cerrena unicolor GSM-01
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2016.10.079
  contributor:
    fullname: Wang
– volume: 17
  start-page: 326
  year: 2015
  ident: B35
  article-title: Properties of bacterial laccases and their application in bioremediation of industrial wastes
  publication-title: Environ. Sci. Process. Impacts
  doi: 10.1039/C4EM00627E
  contributor:
    fullname: Chandra
– volume: 28
  start-page: 694
  year: 2010
  ident: B31
  article-title: Laccases and their natural mediators: biotechnological tools for sustainable eco-friendly processes
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2010.05.002
  contributor:
    fullname: Cañas
– volume: 16
  start-page: 28498
  year: 2015
  ident: B133
  article-title: Cloning and expression analysis of Vvlcc3, a novel and functional laccase gene possibly involved in stipe elongation
  publication-title: Int. J. Mol. Sci.
  doi: 10.3390/ijms161226111
  contributor:
    fullname: Lu
– volume: 3
  start-page: 63
  ident: B139
  article-title: Bacterial versus fungal laccase: potential for micropollutant degradation
  publication-title: AMB Express
  doi: 10.1186/2191-0855-3-63
  contributor:
    fullname: Margot
– volume: 41
  start-page: 353
  year: 2007
  ident: B116
  article-title: Efficacy of mediators for enhancing the laccase-catalyzed oxidation of aqueous phenol
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2007.03.003
  contributor:
    fullname: Kurniawati
– volume: 108
  start-page: 34
  year: 2016
  ident: B196
  article-title: Biotransformation kinetics of pharmaceutical and industrial micropollutants in groundwaters by a laccase cocktail from Pycnoporus sanguineus CS43 fungi
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2015.12.003
  contributor:
    fullname: Rodríguez-Delgado
– volume: 62
  start-page: 871
  year: 2011
  ident: B226
  article-title: The level of secreted laccase activity in the edible fungi and their growing cycles are closely related
  publication-title: Curr. Microbiol.
  doi: 10.1007/s00284-010-9794-z
  contributor:
    fullname: Sun
– volume: 73
  start-page: 118
  ident: B2
  article-title: Large-scale enzymatic membrane reactors for tetracycline degradation in WWTP effluents
  publication-title: Water Res.
  doi: 10.1016/j.watres.2015.01.012
  contributor:
    fullname: Abejón
– volume: 31
  start-page: 1443
  year: 2015
  ident: B70
  article-title: Insights into laccase producing organisms, fermentation states, purification strategies, and biotechnological applications
  publication-title: Biotechnol. Prog.
  doi: 10.1002/btpr.2173
  contributor:
    fullname: Forootanfar
– volume: 210
  start-page: 108
  ident: B161
  article-title: Continuous adsorption and biotransformation of micropollutants by granular activated carbon-bound laccase in a packed-bed enzyme reactor
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2016.01.014
  contributor:
    fullname: Nguyen
– volume: 89
  start-page: 31
  year: 2016
  ident: B144
  article-title: Polyamide 6/chitosan nanofibers as support for the immobilization of Trametes versicolor laccase for the elimination of endocrine disrupting chemicals
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2016.03.001
  contributor:
    fullname: Maryskova
– volume: 54
  start-page: 260
  year: 2007
  ident: B87
  article-title: Cloning of a laccase gene from a novel basidiomycete Trametes sp. 420 and its heterologous expression in Pichia pastoris
  publication-title: Curr. Microbiol.
  doi: 10.1007/s00284-006-0068-8
  contributor:
    fullname: Hong
– volume: 32
  start-page: 52
  year: 2016
  ident: B26
  article-title: The degradation of two fluoroquinolone based antimicrobials by SilA, an alkaline laccase from Streptomyces ipomoeae
  publication-title: World J. Microbiol. Biotechnol.
  doi: 10.1007/s11274-016-2032-5
  contributor:
    fullname: Blánquez
– volume: 30
  start-page: 78
  year: 2012
  ident: B49
  article-title: Classical breeding in Pleurotus ostreatus: a natural approach for laccase production improvement
  publication-title: Biocatal. Biotransformation
  doi: 10.3109/10242422.2012.646032
  contributor:
    fullname: del Vecchio
– volume: 113
  start-page: 169
  year: 2016
  ident: B12
  article-title: Impacts of redox-mediator type on trace organic contaminants degradation by laccase: degradation efficiency, laccase stability and effluent toxicity
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2016.04.027
  contributor:
    fullname: Ashe
– volume: 8
  start-page: 54
  year: 2015
  ident: B63
  article-title: Identification of a laccase Glac15 from Ganoderma lucidum 77002 and its application in bioethanol production
  publication-title: Biotechnol. Biofuels
  doi: 10.1186/s13068-015-0235-x
  contributor:
    fullname: Fang
– volume: 177
  start-page: 924
  year: 2010
  ident: B249
  article-title: Enzymatic degradation of tetracycline and oxytetracycline by crude manganese peroxidase prepared from Phanerochaete chrysosporium
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2010.01.005
  contributor:
    fullname: Wen
– volume: 125
  start-page: 344
  year: 2012
  ident: B173
  article-title: Degradation of some benzodiazepines by a laccase-mediated system in aqueous solution
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2012.09.039
  contributor:
    fullname: Ostadhadi-Dehkordi
– volume: 146
  start-page: 807
  year: 2013
  ident: B216
  article-title: Preparation and characterization of stable cross-linked enzyme aggregates of novel laccase enzyme from Shewanella putrefaciens and using malachite green decolorization
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2013.08.032
  contributor:
    fullname: Sinirlioglu
– volume: 5
  start-page: 81
  year: 2015
  ident: B8
  article-title: Molecular breeding of lignin-degrading brown-rot fungus Gloeophyllum trabeum by homologous expression of laccase gene
  publication-title: AMB Express
  doi: 10.1186/s13568-015-0173-9
  contributor:
    fullname: Arimoto
– volume: 2011
  start-page: 376015
  year: 2011
  ident: B10
  article-title: Laccase-based CLEAs: chitosan as a novel cross-linking agent
  publication-title: Enzyme Res.
  doi: 10.4061/2011/376015
  contributor:
    fullname: Arsenault
– volume: 12
  start-page: 104
  year: 2011
  ident: B180
  article-title: Induction and transcriptional regulation of laccases in fungi
  publication-title: Curr. Genomics
  doi: 10.2174/138920211795564331
  contributor:
    fullname: Piscitelli
– volume: 177
  start-page: 93
  year: 2016
  ident: B91
  article-title: A Pycnoporus sanguineus laccase for denim bleaching and its comparison with an enzymatic commercial formulation
  publication-title: J. Environ. Manage.
  doi: 10.1016/j.jenvman.2016.04.008
  contributor:
    fullname: Iracheta-Cárdenas
– volume: 116
  start-page: 154
  year: 2015
  ident: B239
  article-title: The Trametes hirsuta 072 laccase multigene family: genes identification and transcriptional analysis under copper ions induction
  publication-title: Biochimie
  doi: 10.1016/j.biochi.2015.07.015
  contributor:
    fullname: Vasina
– volume: 141
  start-page: 97
  ident: B268
  article-title: Understanding the factors controlling the removal of trace organic contaminants by white-rot fungi and their lignin modifying enzymes: a critical review
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2013.01.173
  contributor:
    fullname: Yang
– volume: 75
  start-page: 272
  year: 2015
  ident: B36
  article-title: Biodegradation of three tetracyclines in river sediment
  publication-title: Ecol. Eng.
  doi: 10.1016/j.ecoleng.2014.11.039
  contributor:
    fullname: Chang
– volume: 44
  start-page: 1
  year: 2013
  ident: B123
  article-title: In silico bioremediation of polycyclic aromatic hydrocarbon: a frontier in environmental chemistry
  publication-title: J. Mol. Graph. Model.
  doi: 10.1016/j.jmgm.2013.04.011
  contributor:
    fullname: Librando
– volume: 476
  start-page: 384
  year: 2015
  ident: B46
  article-title: Characterization of laccase-grafted ceramic membranes for pharmaceuticals degradation
  publication-title: J. Membr. Sci.
  doi: 10.1016/j.memsci.2014.11.044
  contributor:
    fullname: de Cazes
– volume: 119
  start-page: 108
  year: 2014
  ident: B117
  article-title: Antibiotics in the environment
  publication-title: Ups. J. Med. Sci.
  doi: 10.3109/03009734.2014.896438
  contributor:
    fullname: Larsson
– volume: 72
  start-page: 897
  year: 2015
  ident: B177
  article-title: Laccase engineering by rational and evolutionary design
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-014-1824-8
  contributor:
    fullname: Pardo
– volume: 563
  start-page: 142
  year: 2015
  ident: B246
  article-title: The multigene family of fungal laccases and their expression in the white rot basidiomycete Flammulina velutipes
  publication-title: Gene
  doi: 10.1016/j.gene.2015.03.020
  contributor:
    fullname: Wang
– volume: 236
  start-page: 146
  year: 2014
  ident: B47
  article-title: Design and optimization of an enzymatic membrane reactor for tetracycline degradation
  publication-title: Catal. Today
  doi: 10.1016/j.cattod.2014.02.051
  contributor:
    fullname: de Cazes
– volume: 97
  start-page: 3293
  year: 2013
  ident: B76
  article-title: Enzyme-based formulations for decontamination: current state and perspectives
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-013-4797-x
  contributor:
    fullname: Grover
– volume: 33
  start-page: 260
  year: 2012
  ident: B90
  article-title: Biological and enzymatic treatment of bisphenol A and other endocrine disrupting compounds: a review
  publication-title: Crit. Rev. Biotechnol.
  doi: 10.3109/07388551.2012.694409
  contributor:
    fullname: Husain
– volume: 101
  start-page: 56
  year: 2014
  ident: B11
  article-title: Recent trends and valorization of immobilization strategies and ligninolytic enzymes by industrial biotechnology
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2013.12.016
  contributor:
    fullname: Asgher
– volume: 356
  start-page: 897
  year: 2014
  ident: B155
  article-title: Laccase and laccase-mediated systems in the synthesis of organic compounds
  publication-title: Adv. Synth. Catal.
  doi: 10.1002/adsc.201300960
  contributor:
    fullname: Mogharabi
– volume: 12
  start-page: 1956
  year: 2010
  ident: B175
  article-title: Pharmaceuticals and personal care products in effluent matrices: a survey of transformation and removal during wastewater treatment and implications for wastewater management
  publication-title: J. Environ. Monit.
  doi: 10.1039/c0em00068j
  contributor:
    fullname: Oulton
– volume: 7
  start-page: 429
  year: 2007
  ident: B29
  article-title: Elimination of endocrine disrupting chemicals using white rot fungi and their lignin modifying enzymes: a review
  publication-title: Eng. Life Sci.
  doi: 10.1002/elsc.200700017
  contributor:
    fullname: Cabana
– volume: 182
  start-page: 736
  year: 2009
  ident: B43
  article-title: Phylogenetic analysis, genomic organization, and expression analysis of multi-copper oxidases in the ectomycorrhizal basidiomycete Laccaria bicolor
  publication-title: New Phytol.
  doi: 10.1111/j.1469-8137.2009.02774.x
  contributor:
    fullname: Courty
– volume: 220
  start-page: 333
  year: 2016
  ident: B121
  article-title: Improving the bioremoval of sulfamethoxazole and alleviating cytotoxicity of its biotransformation by laccase producing system under coculture of Pycnoporus sanguineus and Alcaligenes faecalis
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2016.08.088
  contributor:
    fullname: Li
– volume: 43
  start-page: 523
  year: 2007
  ident: B156
  article-title: Laccase-mediator systems and their applications: a review
  publication-title: Appl. Biochem. Microbiol.
  doi: 10.1134/S0003683807050055
  contributor:
    fullname: Morozova
– volume: 322
  start-page: 525
  year: 2017
  ident: B261
  article-title: Degradation of tetracycline by immobilized laccase and the proposed transformation pathway
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2016.10.019
  contributor:
    fullname: Yang
– volume: 493
  start-page: 626
  year: 2014
  ident: B80
  article-title: Prevalence of sulfonamide and tetracycline resistance genes in drinking water treatment plants in the Yangtze River Delta, China
  publication-title: Sci. Total Environ.
  doi: 10.1016/j.scitotenv.2014.06.035
  contributor:
    fullname: Guo
– volume: 59
  start-page: 295
  year: 2012
  ident: B152
  article-title: Comparative analyses of laccase-catalyzed amination reactions for production of novel α-lactam antibiotics
  publication-title: Biotechnol. Appl. Biochem.
  doi: 10.1002/bab.1026
  contributor:
    fullname: Mikolasch
– volume: 15
  start-page: 199
  year: 2013
  ident: B209
  article-title: Study of the physiological characteristics of the medicinal mushroom Trametes pubescens (higher basidiomycetes) during the laccase-producing process
  publication-title: Int. J. Med. Mushrooms
  doi: 10.1615/IntJMedMushr.v15.i2.90
  contributor:
    fullname: Si
– volume: 23
  start-page: 1459
  year: 2007
  ident: B93
  article-title: Increased production of laccase by Cerrena unicolor in submerged liquid cultures
  publication-title: World J. Microbiol. Biotechnol.
  doi: 10.1007/s11274-007-9390-y
  contributor:
    fullname: Janusz
– volume: 6
  start-page: 34309
  year: 2016
  ident: B18
  article-title: Genome-wide identification of multifunctional laccase gene family in cotton (Gossypium spp.); expression and biochemical analysis during fiber development
  publication-title: Sci. Rep.
  doi: 10.1038/srep34309
  contributor:
    fullname: Balasubramanian
– volume: 262
  start-page: 88
  year: 2015
  ident: B257
  article-title: Enhancement of catalytic activity of immobilized laccase for diclofenac biodegradation by carbon nanotubes
  publication-title: Chem. Eng. J.
  doi: 10.1016/j.cej.2014.09.072
  contributor:
    fullname: Xu
– volume: 144
  start-page: 37
  year: 2009
  ident: B57
  article-title: Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2009.06.020
  contributor:
    fullname: Elisashvili
– volume: 3
  start-page: 12485
  year: 2013
  ident: B230
  article-title: Parameters in preparation and characterization of cross linked enzyme aggregates (CLEAs)
  publication-title: RSC Adv.
  doi: 10.1039/c3ra40818c
  contributor:
    fullname: Talekar
– volume: 191
  start-page: 214
  year: 2014
  ident: B124
  article-title: The nucleotide composition of the spacer sequence influences the expression yield of heterologously expressed genes in Bacillus subtilis
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2014.06.027
  contributor:
    fullname: Liebeton
– volume: 280
  start-page: 662
  ident: B17
  article-title: Hybrid bioreactor (HBR) of hollow fiber microfilter membrane and cross-linked laccase aggregates eliminate aromatic pharmaceuticals in wastewaters
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2014.08.062
  contributor:
    fullname: Ba
– volume: 8
  start-page: e58294
  year: 2013
  ident: B21
  article-title: Sequencing and comparative analysis of the straw mushroom (Volvariella volvacea) genome
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0058294
  contributor:
    fullname: Bao
– volume: 67
  start-page: 1216
  ident: B269
  article-title: Removal of trace organic contaminants by nitrifying activated sludge and wholecell and crude enzyme extract of Trametes versicolor
  publication-title: Water Sci. Technol.
  doi: 10.2166/wst.2013.684
  contributor:
    fullname: Yang
– volume: 94
  start-page: 535
  year: 2017
  ident: B170
  article-title: Biochemical characterization of an extremely stable pH-versatile laccase from Sporothrix carnis CPF-05
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2016.10.037
  contributor:
    fullname: Olajuyigbe
– volume: 7
  start-page: 1
  ident: B267
  article-title: Optimal parameters for laccase-mediated destaining of Coomassie Brilliant Blue R-250-stained polyacrylamide gels
  publication-title: Data Brief
  doi: 10.1016/j.dib.2016.01.029
  contributor:
    fullname: Yang
– volume: 100
  start-page: 2381
  year: 2016
  ident: B85
  article-title: Biochemical and physicochemical processes contributing to the removal of endocrine-disrupting chemicals and pharmaceuticals by the aquatic ascomycete Phoma sp. UHH 5-1-03
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-015-7113-0
  contributor:
    fullname: Hofmann
– volume: 79
  start-page: 438
  year: 2002
  ident: B86
  article-title: Fermentation strategies for improved heterologous expression of laccase in Pichia pastoris
  publication-title: Biotechnol. Bioeng.
  doi: 10.1002/bit.10297
  contributor:
    fullname: Hong
– volume: 179
  start-page: 54
  year: 2015
  ident: B275
  article-title: Cloning and functional analysis of a laccase gene during fruiting body formation in Hypsizygus marmoreus
  publication-title: Microbiol. Res.
  doi: 10.1016/j.micres.2015.06.005
  contributor:
    fullname: Zhang
– volume: 70
  start-page: 6379
  year: 2004
  ident: B5
  article-title: Highly efficient production of laccase by the basidiomycete Pycnoporus cinnabarinus
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.70.11.6379-6384.2004
  contributor:
    fullname: Alves
– volume: 5
  start-page: 46
  year: 2013
  ident: B25
  article-title: Stabilized laccases as heterogeneous bioelectrocatalysts
  publication-title: ChemCatChem
  doi: 10.1002/cctc.201200611
  contributor:
    fullname: Betancor
– volume: 75
  start-page: 1003
  year: 2009
  ident: B248
  article-title: Degradation of tetracycline and oxytetracycline by crude lignin peroxidase prepared from Phanerochaete chrysosporium – A white rot fungus
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2009.01.052
  contributor:
    fullname: Wen
– volume: 33
  start-page: 25
  year: 2015
  ident: B145
  article-title: Laccase engineering: from rational design to directed evolution
  publication-title: Biotechnol. Adv.
  doi: 10.1016/j.biotechadv.2014.12.007
  contributor:
    fullname: Mate
– volume: 6
  start-page: 1558
  ident: B262
  article-title: Laccase production and differential transcription of laccase genes in Cerrena sp. in response to metal ions, aromatic compounds, and nutrients
  publication-title: Front. Microbiol.
  doi: 10.3389/fmicb.2015.01558
  contributor:
    fullname: Yang
– volume: 8
  start-page: e79307
  year: 2013
  ident: B271
  article-title: Enhancing the laccase production and laccase gene expression in the white-rot fungus Trametes velutina 5930 with great potential for biotechnological applications by different metal Ions and aromatic compounds
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0079307
  contributor:
    fullname: Yang
– volume: 102
  start-page: 1656
  year: 2011
  ident: B28
  article-title: Conjugation of laccase from the white rot fungus Trametes versicolor to chitosan and its utilization for the elimination of triclosan
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2010.09.080
  contributor:
    fullname: Cabana
– volume: 50
  start-page: 72
  year: 2010
  ident: B125
  article-title: Two laccase isoforms of the basidiomycete Cerrena unicolor VKMF-3196. Induction, isolation and properties
  publication-title: J. Basic Microbiol.
  doi: 10.1002/jobm.200900382
  contributor:
    fullname: Lisova
– volume: 520
  start-page: 869
  ident: B97
  article-title: Cross-linked carbon nanotubes-based biocatalytic membranes for micro-pollutants degradation: performance, stability, and regeneration
  publication-title: J. Membr. Sci.
  doi: 10.1016/j.memsci.2016.08.056
  contributor:
    fullname: Ji
– volume: 14
  start-page: 7
  year: 2016
  ident: B71
  article-title: Studies on the laccase-mediated decolorization, kinetic, and microtoxicity of some synthetic azo dyes
  publication-title: J. Environ. Health Sci. Eng.
  doi: 10.1186/s40201-016-0248-9
  contributor:
    fullname: Forootanfar
– year: 2016
  ident: B146
  article-title: Laccase: a multi-purpose biocatalyst at the forefront of biotechnology
  publication-title: Microb. Biotechnol.
  doi: 10.1111/1751-7915.12422
  contributor:
    fullname: Mate
– volume: 52
  start-page: 2344
  year: 2014
  ident: B48
  article-title: The potential of Cerrena unicolor laccase immobilized on mesoporous silica beads for removal of organic micropollutants in wastewaters
  publication-title: Desalin. Water Treat.
  doi: 10.1080/19443994.2013.877851
  contributor:
    fullname: Debaste
– volume: 223
  start-page: 42
  year: 2016
  ident: B65
  article-title: Diffusional and transcriptional mechanisms involved in laccases production by Pleurotus ostreatus CP50
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2016.02.029
  contributor:
    fullname: Fernandez-Alejandre
– volume: 336
  start-page: 1715
  year: 2012
  ident: B69
  article-title: The Paleozoic origin of enzymatic lignin decomposition reconstructed from 31 fungal genomes
  publication-title: Science
  doi: 10.1126/science.1221748
  contributor:
    fullname: Floudas
– volume: 148
  start-page: 1
  year: 2016
  ident: B273
  article-title: Oxidation of polycyclic aromatic hydrocarbons using Bacillus subtilis CotA with high laccase activity and copper independence
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2016.01.019
  contributor:
    fullname: Zeng
– volume: 68
  start-page: 117
  year: 2011
  ident: B55
  article-title: Structure–function relationship among bacterial, fungal and plant laccases
  publication-title: J. Mol. Catal. B Enzym.
  doi: 10.1016/j.molcatb.2010.11.002
  contributor:
    fullname: Dwivedi
– volume: 23
  start-page: 16904
  year: 2016
  ident: B135
  article-title: Perspectives of using fungi as bioresource for bioremediation of pesticides in the environment: a critical review
  publication-title: Environ. Sci. Pollut. Res.
  doi: 10.1007/s11356-016-7003-8
  contributor:
    fullname: Maqbool
– volume: 65
  start-page: 1
  ident: B264
  article-title: Cross-linked enzyme aggregates of Cerrena laccase: preparation, enhanced NaCl tolerance and decolorization of Remazol Brilliant Blue Reactive
  publication-title: J. Taiwan Inst. Chem. Eng.
  doi: 10.1016/j.jtice.2016.04.025
  contributor:
    fullname: Yang
– volume: 28
  start-page: 63
  year: 2010
  ident: B193
  article-title: Designer laccases: a vogue for high-potential fungal enzymes?
  publication-title: Trends Biotechnol.
  doi: 10.1016/j.tibtech.2009.11.001
  contributor:
    fullname: Rodgers
– volume: 117
  start-page: 52
  year: 2013
  ident: B160
  article-title: Effective induction of pblac1 laccase by copper ion in Polyporus brumalis ibrc05015
  publication-title: Fungal Biol.
  doi: 10.1016/j.funbio.2012.11.005
  contributor:
    fullname: Nakade
– volume: 48
  start-page: 195
  year: 2011
  ident: B110
  article-title: Potential applications of laccase-mediated coupling and grafting reactions: a review
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2010.11.007
  contributor:
    fullname: Kudanga
– volume: 92
  start-page: 467
  year: 2011
  ident: B206
  article-title: Characteristic features and biotechnological applications of cross-linked enzyme aggregates (CLEAs)
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-011-3554-2
  contributor:
    fullname: Sheldon
– volume: 481
  start-page: 90
  year: 2014
  ident: B232
  article-title: Characterization of combined cross-linked enzyme aggregates from laccase, versatile peroxidase and glucose oxidase, and their utilization for the elimination of pharmaceuticals
  publication-title: Sci. Total Environ.
  doi: 10.1016/j.scitotenv.2014.01.132
  contributor:
    fullname: Touahar
– volume: 141
  start-page: 152
  year: 2013
  ident: B251
  article-title: Application parameters of laccase-mediator systems for treatment of sulfonamide antibiotics
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2013.02.093
  contributor:
    fullname: Weng
– volume: 8
  start-page: 125
  year: 2010
  ident: B234
  article-title: Biodegradation characteristics of pharmaceutical substances by whole fungal culture Trametes versicolor and its laccase
  publication-title: J. Water Environ. Technol.
  doi: 10.2965/jwet.2010.125
  contributor:
    fullname: Tran
– volume: 45
  start-page: 9
  year: 2004
  ident: B84
  article-title: The laccase gene family in Coprinopsis cinerea (Coprinus cinereus)
  publication-title: Curr. Genet.
  doi: 10.1007/s00294-003-0452-x
  contributor:
    fullname: Hoegger
– volume: 8
  start-page: e65633
  year: 2013
  ident: B190
  article-title: Laccase versus laccase-like multi-copper oxidase: a comparative study of similar enzymes with diverse substrate spectra
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0065633
  contributor:
    fullname: Reiss
– volume: 22
  start-page: 16868
  year: 2015
  ident: B214
  article-title: Removal of sulfadimethoxine in soil mediated by extracellular oxidoreductases
  publication-title: Environ. Sci. Pollut. Res.
  doi: 10.1007/s11356-015-4893-9
  contributor:
    fullname: Singh
– volume: 6
  start-page: 15
  year: 2016
  ident: B236
  article-title: Bioprospecting and biotechnological applications of fungal laccase
  publication-title: 3 Biotech
  doi: 10.1007/s13205-015-0316-3
  contributor:
    fullname: Upadhyay
– volume: 9
  start-page: e93912
  year: 2014
  ident: B77
  article-title: Engineering the expression and characterization of two novel laccase isoenzymes from Coprinus comatus in Pichia pastoris by fusing an additional ten amino acids tag at N-terminus
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0093912
  contributor:
    fullname: Gu
– start-page: 215
  year: 2012
  ident: B150
  article-title: Biodegradation of oxytetracycline by Pleurotus ostreatus mycelium: a mycoremediation technique
  publication-title: J. Hazard. Mater
  doi: 10.1016/j.jhazmat.2012.02.056
  contributor:
    fullname: Migliore
– volume: 61
  start-page: 127
  year: 2015
  ident: B224
  article-title: Effects of calmodulin on expression of lignin-modifying enzymes in Pleurotus ostreatus
  publication-title: Curr. Genet.
  doi: 10.1007/s00294-014-0460-z
  contributor:
    fullname: Suetomi
– volume: 37
  start-page: 1091
  year: 2010
  ident: B58
  article-title: Effect of aromatic compounds on the production of laccase and manganese peroxidase by white-rot basidiomycetes
  publication-title: J. Ind. Microbiol. Biotechnol.
  doi: 10.1007/s10295-010-0757-y
  contributor:
    fullname: Elisashvili
– volume: 5
  start-page: 250
  year: 2016
  ident: B34
  article-title: Product formation from phenolic compounds removal by laccases: a review
  publication-title: Environ. Technol. Innov.
  doi: 10.1016/j.eti.2016.04.001
  contributor:
    fullname: Catherine
– volume: 30
  start-page: 112
  year: 2016
  ident: B204
  article-title: Fungal decolouration and degradation of azo dyes: a review
  publication-title: Fungal Biol. Rev.
  doi: 10.1016/j.fbr.2016.06.003
  contributor:
    fullname: Sen
– volume: 35
  start-page: 3082
  year: 2014
  ident: B184
  article-title: Potential of newly isolated wild Streptomyces strains as agents for the biodegradation of a recalcitrant pharmaceutical, carbamazepine
  publication-title: Environ. Technol.
  doi: 10.1080/09593330.2014.931468
  contributor:
    fullname: Popa
– volume: 182
  start-page: 620
  year: 2016
  ident: B243
  article-title: Removal of pharmaceuticals and personal care products (PPCPs) from wastewater: a review
  publication-title: J. Environ. Manage.
  doi: 10.1016/j.jenvman.2016.07.049
  contributor:
    fullname: Wang
– volume: 90
  start-page: 1
  year: 2016
  ident: B104
  article-title: Enzymatic modification of polysaccharides: mechanisms, properties, and potential applications: a review
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2016.04.004
  contributor:
    fullname: Karaki
– volume: 97
  start-page: 107
  year: 2015
  ident: B186
  article-title: Elimination and detoxification of sulfathiazole and sulfamethoxazole assisted by laccase immobilized on porous silica beads
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2014.10.018
  contributor:
    fullname: Rahmani
– volume: 317
  start-page: 81
  year: 2016
  ident: B207
  article-title: Laccase-catalyzed removal of the antimicrobials chlorophene and dichlorophen from water: reaction kinetics, pathway and toxicity evaluation
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2016.05.064
  contributor:
    fullname: Shi
– volume: 8
  start-page: e73282
  year: 2013
  ident: B32
  article-title: Non-additive transcriptional profiles underlie dikaryotic superiority in Pleurotus ostreatus laccase activity
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0073282
  contributor:
    fullname: Castanera
– volume: 75
  start-page: 417
  year: 2009
  ident: B115
  article-title: Antibiotics in the aquatic environment – a review – Part II
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2008.11.086
  contributor:
    fullname: Kümmerer
– volume: 362
  start-page: fnv072
  year: 2015
  ident: B174
  article-title: Laccase-like enzyme activities from chlorophycean green algae with potential for bioconversion of phenolic pollutants
  publication-title: FEMS Microbiol. Lett.
  doi: 10.1093/femsle/fnv072
  contributor:
    fullname: Otto
– volume: 37
  start-page: 1387
  year: 2002
  ident: B3
  article-title: Immobilization of wood-rotting fungi laccases on modified cellulose and acrylic carriers
  publication-title: Process Biochem.
  doi: 10.1016/S0032-9592(02)00023-7
  contributor:
    fullname: Al-Adhami
– volume: 67
  start-page: 369
  year: 2010
  ident: B75
  article-title: Laccases: a never-ending story
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-009-0169-1
  contributor:
    fullname: Giardina
– volume: 106
  start-page: 249
  year: 2009
  ident: B68
  article-title: Selection of Trichoderma strains capable of increasing laccase production by Pleurotus ostreatus and Agaricus bisporus in dual cultures
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/j.1365-2672.2008.03998.x
  contributor:
    fullname: Flores
– volume: 157
  start-page: 304
  year: 2012
  ident: B108
  article-title: A chloride tolerant laccase from the plant pathogen ascomycete Botrytis aclada expressed at high levels in Pichia pastoris
  publication-title: J. Biotechnol.
  doi: 10.1016/j.jbiotec.2011.11.021
  contributor:
    fullname: Kittl
– volume: 119
  start-page: 90
  year: 2015
  ident: B129
  article-title: Identification of new transformation products during enzymatic treatment of tetracycline and erythromycin antibiotics at laboratory scale by an on-line turbulent flow liquid-chromatography coupled to a high resolution mass spectrometer LTQ-Orbitrap
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2014.05.072
  contributor:
    fullname: Llorca
– volume: 95
  start-page: 25
  ident: B165
  article-title: Continuous biotransformation of bisphenol A and diclofenac by laccase in an enzymatic membrane reactor
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2014.05.017
  contributor:
    fullname: Nguyen
– volume: 21
  start-page: 1017
  ident: B263
  article-title: Laccase gene family in Cerrena sp. HYB07: sequences, heterologous expression and transcriptional analysis
  publication-title: Molecules
  doi: 10.3390/molecules21081017
  contributor:
    fullname: Yang
– volume: 552
  start-page: 98
  year: 2014
  ident: B41
  article-title: Overexpression of the OsChI1 gene, encoding a putative laccase precursor, increases tolerance to drought and salinity stress in transgenic Arabidopsis
  publication-title: Gene
  doi: 10.1016/j.gene.2014.09.018
  contributor:
    fullname: Cho
– volume: 279
  start-page: 203
  year: 2014
  ident: B208
  article-title: Removal of sulfonamide antibiotics by oriented immobilized laccase on Fe3O4 nanoparticles with natural mediators
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2014.06.070
  contributor:
    fullname: Shi
– volume: 226
  start-page: 251
  year: 2015
  ident: B73
  article-title: Biotransformation of endocrine-disrupting compounds in groundwater: bisphenol A, nonylphenol, ethynylestradiol and triclosan by a laccase cocktail from Pycnoporus sanguineus CS43
  publication-title: Water Air Soil Pollut.
  doi: 10.1007/s11270-015-2514-3
  contributor:
    fullname: Garcia-Morales
– volume: 502
  start-page: 11
  ident: B98
  article-title: Biocatalytic degradation of carbamazepine with immobilized laccase-mediator membrane hybrid reactor
  publication-title: J. Membr. Sci.
  doi: 10.1016/j.memsci.2015.12.043
  contributor:
    fullname: Ji
– volume: 224
  start-page: 1185
  year: 2006
  ident: B122
  article-title: Involvement of AtLAC15 in lignin synthesis in seeds and in root elongation of Arabidopsis
  publication-title: Planta
  doi: 10.1007/s00425-006-0300-6
  contributor:
    fullname: Liang
– volume: 88
  start-page: 169
  ident: B166
  article-title: Removal of pharmaceuticals, steroid hormones, phytoestrogens, UV-filters, industrial chemicals and pesticides by Trametes versicolor: role of biosorption and biodegradation
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2013.12.017
  contributor:
    fullname: Nguyen
– volume: 10
  start-page: e0127714
  year: 2015
  ident: B265
  article-title: Laccase-catalyzed decolorization of malachite green: performance optimization and degradation mechanism
  publication-title: PLoS ONE
  doi: 10.1371/journal.pone.0127714
  contributor:
    fullname: Yang
– volume: 5
  start-page: 318
  year: 2012
  ident: B96
  article-title: Laccase-catalysed oxidations of naturally occurring phenols: from in vivo biosynthetic pathways to green synthetic applications
  publication-title: Microb. Biotechnol.
  doi: 10.1111/j.1751-7915.2011.00273.x
  contributor:
    fullname: Jeon
– volume: 79
  start-page: 459
  year: 2015
  ident: B154
  article-title: Fungus Cerrena unicolor as an effective source of new antiviral, immunomodulatory, and anticancer compounds
  publication-title: Int. J. Biol. Macromol.
  doi: 10.1016/j.ijbiomac.2015.05.015
  contributor:
    fullname: Mizerska-Dudka
– volume: 149
  start-page: 373
  year: 2016
  ident: B142
  article-title: Biodegradation of phenolic compounds by Basidiomycota and its phenol oxidases: a review
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2016.01.022
  contributor:
    fullname: Martinkova
– volume: 51
  start-page: 68
  year: 2010
  ident: B132
  article-title: Effect of Cu2+, Mn2+ and aromatic compounds on the production of laccase isoforms by Coprinus comatus
  publication-title: Mycoscience
  doi: 10.1007/S10267-009-0002-6
  contributor:
    fullname: Lu
– volume: 200
  start-page: 81
  year: 2016
  ident: B113
  article-title: Towards high potential magnetic biocatalysts for on-demand elimination of pharmaceuticals
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2015.09.100
  contributor:
    fullname: Kumar
– volume: 47
  start-page: 6916
  year: 2013
  ident: B79
  article-title: Covalent binding of sulfamethazine to natural and synthetic humic acids: assessing laccase catalysis and covalent bond stability
  publication-title: Environ. Sci. Technol.
  doi: 10.1021/es3044592
  contributor:
    fullname: Gulkowska
– volume: 180
  start-page: 228
  year: 2016
  ident: B238
  article-title: Biological removal of pharmaceutical compounds using white-rot fungi with concomitant FAME production of the residual biomass
  publication-title: J. Environ. Manage.
  doi: 10.1016/j.jenvman.2016.05.035
  contributor:
    fullname: Vasiliadou
– volume: 52
  start-page: 431
  year: 2011
  ident: B157
  article-title: Molecular breeding of a novel Coprinopsis cinerea strain possessing a heterologous laccase gene, lccK, driven by a constitutive promoter
  publication-title: Mycoscience
  doi: 10.1007/S10267-011-0122-7
  contributor:
    fullname: Muraguchi
– volume: 30
  start-page: 2005
  year: 2014
  ident: B227
  article-title: A novel breeding strategy for new strains of Hypsizygus marmoreus and Grifola frondosa based on ligninolytic enzymes
  publication-title: World J. Microbiol. Biotechnol.
  doi: 10.1007/s11274-014-1624-1
  contributor:
    fullname: Sun
– volume: 17
  start-page: 946
  year: 2012
  ident: B241
  article-title: The effects of N+ ion implantation mutagenesis on the laccase production of Ceriporiopsis subvermispora
  publication-title: Biotechnol. Bioprocess Eng.
  doi: 10.1007/s12257-012-0125-z
  contributor:
    fullname: Wang
– volume: 110
  start-page: 181
  year: 2016
  ident: B45
  article-title: Degradation of bisphenol A by different fungal laccases and identification of its degradation products
  publication-title: Int. Biodeterior. Biodegradation
  doi: 10.1016/j.ibiod.2016.03.017
  contributor:
    fullname: Daâssi
– volume: 147
  start-page: 667
  year: 2013
  ident: B233
  article-title: Removal of the insect repellent N,N-diethyl-m-toluamide (DEET) by laccase-mediated systems
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2013.08.113
  contributor:
    fullname: Tran
– volume: 100
  start-page: 4885
  year: 2016
  ident: B151
  article-title: Targeted synthesis of novel α-lactam antibiotics by laccase-catalyzed reaction of aromatic substrates selected by pre-testing for their antimicrobial and cytotoxic activity
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-016-7288-z
  contributor:
    fullname: Mikolasch
– volume: 167
  start-page: 169
  ident: B164
  article-title: The effects of mediator and granular activated carbon addition on degradation of trace organic contaminants by an enzymatic membrane reactor
  publication-title: Bioresour. Technol.
  doi: 10.1016/j.biortech.2014.05.125
  contributor:
    fullname: Nguyen
– volume: 67
  start-page: 97
  year: 2012
  ident: B67
  article-title: Biodeinking of flexographic inks by fungal laccases using synthetic and natural mediators
  publication-title: Biochem. Eng. J.
  doi: 10.1016/j.bej.2012.05.010
  contributor:
    fullname: Fillat
– volume: 307
  start-page: 350
  year: 2016
  ident: B51
  article-title: Simultaneous removal and degradation characteristics of sulfonamide, tetracycline, and quinolone antibiotics by laccase-mediated oxidation coupled with soil adsorption
  publication-title: J. Hazard. Mater.
  doi: 10.1016/j.jhazmat.2015.12.062
  contributor:
    fullname: Ding
– volume: 82
  start-page: 887
  year: 2014
  ident: B191
  article-title: Phenotypic comparisons of consensus variants versus laboratory resurrections of Precambrian proteins
  publication-title: Proteins
  doi: 10.1002/prot.24575
  contributor:
    fullname: Risso
– volume: 72
  start-page: 869
  year: 2015
  ident: B101
  article-title: Electron transfer and reaction mechanism of laccases
  publication-title: Cell. Mol. Life Sci.
  doi: 10.1007/s00018-014-1826-6
  contributor:
    fullname: Jones
– volume: 10
  start-page: 309
  year: 2011
  ident: B212
  article-title: Laccase from prokaryotes: a new source for an old enzyme
  publication-title: Rev. Environ. Sci. Biotechnol.
  doi: 10.1007/s11157-011-9257-4
  contributor:
    fullname: Singh
– volume: 233
  start-page: 439
  year: 2011
  ident: B235
  article-title: The laccase multigene family in Arabidopsis thaliana: towards addressing the mystery of their gene function(s)
  publication-title: Planta
  doi: 10.1007/s00425-010-1298-3
  contributor:
    fullname: Turlapati
– volume: 78
  start-page: 474
  ident: B136
  article-title: White-rot fungus-mediated degradation of the analgesic ketoprofen and identification of intermediates by HPLC–DAD–MS and NMR
  publication-title: Chemosphere
  doi: 10.1016/j.chemosphere.2009.10.009
  contributor:
    fullname: Marco-Urrea
– volume: 84
  start-page: 289
  year: 2003
  ident: B237
  article-title: Evolutionary and structural diversity of fungal laccases
  publication-title: Antonie van Leeuwenhoek
  doi: 10.1023/A:1026070122451
  contributor:
    fullname: Valderrama
– volume: 71
  start-page: 493
  year: 2006
  ident: B254
  article-title: Cloning of novel laccase isozyme genes from Trametes sp. AH28-2 and analyses of their differential expression
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-005-0188-2
  contributor:
    fullname: Xiao
SSID ssj0000402000
Score 2.5951216
SecondaryResourceType review_article
Snippet Laccases are a family of copper-containing oxidases with important applications in bioremediation and other various industrial and biotechnological areas....
SourceID doaj
pubmedcentral
proquest
crossref
pubmed
SourceType Open Website
Open Access Repository
Aggregation Database
Index Database
StartPage 832
SubjectTerms antibiotics
bioremediation
expression regulation
laccase
Microbiology
PPCPs
production
SummonAdditionalLinks – databaseName: Directory of Open Access Journals
  dbid: DOA
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwrV3PSxwxFA5FKPQiaq2u1ZKCF6FDM_kxk3hTWVmKiojCngz5iXuZFXcX2v_el2RXZqXQS29DZph5fG-SfG_em-8hdBwjTLGGxkp6YytuDK9sbEnl66AI9Vxykf53vr5pRg_811iMe62-Uk1YkQcuwP2kUXDDfa2EE5xGoxoVHHOUBlVTakJefYnqBVN5DU5hESElLwlRmAI3TZxNpVxJslAyurYPZbn-v3HM96WSvb3ncgttLkkjPivGbqMPodtBH0sbyT-f0eOVAYRmYXaKb4uAK4D9Aw9_L4tcO3xXOs7nYdN5fNZLW-NJh2-f-l-2MdzZJxGJ0m9pFz1cDu8vRtWyb0LleEPnVRRBubqVztXUM5MmHVPEUA5rGVfMt1bCxm8hOHIu2JZRb6iQLDReEcuNY1_QRjftwj7CTNpIQmBKWs5j20pvBRwa1khTA1caoJMVivq5yGNoCCsS4jojrhPiOiM-QOcJ5rfrkrB1HgB366W79b_cPUDfV07SMBFSdsN0YbqYaWA2QA2Bv4gB2itOe3sUlUmHXoK57Zo712xZP9NNnrLYtuAMoi5y8D-M_4o-JThS8UHdHKKN-csiHAGnmdtv-fV9BRrq9tU
  priority: 102
  providerName: Directory of Open Access Journals
– databaseName: Scholars Portal Open Access Journals
  dbid: M48
  link: http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1ba9RAFD5oRfClWK_xxgi-CEaSuSQzgkgrLUVUirjQJ4e52oWS1d0ttP_ec5Js3ZV98i1MMkn4zpzMdzJnvgPwKmd0sYbnUkfnS-mcLH1uqzLWyVQ8Si0V7Xf-8rU5nshPp-r07_boEcDF1tCO6klN5udvL39ffUCHf08RJ863aIFp8JSlRWqEOEJvwi0uMU6nRL6R7PffZQqVqmpYq9zakZSBNSmWk0jk2jTVq_lvo6D_ZlKuTU1Hd2F35JRsfxgEe3Ajdffg9lBl8uo-_PjsEMBFWrxjJ4O-K9riDTu8HHNgO_ZtKEjfN7susv21VW027djJ2fqPb4Z3jqQxMZRjegCTo8PvH4_LsaxCGWTDl2VWyYS61SHUPApHPilM5bjET500IrZeIy_wGDuFkHwreHRcaZGaaCovXRAPYaebdekxMKF9rlISRnspc9vq6BUeOtFoVyOVKuD1CkX7a1DPsBh1EPi2B98S-LYHv4ADgvn6OtK97htm8592dCPLs5JOxtqooCTPzjQmBRE4T6bm3KUCXq6MZNFPaPHDdWl2sbBIfJA5Ir1RBTwajHb9qJXRC2g3zLnxLptnuulZr8WtpMCgrHry3z2fwh3CgBIS6uYZ7CznF-k58pylf9EP3z_yEf8f
  priority: 102
  providerName: Scholars Portal
Title Laccases: Production, Expression Regulation, and Applications in Pharmaceutical Biodegradation
URI https://www.ncbi.nlm.nih.gov/pubmed/28559880
https://search.proquest.com/docview/1904235125
https://pubmed.ncbi.nlm.nih.gov/PMC5432550
https://doaj.org/article/2f54a4d195c542fa969ec3c22e9122ae
Volume 8
hasFullText 1
inHoldings 1
isFullTextHit
isPrint
link http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1La9wwEB6SQKGX0nfdR3Chl0Kd2HrYUm9pSBpKtyylgT1V6NksNNqQ3UD77zuS7eAtPfUijPwS34ykGWn0DcCbELCLtSRUwmlTMa1ZZUJXV67xsiaOCcbTeefZl_bsnH1a8MUO8PEsTA7at2Z5EH9eHsTlRY6tvLq0h2Oc2OF8dswZJYleexd2UUEnLnoefpNHVNf9liQ6YBIltLQmRXEltkLU4EQALBIxeeKCnMxGmbT_X5bm3wGTkxno9D7cG0zH8qhv4gPY8fEh3OmTSf5-BN8_a8Rp7dfvy3lP44qQvytPfg2hrrH82uedz9U6uvJosnldLmM5v5iub5f4ZZeoJPqsS4_h_PTk2_FZNWRPqCxryaYK3EvbdMLahjiqU9ejstaE4YjGJHWdETj9G3SRrPWmo8RpwgX1rZO1YdrSJ7AXV9E_g5IKE2rvqRSGsdB1whmOl5q2QjdoMRXwdkRRXfUkGQqdiwS-yuCrBL7K4BfwIcF8-1yit84Vq-sfahCyIoEzzVwjueWMBC1b6S21hHjZEKJ9Aa9HISnsDmmPQ0e_ulkrtG_QQEQrhhfwtBfa7a9GoRfQbYlzqy3bd1ADM-X2oHHP__vNF3A3YZDiDpr2Jextrm_8KzRnNmY_LwNg-XHRYDljYj8r9B_i5Pnt
link.rule.ids 230,315,730,783,787,867,888,2109,24330,27936,27937,53804,53806
linkProvider National Library of Medicine
linkToHtml http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Lb9QwEB6VIkQvvAvLM0hckMg28SOxuZWq1QK71Qq1qCcsv0JXpdmquysBv56xk1TZigvcIufl-PPY38TjbwDeVBWaWEGqVDhtUqY1S01VZqnLvcyIY4LxsN95cliMjtmnE36yAbzbCxOD9q2ZDesf58N6dhpjKy_O7U4XJ7YznexxRkmQ174BN9FeM9Zz0uMAHHyiLGsWJdEFk4jRzJoQxxX0CrEPBwlgEaTJgxpkbz6Ksv1_45rXQyZ7c9DBXfja1b4JPTkbrpZmaH9fE3b858-7B3daVprsNqfvw4avH8CtJk_lr4fwbawRgoVfvE-mjUIsovku2f_ZRtHWyZcmpX0s1rVLdnvr4smsTqan_V_nCT7ZBZWKJqHTIzg-2D_aG6VtYobUsoIs04p7afNSWJsTR3WwaiozTRgOlkxSVxqBzMKg92WtNyUlThMuqC-czAzTlm7DZj2v_RNIqDBV5j2VwjBWlaVwhuOhpoXQOZKxAbzt4FEXjf6GQr8loKoiqiqgqiKqA_gQ8Lu6Lihnx4L55XfVNrAiFWeauVxyyxmptCykt9QS4mVOiPYDeN2hr9DSwvKJrv18tVBInZB7IkHiA3jc9IarV3W9aQDlWj9Zq8v6GUQ_qnm3aD_97ztfwe3R0WSsxh8PPz-DrdAeIbwhL57D5vJy5V8ga1qal9FG_gCaMxkq
linkToPdf http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1Jb9QwFLagCMSFfQlrkLggkZnES2JzK6WjAm01QlSqOGB5pSNoZtSZkYBfz7OdVJmKU2-Rs_t7z34v_vI9hF57Dy5WY19wq3RBlaKF9k1Z2MqJElvKKQv_Ox8c1ntH9NMxOx6U-oqkfaNno_bX6aidnURu5eLUjHue2Hh6sMMowUFee2H9-Cq6Bj5b1oNEPQ7CIS8qy7QwCWmYAJxmRgcuV9AsBDsOMsA8yJMHRcjBnBSl-_8Xb16kTQ7moclt9K1_g0Q_-Tlar_TI_L0g7nipV7yDbnXRab6dDrmLrrj2Hrqe6lX-uY--7yuAYumW7_JpUooFVN_mu787Nm2bf0ml7WOzam2-PVgfz2dtPj0ZfkLP4co2qFWkwk4P0NFk9-vOXtEVaCgMrfGq8MwJUzXcmApbooJ3E1EqTGHQpILYRnOIMDRkYcY43RBsFWacuNqKUlNlyEO01c5b9xjlhGtfOkcE15T6puFWM9hUpOaqgqAsQ296iOQi6XBIyF8CsjIiKwOyMiKbofcBw_PjgoJ2bJif_ZBdJ0vsGVXUVoIZRrFXohbOEIOxExXGymXoVW8BEjwuLKOo1s3XSwkhFMSgECixDD1KFnF-q96iMtRs2MrGs2zuAQuIqt4d4k8ufeZLdGP6YSL3Px5-fopuhu4ILIeqfoa2Vmdr9xyCp5V-Ed3kH1q-G6o
openUrl ctx_ver=Z39.88-2004&ctx_enc=info%3Aofi%2Fenc%3AUTF-8&rfr_id=info%3Asid%2Fsummon.serialssolutions.com&rft_val_fmt=info%3Aofi%2Ffmt%3Akev%3Amtx%3Ajournal&rft.genre=article&rft.atitle=Laccases%3A+Production%2C+Expression+Regulation%2C+and+Applications+in+Pharmaceutical+Biodegradation&rft.jtitle=Frontiers+in+microbiology&rft.au=Yang%2C+Jie&rft.au=Li%2C+Wenjuan&rft.au=Ng%2C+Tzi+Bun&rft.au=Deng%2C+Xiangzhen&rft.date=2017-05-16&rft.pub=Frontiers+Media+S.A&rft.eissn=1664-302X&rft.volume=8&rft_id=info:doi/10.3389%2Ffmicb.2017.00832&rft_id=info%3Apmid%2F28559880&rft.externalDBID=PMC5432550
thumbnail_l http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=1664-302X&client=summon
thumbnail_m http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=1664-302X&client=summon
thumbnail_s http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=1664-302X&client=summon