Identification of Copper-Containing Oxidoreductases in the Secretomes of Three Colletotrichum Species with a Focus on Copper Radical Oxidases for the Biocatalytic Production of Fatty Aldehydes
Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analys...
Saved in:
| Published in | Applied and environmental microbiology Vol. 87; no. 24; p. e0152621 |
|---|---|
| Main Authors | , , , , , , , , , , , , , |
| Format | Journal Article |
| Language | English |
| Published |
United States
American Society for Microbiology
24.11.2021
|
| Subjects | |
| Online Access | Get full text |
Cover
Loading…
| Abstract | Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species (C. graminicola, C. tabacum, and C. destructivum) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plant-biomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CRO-AlcOx were thus expressed in Pichia pastoris, and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C
and C
alcohols into their corresponding fragrant aldehydes.
In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for their use as flavor and fragrance ingredients. Copper radical alcohol oxidases (CRO-AlcOx) have the potential to become platform enzymes for the oxidation of alcohols to aldehydes. However, the secretion of CRO-AlcOx by natural fungal strains has never been explored, while the use of crude fungal secretomes is an appealing approach for industrial applications to alleviate various costs pertaining to biocatalyst production. While investigating this primary objective, the secretomics studies revealed unexpected results showing that under the oxidative stress conditions we probed, Colletotrichum species can secrete a broad diversity of copper-containing enzymes (laccases, sugar oxidoreductases, and lytic polysaccharide monooxygenases [LPMOs]) usually assigned to "plant cell wall degradation," despite the absence of any plant-biomass mimicking compound. However, in these conditions, only small amounts of CRO-AlcOx were secreted, pointing out recombinant expression as the most promising path for their biocatalytic application. |
|---|---|
| AbstractList | Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species (C. graminicola, C. tabacum, and C. destructivum) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plant-biomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CRO-AlcOx were thus expressed in Pichia pastoris, and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C6 and C8 alcohols into their corresponding fragrant aldehydes. IMPORTANCE In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for their use as flavor and fragrance ingredients. Copper radical alcohol oxidases (CRO-AlcOx) have the potential to become platform enzymes for the oxidation of alcohols to aldehydes. However, the secretion of CRO-AlcOx by natural fungal strains has never been explored, while the use of crude fungal secretomes is an appealing approach for industrial applications to alleviate various costs pertaining to biocatalyst production. While investigating this primary objective, the secretomics studies revealed unexpected results showing that under the oxidative stress conditions we probed, Colletotrichum species can secrete a broad diversity of copper-containing enzymes (laccases, sugar oxidoreductases, and lytic polysaccharide monooxygenases [LPMOs]) usually assigned to “plant cell wall degradation,” despite the absence of any plant-biomass mimicking compound. However, in these conditions, only small amounts of CRO-AlcOx were secreted, pointing out recombinant expression as the most promising path for their biocatalytic application. Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species (C. graminicola, C. tabacum, and C. destructivum) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plant-biomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CRO-AlcOx were thus expressed in Pichia pastoris, and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C6 and C8 alcohols into their corresponding fragrant aldehydes. Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species (C. graminicola, C. tabacum, and C. destructivum) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plantbiomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CROAlcOx were thus expressed in Pichia pastoris, and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C-6 and C-8 alcohols into their corresponding fragrant aldehydes. Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species ( C. graminicola , C. tabacum , and C. destructivum ) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plant-biomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CRO-AlcOx were thus expressed in Pichia pastoris , and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C 6 and C 8 alcohols into their corresponding fragrant aldehydes. IMPORTANCE In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for their use as flavor and fragrance ingredients. Copper radical alcohol oxidases (CRO-AlcOx) have the potential to become platform enzymes for the oxidation of alcohols to aldehydes. However, the secretion of CRO-AlcOx by natural fungal strains has never been explored, while the use of crude fungal secretomes is an appealing approach for industrial applications to alleviate various costs pertaining to biocatalyst production. While investigating this primary objective, the secretomics studies revealed unexpected results showing that under the oxidative stress conditions we probed, Colletotrichum species can secrete a broad diversity of copper-containing enzymes (laccases, sugar oxidoreductases, and lytic polysaccharide monooxygenases [LPMOs]) usually assigned to “plant cell wall degradation,” despite the absence of any plant-biomass mimicking compound. However, in these conditions, only small amounts of CRO-AlcOx were secreted, pointing out recombinant expression as the most promising path for their biocatalytic application. Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species (C. graminicola, C. tabacum, and C. destructivum) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plant-biomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CRO-AlcOx were thus expressed in Pichia pastoris, and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C and C alcohols into their corresponding fragrant aldehydes. In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for their use as flavor and fragrance ingredients. Copper radical alcohol oxidases (CRO-AlcOx) have the potential to become platform enzymes for the oxidation of alcohols to aldehydes. However, the secretion of CRO-AlcOx by natural fungal strains has never been explored, while the use of crude fungal secretomes is an appealing approach for industrial applications to alleviate various costs pertaining to biocatalyst production. While investigating this primary objective, the secretomics studies revealed unexpected results showing that under the oxidative stress conditions we probed, Colletotrichum species can secrete a broad diversity of copper-containing enzymes (laccases, sugar oxidoreductases, and lytic polysaccharide monooxygenases [LPMOs]) usually assigned to "plant cell wall degradation," despite the absence of any plant-biomass mimicking compound. However, in these conditions, only small amounts of CRO-AlcOx were secreted, pointing out recombinant expression as the most promising path for their biocatalytic application. In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for their use as flavor and fragrance ingredients. Copper radical alcohol oxidases (CRO-AlcOx) have the potential to become platform enzymes for the oxidation of alcohols to aldehydes. ABSTRACT Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant fatty aldehydes. With the initial objective to investigate the secretion of CRO-AlcOx by natural fungal strains, we undertook time course analyses of the secretomes of three Colletotrichum species ( C. graminicola , C. tabacum , and C. destructivum ) using proteomics. The addition of a copper-manganese-ethanol mixture in the absence of any plant-biomass mimicking compounds to Colletotrichum cultures unexpectedly induced the secretion of up to 400 proteins, 29 to 52% of which were carbohydrate-active enzymes (CAZymes), including a wide diversity of copper-containing oxidoreductases from the auxiliary activities (AA) class (AA1, AA3, AA5, AA7, AA9, AA11, AA12, AA13, and AA16). Under these specific conditions, while a CRO-glyoxal oxidase from the AA5_1 subfamily was among the most abundantly secreted proteins, the targeted AA5_2 CRO-AlcOx were secreted at lower levels, suggesting heterologous expression as a more promising strategy for CRO-AlcOx production and utilization. C. tabacum and C. destructivum CRO-AlcOx were thus expressed in Pichia pastoris , and their preference toward both aromatic and aliphatic primary alcohols was assessed. The CRO-AlcOx from C. destructivum was further investigated in applied settings, revealing a full conversion of C 6 and C 8 alcohols into their corresponding fragrant aldehydes. IMPORTANCE In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for their use as flavor and fragrance ingredients. Copper radical alcohol oxidases (CRO-AlcOx) have the potential to become platform enzymes for the oxidation of alcohols to aldehydes. However, the secretion of CRO-AlcOx by natural fungal strains has never been explored, while the use of crude fungal secretomes is an appealing approach for industrial applications to alleviate various costs pertaining to biocatalyst production. While investigating this primary objective, the secretomics studies revealed unexpected results showing that under the oxidative stress conditions we probed, Colletotrichum species can secrete a broad diversity of copper-containing enzymes (laccases, sugar oxidoreductases, and lytic polysaccharide monooxygenases [LPMOs]) usually assigned to “plant cell wall degradation,” despite the absence of any plant-biomass mimicking compound. However, in these conditions, only small amounts of CRO-AlcOx were secreted, pointing out recombinant expression as the most promising path for their biocatalytic application. |
| Author | Ribeaucourt, David Lafond, Mickaël Navarro, David Correia, Lydie Oliveira Haon, Mireille Lapalu, Nicolas Bissaro, Bastien Berrin, Jean-Guy Drula, Elodie Saker, Safwan Henrissat, Bernard Lambert, Fanny Grisel, Sacha O'Connell, Richard J |
| Author_xml | – sequence: 1 givenname: David orcidid: 0000-0003-0927-1491 surname: Ribeaucourt fullname: Ribeaucourt, David organization: V. Mane Fils, Le Bar sur Loup, France – sequence: 2 givenname: Safwan surname: Saker fullname: Saker, Safwan organization: INRAE, Aix Marseille Université, UMR1163 Biodiversité et Biotechnologie Fongiques, Marseille, France – sequence: 3 givenname: David surname: Navarro fullname: Navarro, David organization: INRAE, Aix Marseille Université, UMR1163 Biodiversité et Biotechnologie Fongiques, Marseille, France – sequence: 4 givenname: Bastien surname: Bissaro fullname: Bissaro, Bastien organization: INRAE, Aix Marseille Université, UMR1163 Biodiversité et Biotechnologie Fongiques, Marseille, France – sequence: 5 givenname: Elodie surname: Drula fullname: Drula, Elodie organization: CNRS, Aix Marseille Université, UMR7257, AFMB, Marseille, France – sequence: 6 givenname: Lydie Oliveira surname: Correia fullname: Correia, Lydie Oliveira organization: Plateforme d'Analyse Protéomique de Paris Sud-Ouest, INRAE, AgroParisTech, Université Paris-Saclay, Micalis Institute, Jouy-en-Josas, France – sequence: 7 givenname: Mireille surname: Haon fullname: Haon, Mireille organization: INRAE, Aix Marseille Université, UMR1163 Biodiversité et Biotechnologie Fongiques, Marseille, France – sequence: 8 givenname: Sacha surname: Grisel fullname: Grisel, Sacha organization: INRAE, Aix Marseille Université, UMR1163 Biodiversité et Biotechnologie Fongiques, Marseille, France – sequence: 9 givenname: Nicolas surname: Lapalu fullname: Lapalu, Nicolas organization: UMR BIOGER, Institut National de la Recherche Agronomique, AgroParisTech, Université Paris-Saclay, Versailles, France – sequence: 10 givenname: Bernard surname: Henrissat fullname: Henrissat, Bernard organization: Department of Biological Sciences, King Abdulaziz University, Jeddah, Saudi Arabia – sequence: 11 givenname: Richard J surname: O'Connell fullname: O'Connell, Richard J organization: UMR BIOGER, Institut National de la Recherche Agronomique, AgroParisTech, Université Paris-Saclay, Versailles, France – sequence: 12 givenname: Fanny surname: Lambert fullname: Lambert, Fanny organization: V. Mane Fils, Le Bar sur Loup, France – sequence: 13 givenname: Mickaël orcidid: 0000-0003-2646-0286 surname: Lafond fullname: Lafond, Mickaël organization: Aix Marseille Université, CNRS, Marseille, France – sequence: 14 givenname: Jean-Guy orcidid: 0000-0001-7570-3745 surname: Berrin fullname: Berrin, Jean-Guy organization: INRAE, Aix Marseille Université, UMR1163 Biodiversité et Biotechnologie Fongiques, Marseille, France |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/34613753$$D View this record in MEDLINE/PubMed https://hal.science/hal-03619439$$DView record in HAL |
| BookMark | eNp1kl9rFDEUxQep2G31zWcJ-KLg1CQzk828COvStYWViq3PIZO56aTMJGuSqd1v149m9o-tFnwK3Jz7O4fLOcoOrLOQZa8JPiGE8o-z068nmFSU5ZQ8yyYE1zyvioIdZBOM6zqntMSH2VEINxjjEjP-IjssSkaKaVVMsvvzFmw02igZjbPIaTR3qxX4fO5slMYae40u7kzrPLSjijJAQMai2AG6BOUhuiFN0tpV5wHSct-nWfRGdeOALlegTPr_ZWKHJFo4NSax3Xug77JNxv3WYEvWzm_Rn41LgWS_jkahb95trPfxFjLGNZr1LXTrFsLL7LmWfYBX-_c4-7E4vZqf5cuLL-fz2TKXJccx1y2XZcUqQjRtJGnbhuOa0Ao0B9ZoOq2xVrpipC5pU2qqW9awWjIARXiBZXGcfdpxV2MzQKvS1bzsxcqbQfq1cNKIf3-s6cS1uxWcEUoZS4D3O0D3ZO1sthSbGS427kV9S5L23d7Mu58jhCgGExT0vbTgxiBoxTEmjHOcpG-fSG_c6G06haAMJyKv6TSpPuxUyrsQPOiHBASLTY1EqpHY1khQ8phVhoE-Av-jffP3YR7AfzpW_AaE8NUF |
| CitedBy_id | crossref_primary_10_1042_EBC20220124 crossref_primary_10_17221_52_2023_PPS crossref_primary_10_1016_j_copbio_2022_102842 crossref_primary_10_1128_aem_01931_23 crossref_primary_10_1021_acscatal_1c05334 crossref_primary_10_1016_j_engmic_2022_100037 crossref_primary_10_1039_D2RA04485D crossref_primary_10_1002_ffj_3739 crossref_primary_10_1016_j_biortech_2022_127814 crossref_primary_10_1128_aem_01014_24 crossref_primary_10_1093_gigascience_giae036 crossref_primary_10_1111_febs_16713 crossref_primary_10_1186_s13068_023_02406_z crossref_primary_10_1002_1873_3468_14632 crossref_primary_10_1021_acscatal_2c01956 |
| Cites_doi | 10.1016/j.nbt.2017.07.005 10.1186/1471-2164-13-57 10.1111/nph.13994 10.1021/acs.jafc.9b01131 10.1007/s11743-016-1867-y 10.1007/s10295-007-0203-y 10.1038/nchem.1536 10.1128/AEM.02826-17 10.1271/bbb.60.1598 10.1046/j.1365-2672.2003.01879.x 10.1038/s41598-020-75217-z 10.1128/AEM.01383-17 10.1021/bi00677a003 10.1016/j.enzmictec.2019.02.009 10.1017/S0953756202006494 10.1016/s0014-5793(99)01416-7 10.1146/annurev-micro-092611-150044 10.1016/j.biotechadv.2021.107787 10.1038/s41598-018-25016-4 10.1016/j.nbt.2020.11.006 10.1186/s12864-016-2917-6 10.1006/fgbi.1999.1143 10.1016/j.cub.2019.07.060 10.3390/jof7030185 10.1007/s00294-014-0471-9 10.1016/s0300-483x(03)00159-8 10.1093/nar/gkt1178 10.1016/j.nbt.2017.06.005 10.1021/acscatal.9b04727 10.1073/pnas.87.8.2936 10.3390/cells7090128 10.1007/s11274-017-2254-1 10.1007/s00438-004-1085-6 10.1038/ng.2372 10.1007/s00253-008-1596-x 10.1038/ncomms10197 10.1016/j.micres.2019.02.007 10.1021/acssuschemeng.0c07406 10.1021/jf9031958 10.1186/1754-6834-6-41 10.1186/s13068-019-1394-y 10.1038/s41589-019-0438-8 10.1016/j.biortech.2012.03.009 10.1007/s12010-008-8174-7 10.1002/anie.201800343 10.1186/s13068-014-0143-5 10.1016/S0021-9258(18)70223-8 10.1038/s41589-019-0437-9 10.3390/jof7040278 10.1073/pnas.1323629111 10.1186/s12896-015-0192-2 10.1016/j.cbpa.2017.12.001 10.1590/0100-5405/191071 10.1021/acs.oprd.5b00278 10.1371/journal.pone.0157844 10.1016/j.bioelechem.2021.107845 10.1016/j.simyco.2014.09.003 10.1128/am.13.5.686-693.1965 10.21203/rs.3.rs-493001/v1 10.1371/journal.ppat.1008652 10.1080/01926230290166724 10.1016/S0021-9258(18)60220-0 10.1186/s40694-020-00095-z 10.1007/s00253-014-5698-3 10.3389/fmicb.2015.01002 10.1039/C9OB02757B 10.1002/9783527693153 10.1007/978-3-540-49339-6_6 10.1201/9781439847503 10.3389/fpls.2018.01976 10.1002/14356007.a01_321.pub3 |
| ContentType | Journal Article |
| Copyright | Copyright © 2021 American Society for Microbiology. Copyright American Society for Microbiology Nov 2021 Attribution Copyright © 2021 American Society for Microbiology. 2021 American Society for Microbiology |
| Copyright_xml | – notice: Copyright © 2021 American Society for Microbiology. – notice: Copyright American Society for Microbiology Nov 2021 – notice: Attribution – notice: Copyright © 2021 American Society for Microbiology. 2021 American Society for Microbiology |
| DBID | CGR CUY CVF ECM EIF NPM AAYXX CITATION 7QL 7QO 7SN 7SS 7ST 7T7 7TM 7U9 8FD C1K FR3 H94 M7N P64 RC3 SOI 7X8 1XC VOOES 5PM |
| DOI | 10.1128/AEM.01526-21 |
| DatabaseName | Medline MEDLINE MEDLINE (Ovid) MEDLINE MEDLINE PubMed CrossRef Bacteriology Abstracts (Microbiology B) Biotechnology Research Abstracts Ecology Abstracts Entomology Abstracts (Full archive) Environment Abstracts Industrial and Applied Microbiology Abstracts (Microbiology A) Nucleic Acids Abstracts Virology and AIDS Abstracts Technology Research Database Environmental Sciences and Pollution Management Engineering Research Database AIDS and Cancer Research Abstracts Algology Mycology and Protozoology Abstracts (Microbiology C) Biotechnology and BioEngineering Abstracts Genetics Abstracts Environment Abstracts MEDLINE - Academic Hyper Article en Ligne (HAL) Hyper Article en Ligne (HAL) (Open Access) PubMed Central (Full Participant titles) |
| DatabaseTitle | MEDLINE Medline Complete MEDLINE with Full Text PubMed MEDLINE (Ovid) CrossRef Virology and AIDS Abstracts Technology Research Database Nucleic Acids Abstracts Ecology Abstracts Biotechnology and BioEngineering Abstracts Environmental Sciences and Pollution Management Entomology Abstracts Genetics Abstracts Biotechnology Research Abstracts Bacteriology Abstracts (Microbiology B) Algology Mycology and Protozoology Abstracts (Microbiology C) AIDS and Cancer Research Abstracts Engineering Research Database Industrial and Applied Microbiology Abstracts (Microbiology A) Environment Abstracts MEDLINE - Academic |
| DatabaseTitleList | Virology and AIDS Abstracts MEDLINE CrossRef |
| Database_xml | – sequence: 1 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 – sequence: 2 dbid: EIF name: MEDLINE url: https://proxy.k.utb.cz/login?url=https://www.webofscience.com/wos/medline/basic-search sourceTypes: Index Database |
| DeliveryMethod | fulltext_linktorsrc |
| Discipline | Economics Engineering Biology |
| EISSN | 1098-5336 |
| Editor | Buan, Nicole R |
| Editor_xml | – sequence: 1 givenname: Nicole R surname: Buan fullname: Buan, Nicole R – sequence: 1 givenname: Nicole R. surname: Buan fullname: Buan, Nicole R. |
| EndPage | e0152621 |
| ExternalDocumentID | oai_HAL_hal_03619439v1 10_1128_AEM_01526_21 01526-21 34613753 |
| Genre | Research Support, Non-U.S. Gov't Journal Article |
| GrantInformation_xml | – fundername: Agence Nationale de la Recherche (ANR) grantid: ANR-17-CE07-0047 – fundername: Association Nationale de la Recherche et de la Technologie (ANRT) grantid: 2017/1169 – fundername: Agence Nationale de la Recherche (ANR) grantid: ANR-17-CAPS-0004-01 – fundername: Agence Nationale de la Recherche (ANR) grantid: ANR-17-CE07-0047 funderid: https://doi.org/10.13039/501100001665 – fundername: Agence Nationale de la Recherche (ANR) grantid: ANR-17-CAPS-0004-01 funderid: https://doi.org/10.13039/501100001665 – fundername: Association Nationale de la Recherche et de la Technologie (ANRT) grantid: 2017/1169 funderid: https://doi.org/10.13039/501100003032 – fundername: ; grantid: ANR-17-CAPS-0004-01 – fundername: ; grantid: ANR-17-CE07-0047 – fundername: ; grantid: 2017/1169 |
| GroupedDBID | --- -~X 0R~ 23M 2WC 39C 4.4 53G 5GY 5RE 5VS 6J9 85S AAZTW ABOGM ABPPZ ACBTR ACGFO ACIWK ACNCT ACPRK ADBBV ADUKH AENEX AFRAH AGVNZ ALMA_UNASSIGNED_HOLDINGS AOIJS BAWUL BKOMP BTFSW CGR CS3 CUY CVF D0L DIK E.- E3Z EBS ECM EIF F5P GX1 H13 HYE HZ~ K-O KQ8 L7B NPM O9- P2P PQQKQ RHF RHI RNS RPM RSF RXW TAE TN5 TR2 TWZ UCJ UHB W8F WH7 WOQ X6Y ~02 ~KM - 02 0R AAPBV ABFLS ABPTK ADACO BXI HZ KM OK1 PQEST X ZA5 AAYXX CITATION 7QL 7QO 7SN 7SS 7ST 7T7 7TM 7U9 8FD C1K FR3 H94 M7N P64 RC3 SOI 7X8 .55 .GJ 1XC 3O- ABTAH AFFNX AGCDD AI. C1A EJD F20 H~9 MVM NEJ OHT TAF VH1 VOOES WHG X7M XJT YV5 ZCG ZGI ZXP ZY4 5PM |
| ID | FETCH-LOGICAL-a480t-fd8a456511f2ba1ddb809125ef8e6bf2790fcf561942b4f2fd6b69a6eec1830a3 |
| IEDL.DBID | RPM |
| ISSN | 0099-2240 |
| IngestDate | Tue Sep 17 21:16:13 EDT 2024 Fri Sep 06 13:08:27 EDT 2024 Sat Aug 17 00:34:19 EDT 2024 Fri Sep 13 07:23:22 EDT 2024 Thu Sep 12 17:25:26 EDT 2024 Tue Dec 28 13:57:58 EST 2021 Sat Sep 28 08:22:25 EDT 2024 |
| IsDoiOpenAccess | true |
| IsOpenAccess | true |
| IsPeerReviewed | true |
| IsScholarly | true |
| Issue | 24 |
| Keywords | flavors and fragrances filamentous fungi secretomics alcohol oxidase copper radical oxidase CAZymes phytopathogen Colletotrichum copper-containing enzymes Alcohol oxidase Filamentous fungi Secretomics Copper-containing enzymes Phytopathogen Flavors and fragrances Copper radical oxidase |
| Language | English |
| License | All Rights Reserved. https://doi.org/10.1128/ASMCopyrightv2 Attribution: http://creativecommons.org/licenses/by All Rights Reserved. |
| LinkModel | DirectLink |
| MergedId | FETCHMERGED-LOGICAL-a480t-fd8a456511f2ba1ddb809125ef8e6bf2790fcf561942b4f2fd6b69a6eec1830a3 |
| Notes | ObjectType-Article-1 SourceType-Scholarly Journals-1 ObjectType-Feature-2 content type line 23 Present address: Safwan Saker, CRITT Bois, Epinal, France. Citation Ribeaucourt D, Saker S, Navarro D, Bissaro B, Drula E, Correia LO, Haon M, Grisel S, Lapalu N, Henrissat B, O’Connell RJ, Lambert F, Lafond M, Berrin J-G. 2021. Identification of copper-containing oxidoreductases in the secretomes of three Colletotrichum species with a focus on copper radical oxidases for the biocatalytic production of fatty aldehydes. Appl Environ Microbiol 87:e01526-21. https://doi.org/10.1128/AEM.01526-21. |
| ORCID | 0000-0003-0927-1491 0000-0001-7570-3745 0000-0003-2646-0286 0000-0001-8354-3892 0000-0002-9168-5214 0000-0002-3434-8588 0000-0002-5358-6143 0000-0002-8590-250X 0000-0002-9773-4611 |
| OpenAccessLink | https://hal.science/hal-03619439 |
| PMID | 34613753 |
| PQID | 2606198927 |
| PQPubID | 42251 |
| PageCount | 15 |
| ParticipantIDs | pubmedcentral_primary_oai_pubmedcentral_nih_gov_8612266 hal_primary_oai_HAL_hal_03619439v1 proquest_miscellaneous_2580016880 proquest_journals_2606198927 crossref_primary_10_1128_AEM_01526_21 asm2_journals_10_1128_AEM_01526_21 pubmed_primary_34613753 |
| PublicationCentury | 2000 |
| PublicationDate | 20211124 |
| PublicationDateYYYYMMDD | 2021-11-24 |
| PublicationDate_xml | – month: 11 year: 2021 text: 20211124 day: 24 |
| PublicationDecade | 2020 |
| PublicationPlace | United States |
| PublicationPlace_xml | – name: United States – name: 1752 N St., N.W., Washington, DC – name: Washington |
| PublicationTitle | Applied and environmental microbiology |
| PublicationTitleAbbrev | Appl Environ Microbiol |
| PublicationTitleAlternate | Appl Environ Microbiol |
| PublicationYear | 2021 |
| Publisher | American Society for Microbiology |
| Publisher_xml | – name: American Society for Microbiology |
| References | Lokko, Y, Heijde, M, Schebesta, K, Scholtès, P, Van Montagu, M, Giacca, M (B2) 2018; 40 Balaraman, E, Khaskin, E, Leitus, G, Milstein, D (B54) 2013; 5 Hage, H, Rosso, M-N (B5) 2021; 7 Pellis, A, Cantone, S, Ebert, C, Gardossi, L (B3) 2018; 40 Emri, T, Molnár, Z, Szilágyi, M, Pócsi, I (B67) 2008; 151 Ribeaucourt, D, Bissaro, B, Guallar, V, Yemloul, M, Haon, M, Grisel, S, Alphand, V, Brumer, H, Lambert, F, Berrin, J-G, Lafond, M (B21) 2021; 9 Rispoli, FJ, Shah, V (B40) 2007; 34 Mathieu, Y, Offen, WA, Forget, SM, Ciano, L, Viborg, AH, Blagova, E, Henrissat, B, Walton, PH, Davies, GJ, Brumer, H (B44) 2020; 10 Ribeaucourt, D, Bissaro, B, Lambert, F, Lafond, M, Berrin, J-G (B32) 2021 Sánchez-Vallet, A, Tian, H, Rodriguez-Moreno, L, Valkenburg, D-J, Saleem-Batcha, R, Wawra, S, Kombrink, A, Verhage, L, de Jonge, R, van Esse, HP, Zuccaro, A, Croll, D, Mesters, JR, Thomma, BPHJ (B64) 2020; 16 Couturier, M, Navarro, D, Olivé, C, Chevret, D, Haon, M, Favel, A, Lesage-Meessen, L, Henrissat, B, Coutinho, PM, Berrin, J-G (B8) 2012; 13 Ravalason, H, Grisel, S, Chevret, D, Favel, A, Berrin, J-G, Sigoillot, J-C, Herpoël-Gimbert, I (B56) 2012; 114 Onofre, SB, Steilmann, P, Bertolini, J, Rotta, D, Francini, AS, Kagimura, Y, Acirc, S, Groff, N, Mazzali, L (B38) 2011; 2 Haon, M, Grisel, S, Navarro, D, Gruet, A, Berrin, J-G, Bignon, C (B71) 2015; 6 Cooper, JAD, Smith, W, Bacila, M, Medina, H (B16) 1959; 234 Andberg, M, Mollerup, F, Parikka, K, Koutaniemi, S, Boer, H, Juvonen, M, Master, E, Tenkanen, M, Kruus, K (B43) 2017; 83 Zeiner, CA, Purvine, SO, Zink, EM, Paša-Tolić, L, Chaput, DL, Haridas, S, Wu, S, LaButti, K, Grigoriev, IV, Henrissat, B, Santelli, CM, Hansel, CM (B46) 2016; 11 Poidevin, L, Berrin, J-G, Bennati-Granier, C, Levasseur, A, Herpoël-Gimbert, I, Chevret, D, Coutinho, PM, Henrissat, B, Heiss-Blanquet, S, Record, E (B55) 2014; 98 Akcapinar, GB, Kappel, L, Sezerman, OU, Seidl-Seiboth, V (B65) 2015; 61 Grandmontagne, D, Navarro, D, Neugnot-Roux, V, Ladevèze, S, Berrin, J-G (B9) 2021; 7 Gaetke, LM, Chow, CK (B62) 2003; 189 Oide, S, Tanaka, Y, Watanabe, A, Inui, M (B19) 2019; 125 Baroncelli, R, Amby, DB, Zapparata, A, Sarrocco, S, Vannacci, G, Le Floch, G, Harrison, RJ, Holub, E, Sukno, SA, Sreenivasaprasad, S, Thon, MR (B34) 2016; 17 Labourel, A, Frandsen, KEH, Zhang, F, Brouilly, N, Grisel, S, Haon, M, Ciano, L, Ropartz, D, Fanuel, M, Martin, F, Navarro, D, Rosso, M-N, Tandrup, T, Bissaro, B, Johansen, KS, Zerva, A, Walton, PH, Henrissat, B, Leggio, LL, Berrin, J-G (B58) 2020; 16 Tsuzuki, S (B25) 2019; 67 Lomascolo, A, Record, E, Herpoel-Gimbert, I, Delattre, M, Robert, JL, Georis, J, Dauvrin, T, Sigoillot, J-C, Asther, M (B12) 2003; 94 Agger, JW, Isaksen, T, Várnai, A, Vidal-Melgosa, S, Willats, WGT, Ludwig, R, Horn, SJ, Eijsink, VGH, Westereng, B (B57) 2014; 111 Leuthner, B, Aichinger, C, Oehmen, E, Koopmann, E, Müller, O, Müller, P, Kahmann, R, Bölker, M, Schreier, PH (B69) 2005; 272 Yin, D, Urresti, S, Lafond, M, Johnston, EM, Derikvand, F, Ciano, L, Berrin, J-G, Henrissat, B, Walton, PH, Davies, GJ, Brumer, H (B18) 2015; 6 Tordai, H, Bányai, L, Patthy, L (B53) 1999; 461 Takahara, H, Hacquard, S, Kombrink, A, Hughes, HB, Halder, V, Robin, GP, Hiruma, K, Neumann, U, Shinya, T, Kombrink, E, Shibuya, N, Thomma, BPHJ, O’Connell, RJ (B66) 2016; 211 Amara, S, Perrot, T, Navarro, D, Deroy, A, Benkhelfallah, A, Chalak, A, Daou, M, Chevret, D, Faulds, CB, Berrin, J-G, Morel-Rouhier, M, Gelhaye, E, Record, E (B72) 2018; 84 Tokuyasu, K, Ohnishi-Kameyama, M, Hayashi, K (B39) 1996; 60 Vivek-Ananth, RP, Mohanraj, K, Vandanashree, M, Jhingran, A, Craig, JP, Samal, A (B49) 2018; 8 Filiatrault-Chastel, C, Navarro, D, Haon, M, Grisel, S, Herpoël-Gimbert, I, Chevret, D, Fanuel, M, Henrissat, B, Heiss-Blanquet, S, Margeot, A, Berrin, J-G (B10) 2019; 12 Copete, LS, Chanagá, X, Barriuso, J, López-Lucendo, MF, Martínez, MJ, Camarero, S (B45) 2015; 15 Arntzen, MØ, Bengtsson, O, Várnai, A, Delogu, F, Mathiesen, G, Eijsink, VGH (B7) 2020; 10 Navarro, D, Rosso, M-N, Haon, M, Olivé, C, Bonnin, E, Lesage-Meessen, L, Chevret, D, Coutinho, PM, Henrissat, B, Berrin, J-G (B50) 2014; 7 Kohen, R, Nyska, A (B63) 2002; 30 Lombard, V, Golaconda Ramulu, H, Drula, E, Coutinho, PM, Henrissat, B (B15) 2014; 42 Shah, J, Arslan, E, Cirucci, J, O’Brien, J, Moss, D (B29) 2016; 19 Pedersen, A, Birmingham, WR, Rehn, G, Charnock, SJ, Turner, NJ, Woodley, JM (B41) 2015; 19 Liu, J, Wu, S, Li, Z (B22) 2018; 43 Daou, M, Faulds, CB (B68) 2017; 33 Wohlgemuth, R, Twardowski, T, Aguilar, A (B1) 2021; 61 Lomascolo, A, Cayol, J-L, Roche, M, Guo, L, Robert, J-L, Record, E, Lesage-Meessen, L, Ollivier, B, Sigoillot, J-C, Asther, M (B13) 2002; 106 Burdock, GA (B26) 2016 Garcia-Santamarina, S, Probst, C, Festa, RA, Ding, C, Smith, AD, Conklin, SE, Brander, S, Kinch, LN, Grishin, NV, Franz, KJ, Riggs-Gelasco, P, Lo Leggio, L, Johansen, KS, Thiele, DJ (B59) 2020; 16 Baldwin, E, Plotto, A, Manthey, J, McCollum, G, Bai, J, Irey, M, Cameron, R, Luzio, G (B30) 2010; 58 Miura, N, Ueda, M (B48) 2018; 7 Bissaro, B, Kodama, S, Hage, H, Ribeaucourt, D, Haon, M, Grisel, S, Simaan, J, Beisson, F, Forget, S, Brumer, H, Rosso, M-N, O’Connell, R, Lafond, M, Kubo, Y, Berrin, J-G (B20) 2021 Kaur, K, Sharma, A, Capalash, N, Sharma, P (B61) 2019; 222 Meyer, V, Basenko, EY, Benz, JP, Braus, GH, Caddick, MX, Csukai, M, de Vries, RP, Endy, D, Frisvad, JC, Gunde-Cimerman, N, Haarmann, T, Hadar, Y, Hansen, K, Johnson, RI, Keller, NP, Kraševec, N, Mortensen, UH, Perez, R, Ram, AFJ, Record, E, Ross, P, Shapaval, V, Steiniger, C, van den Brink, H, van Munster, J, Yarden, O, Wösten, HAB (B4) 2020; 7 Levasseur, A, Drula, E, Lombard, V, Coutinho, PM, Henrissat, B (B14) 2013; 6 Armesto, C, Maia, FGM, Monteiro, FP, de Abreu, MS (B37) 2019; 45 Dong, J, Fernández‐Fueyo, E, Hollmann, F, Paul, CE, Pesic, M, Schmidt, S, Wang, Y, Younes, S, Zhang, W (B23) 2018; 57 Kersten, PJ (B42) 1990; 87 Rouseff, R, Perez-Cacho, PR, Berger, RG (B27) 2007 Forget, S, Xia, R, Hein, JE, Brumer, H (B33) 2020; 18 Gonçalves, AP, Heller, J, Span, EA, Rosenfield, G, Do, HP, Palma-Guerrero, J, Requena, N, Marletta, MA, Glass, NL (B60) 2019; 29 O’Connell, RJ, Thon, MR, Hacquard, S, Amyotte, SG, Kleemann, J, Torres, MF, Damm, U, Buiate, EA, Epstein, L, Alkan, N, Altmüller, J, Alvarado-Balderrama, L, Bauser, CA, Becker, C, Birren, BW, Chen, Z, Choi, J, Crouch, JA, Duvick, JP, Farman, MA, Gan, P, Heiman, D, Henrissat, B, Howard, RJ, Kabbage, M, Koch, C, Kracher, B, Kubo, Y, Law, AD, Lebrun, M-H, Lee, Y-H, Miyara, I, Moore, N, Neumann, U, Nordström, K, Panaccione, DG, Panstruga, R, Place, M, Proctor, RH, Prusky, D, Rech, G, Reinhardt, R, Rollins, JA, Rounsley, S, Schardl, CL, Schwartz, DC, Shenoy, N, Shirasu, K, Sikhakolli, UR, Stüber, K (B35) 2012; 44 Surburg, H, Panten, J (B24) 2016 Glass, NL, Schmoll, M, Cate, JHD, Coradetti, S (B6) 2013; 67 Damm, U, O’Connell, RJ, Groenewald, JZ, Crous, PW (B70) 2014; 79 Dala-Paula, BM, Plotto, A, Bai, J, Manthey, JA, Baldwin, EA, Ferrarezi, RS, Gloria, MBA (B31) 2018; 9 Ravalason, H, Jan, G, Mollé, D, Pasco, M, Coutinho, PM, Lapierre, C, Pollet, B, Bertaud, F, Petit-Conil, M, Grisel, S, Sigoillot, J-C, Asther, M, Herpoël-Gimbert, I (B11) 2008; 80 Kohlpaintner, C, Schulte, M, Falbe, J, Lappe, P, Weber, J, Frey, GD (B28) 2013 Cleveland, L, Coffman, RE, Coon, P, Davis, L (B51) 1975; 14 Avigad, G, Amaral, D, Asensio, C, Horecker, BL (B17) 1962; 237 Markus, Z, Miller, G, Avigad, G (B47) 1965; 13 Wohlschlager, L, Kracher, D, Scheiblbrandner, S, Csarman, F, Ludwig, R (B52) 2021; 141 Perfect, SE, Hughes, HB, O’Connell, RJ, Green, JR (B36) 1999; 27 e_1_3_3_50_2 e_1_3_3_71_2 e_1_3_3_16_2 e_1_3_3_18_2 e_1_3_3_12_2 e_1_3_3_37_2 e_1_3_3_58_2 e_1_3_3_14_2 e_1_3_3_35_2 e_1_3_3_56_2 e_1_3_3_33_2 e_1_3_3_54_2 e_1_3_3_10_2 e_1_3_3_31_2 e_1_3_3_52_2 e_1_3_3_73_2 e_1_3_3_40_2 e_1_3_3_61_2 e_1_3_3_5_2 e_1_3_3_7_2 e_1_3_3_9_2 e_1_3_3_27_2 e_1_3_3_29_2 e_1_3_3_23_2 e_1_3_3_48_2 e_1_3_3_69_2 e_1_3_3_25_2 e_1_3_3_46_2 e_1_3_3_67_2 e_1_3_3_44_2 e_1_3_3_65_2 e_1_3_3_3_2 e_1_3_3_21_2 e_1_3_3_42_2 e_1_3_3_63_2 e_1_3_3_51_2 e_1_3_3_70_2 e_1_3_3_17_2 e_1_3_3_19_2 e_1_3_3_38_2 e_1_3_3_13_2 e_1_3_3_36_2 e_1_3_3_59_2 e_1_3_3_15_2 e_1_3_3_34_2 e_1_3_3_57_2 e_1_3_3_32_2 e_1_3_3_55_2 e_1_3_3_11_2 e_1_3_3_30_2 e_1_3_3_53_2 e_1_3_3_72_2 e_1_3_3_62_2 e_1_3_3_60_2 e_1_3_3_6_2 e_1_3_3_8_2 e_1_3_3_28_2 Onofre SB (e_1_3_3_39_2) 2011; 2 e_1_3_3_49_2 e_1_3_3_24_2 e_1_3_3_47_2 e_1_3_3_26_2 e_1_3_3_45_2 e_1_3_3_68_2 e_1_3_3_2_2 e_1_3_3_20_2 e_1_3_3_43_2 e_1_3_3_66_2 e_1_3_3_4_2 e_1_3_3_22_2 e_1_3_3_41_2 e_1_3_3_64_2 |
| References_xml | – volume: 40 start-page: 154 year: 2018 end-page: 169 ident: B3 article-title: Evolving biocatalysis to meet bioeconomy challenges and opportunities publication-title: N Biotechnol doi: 10.1016/j.nbt.2017.07.005 contributor: fullname: Gardossi, L – volume: 13 start-page: 57 year: 2012 ident: B8 article-title: Post-genomic analyses of fungal lignocellulosic biomass degradation reveal the unexpected potential of the plant pathogen Ustilago maydis publication-title: BMC Genomics doi: 10.1186/1471-2164-13-57 contributor: fullname: Berrin, J-G – volume: 211 start-page: 1323 year: 2016 end-page: 1337 ident: B66 article-title: Colletotrichum higginsianum extracellular LysM proteins play dual roles in appressorial function and suppression of chitin-triggered plant immunity publication-title: New Phytol doi: 10.1111/nph.13994 contributor: fullname: O’Connell, RJ – volume: 67 start-page: 4720 year: 2019 end-page: 4725 ident: B25 article-title: Higher straight-chain aliphatic aldehydes: importance as odor-active volatiles in human foods and issues for future research publication-title: J Agric Food Chem doi: 10.1021/acs.jafc.9b01131 contributor: fullname: Tsuzuki, S – volume: 19 start-page: 1333 year: 2016 end-page: 1351 ident: B29 article-title: Comparison of oleo- vs. petro-sourcing of fatty alcohols via cradle-to-gate life cycle assessment publication-title: J Surfactants Deterg doi: 10.1007/s11743-016-1867-y contributor: fullname: Moss, D – volume: 34 start-page: 349 year: 2007 end-page: 355 ident: B40 article-title: Mixture design as a first step for optimization of fermentation medium for cutinase production from Colletotrichum lindemuthianum publication-title: J Ind Microbiol Biotechnol doi: 10.1007/s10295-007-0203-y contributor: fullname: Shah, V – volume: 5 start-page: 122 year: 2013 end-page: 125 ident: B54 article-title: Catalytic transformation of alcohols to carboxylic acid salts and H2 using water as the oxygen atom source publication-title: Nat Chem doi: 10.1038/nchem.1536 contributor: fullname: Milstein, D – volume: 84 year: 2018 ident: B72 article-title: Enzyme activities of two recombinant heme-containing peroxidases, Tv DyP1 and Tv VP2, identified from the secretome of Trametes versicolor publication-title: Appl Environ Microbiol doi: 10.1128/AEM.02826-17 contributor: fullname: Record, E – volume: 60 start-page: 1598 year: 1996 end-page: 1603 ident: B39 article-title: Purification and characterization of extracellular chitin deacetylase from Colletotrichum lindemuthianum publication-title: Biosci Biotechnol Biochem doi: 10.1271/bbb.60.1598 contributor: fullname: Hayashi, K – volume: 94 start-page: 618 year: 2003 end-page: 624 ident: B12 article-title: Overproduction of laccase by a monokaryotic strain of Pycnoporus cinnabarinus using ethanol as inducer publication-title: J Appl Microbiol doi: 10.1046/j.1365-2672.2003.01879.x contributor: fullname: Asther, M – volume: 10 start-page: 20267 year: 2020 ident: B7 article-title: Quantitative comparison of the biomass-degrading enzyme repertoires of five filamentous fungi publication-title: Sci Rep doi: 10.1038/s41598-020-75217-z contributor: fullname: Eijsink, VGH – year: 2016 ident: B24 publication-title: Common fragrance and flavor materials: preparation, properties and uses ;6th ed, ;Wiley-VCH ;Weinheim, Germany contributor: fullname: Panten, J – volume: 83 start-page: e01383-17 year: 2017 ident: B43 article-title: A novel Colletotrichum graminicola raffinose oxidase in the AA5 family publication-title: Appl Environ Microbiol doi: 10.1128/AEM.01383-17 contributor: fullname: Kruus, K – volume: 14 start-page: 1108 year: 1975 end-page: 1115 ident: B51 article-title: Role of the copper in galactose oxidase publication-title: Biochemistry doi: 10.1021/bi00677a003 contributor: fullname: Davis, L – volume: 125 start-page: 13 year: 2019 end-page: 20 ident: B19 article-title: Carbohydrate-binding property of a cell wall integrity and stress response component (WSC) domain of an alcohol oxidase from the rice blast pathogen Pyricularia oryzae publication-title: Enzyme Microb Technol doi: 10.1016/j.enzmictec.2019.02.009 contributor: fullname: Inui, M – volume: 106 start-page: 1193 year: 2002 end-page: 1203 ident: B13 article-title: Molecular clustering of Pycnoporus strains from various geographic origins and isolation of monokaryotic strains for laccase hyperproduction publication-title: Mycol Res doi: 10.1017/S0953756202006494 contributor: fullname: Asther, M – volume: 461 start-page: 63 year: 1999 end-page: 67 ident: B53 article-title: The PAN module: the N-terminal domains of plasminogen and hepatocyte growth factor are homologous with the apple domains of the prekallikrein family and with a novel domain found in numerous nematode proteins publication-title: FEBS Lett doi: 10.1016/s0014-5793(99)01416-7 contributor: fullname: Patthy, L – volume: 67 start-page: 477 year: 2013 end-page: 498 ident: B6 article-title: Plant cell wall deconstruction by ascomycete fungi publication-title: Annu Rev Microbiol doi: 10.1146/annurev-micro-092611-150044 contributor: fullname: Coradetti, S – year: 2021 ident: B32 article-title: Biocatalytic oxidation of fatty alcohols into aldehydes for the flavors and fragrances industry publication-title: Biotechnol Adv doi: 10.1016/j.biotechadv.2021.107787 contributor: fullname: Berrin, J-G – volume: 8 start-page: 6617 year: 2018 ident: B49 article-title: Comparative systems analysis of the secretome of the opportunistic pathogen Aspergillus fumigatus and other Aspergillus species publication-title: Sci Rep doi: 10.1038/s41598-018-25016-4 contributor: fullname: Samal, A – volume: 61 start-page: 22 year: 2021 end-page: 28 ident: B1 article-title: Bioeconomy moving forward step by step—a global journey publication-title: N Biotechnol doi: 10.1016/j.nbt.2020.11.006 contributor: fullname: Aguilar, A – volume: 17 start-page: 555 year: 2016 ident: B34 article-title: Gene family expansions and contractions are associated with host range in plant pathogens of the genus Colletotrichum publication-title: BMC Genomics doi: 10.1186/s12864-016-2917-6 contributor: fullname: Thon, MR – volume: 27 start-page: 186 year: 1999 end-page: 198 ident: B36 article-title: Colletotrichum: a model genus for studies on pathology and fungal–plant interactions publication-title: Fungal Genet Biol doi: 10.1006/fgbi.1999.1143 contributor: fullname: Green, JR – volume: 29 start-page: 3006 year: 2019 end-page: 3017.e3 ident: B60 article-title: Allorecognition upon fungal cell–cell contact determines social cooperation and impacts the acquisition of multicellularity publication-title: Curr Biol doi: 10.1016/j.cub.2019.07.060 contributor: fullname: Glass, NL – volume: 7 start-page: 185 year: 2021 ident: B5 article-title: Evolution of fungal carbohydrate-active enzyme portfolios and adaptation to plant cell-wall polymers publication-title: J Fungi doi: 10.3390/jof7030185 contributor: fullname: Rosso, M-N – volume: 61 start-page: 103 year: 2015 end-page: 113 ident: B65 article-title: Molecular diversity of LysM carbohydrate-binding motifs in fungi publication-title: Curr Genet doi: 10.1007/s00294-014-0471-9 contributor: fullname: Seidl-Seiboth, V – volume: 189 start-page: 147 year: 2003 end-page: 163 ident: B62 article-title: Copper toxicity, oxidative stress, and antioxidant nutrients publication-title: Toxicology doi: 10.1016/s0300-483x(03)00159-8 contributor: fullname: Chow, CK – volume: 42 start-page: D490 year: 2014 end-page: D495 ident: B15 article-title: The carbohydrate-active enzymes database (CAZy) in 2013 publication-title: Nucleic Acids Res doi: 10.1093/nar/gkt1178 contributor: fullname: Henrissat, B – volume: 40 start-page: 5 year: 2018 end-page: 10 ident: B2 article-title: Biotechnology and the bioeconomy—towards inclusive and sustainable industrial development publication-title: N Biotechnol doi: 10.1016/j.nbt.2017.06.005 contributor: fullname: Giacca, M – volume: 10 start-page: e3042 year: 2020 end-page: 3058 ident: B44 article-title: Discovery of a fungal copper radical oxidase with high catalytic efficiency towards 5-hydroxymethylfurfural and benzyl alcohols for bioprocessing publication-title: ACS Catal doi: 10.1021/acscatal.9b04727 contributor: fullname: Brumer, H – year: 2016 ident: B26 publication-title: Fenaroli’s handbook of flavor ingredients. ;CRC Press LLC ;Boca Raton, Florida contributor: fullname: Burdock, GA – volume: 18 start-page: 2005 year: 2020 end-page: 2184 ident: B33 article-title: Determination of biocatalytic parameters of a copper radical oxidase using real-time reaction progress monitoring publication-title: Org Biomol Chem contributor: fullname: Brumer, H – volume: 87 start-page: 2936 year: 1990 end-page: 2940 ident: B42 article-title: Glyoxal oxidase of Phanerochaete chrysosporium: its characterization and activation by lignin peroxidase publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.87.8.2936 contributor: fullname: Kersten, PJ – volume: 7 start-page: 128 year: 2018 ident: B48 article-title: Evaluation of unconventional protein secretion by Saccharomyces cerevisiae and other fungi publication-title: Cells doi: 10.3390/cells7090128 contributor: fullname: Ueda, M – volume: 33 start-page: 87 year: 2017 ident: B68 article-title: Glyoxal oxidases: their nature and properties publication-title: World J Microbiol Biotechnol doi: 10.1007/s11274-017-2254-1 contributor: fullname: Faulds, CB – volume: 272 start-page: 639 year: 2005 end-page: 650 ident: B69 article-title: A H2O2-producing glyoxal oxidase is required for filamentous growth and pathogenicity in Ustilago maydis publication-title: Mol Genet Genomics doi: 10.1007/s00438-004-1085-6 contributor: fullname: Schreier, PH – volume: 44 start-page: 1060 year: 2012 end-page: 1065 ident: B35 article-title: Lifestyle transitions in plant pathogenic Colletotrichum fungi deciphered by genome and transcriptome analyses publication-title: Nat Genet doi: 10.1038/ng.2372 contributor: fullname: Stüber, K – volume: 80 start-page: 719 year: 2008 end-page: 733 ident: B11 article-title: Secretome analysis of Phanerochaete chrysosporium strain CIRM-BRFM41 grown on softwood publication-title: Appl Microbiol Biotechnol doi: 10.1007/s00253-008-1596-x contributor: fullname: Herpoël-Gimbert, I – volume: 6 start-page: 10197 year: 2015 ident: B18 article-title: Structure–function characterization reveals new catalytic diversity in the galactose oxidase and glyoxal oxidase family publication-title: Nat Commun doi: 10.1038/ncomms10197 contributor: fullname: Brumer, H – volume: 222 start-page: 1 year: 2019 end-page: 13 ident: B61 article-title: Multicopper oxidases: biocatalysts in microbial pathogenesis and stress management publication-title: Microbiol Res doi: 10.1016/j.micres.2019.02.007 contributor: fullname: Sharma, P – volume: 9 start-page: 4411 year: 2021 end-page: 4421 ident: B21 article-title: Comprehensive insights into the production of long chain aliphatic aldehydes using a copper-radical alcohol oxidase as biocatalyst publication-title: ACS Sustainable Chem Eng doi: 10.1021/acssuschemeng.0c07406 contributor: fullname: Lafond, M – volume: 58 start-page: 1247 year: 2010 end-page: 1262 ident: B30 article-title: Effect of liberibacter infection (Huanglongbing disease) of citrus on orange fruit physiology and fruit/fruit juice quality: chemical and physical analyses publication-title: J Agric Food Chem doi: 10.1021/jf9031958 contributor: fullname: Luzio, G – volume: 6 start-page: 41 year: 2013 ident: B14 article-title: Expansion of the enzymatic repertoire of the CAZy database to integrate auxiliary redox enzymes publication-title: Biotechnol Biofuels doi: 10.1186/1754-6834-6-41 contributor: fullname: Henrissat, B – volume: 12 start-page: 55 year: 2019 ident: B10 article-title: AA16, a new lytic polysaccharide monooxygenase family identified in fungal secretomes publication-title: Biotechnol Biofuels doi: 10.1186/s13068-019-1394-y contributor: fullname: Berrin, J-G – volume: 16 start-page: 345 year: 2020 end-page: 350 ident: B58 article-title: A fungal family of lytic polysaccharide monooxygenase-like copper proteins publication-title: Nat Chem Biol doi: 10.1038/s41589-019-0438-8 contributor: fullname: Berrin, J-G – volume: 6 start-page: 1002 year: 2015 ident: B71 article-title: Recombinant protein production facility for fungal biomass-degrading enzymes using the yeast Pichia pastoris publication-title: Front Microbiol contributor: fullname: Bignon, C – volume: 2 start-page: 28 year: 2011 end-page: 32 ident: B38 article-title: Amylolytic enzymes produced by the fungus Colletotrichum gloeosporioides in rice semi-solid fermentation publication-title: J Yeast Fungal Res contributor: fullname: Mazzali, L – volume: 114 start-page: 589 year: 2012 end-page: 596 ident: B56 article-title: Fusarium verticillioides secretome as a source of auxiliary enzymes to enhance saccharification of wheat straw publication-title: Bioresour Technol doi: 10.1016/j.biortech.2012.03.009 contributor: fullname: Herpoël-Gimbert, I – volume: 151 start-page: 211 year: 2008 end-page: 220 ident: B67 article-title: Regulation of autolysis in Aspergillus nidulans publication-title: Appl Biochem Biotechnol doi: 10.1007/s12010-008-8174-7 contributor: fullname: Pócsi, I – volume: 57 start-page: 9238 year: 2018 end-page: 9261 ident: B23 article-title: Biocatalytic oxidation reactions: a chemist’s perspective publication-title: Angew Chem Int Ed Engl doi: 10.1002/anie.201800343 contributor: fullname: Zhang, W – volume: 7 start-page: 143 year: 2014 ident: B50 article-title: Fast solubilization of recalcitrant cellulosic biomass by the basidiomycete fungus Laetisaria arvalis involves successive secretion of oxidative and hydrolytic enzymes publication-title: Biotechnol Biofuels doi: 10.1186/s13068-014-0143-5 contributor: fullname: Berrin, J-G – volume: 234 start-page: 445 year: 1959 end-page: 448 ident: B16 article-title: Galactose oxidase from Polyporus circinatus, Fr publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)70223-8 contributor: fullname: Medina, H – volume: 16 start-page: 337 year: 2020 end-page: 344 ident: B59 article-title: A lytic polysaccharide monooxygenase-like protein functions in fungal copper import and meningitis publication-title: Nat Chem Biol doi: 10.1038/s41589-019-0437-9 contributor: fullname: Thiele, DJ – volume: 7 start-page: 278 year: 2021 ident: B9 article-title: The secretomes of Aspergillus japonicus and Aspergillus terreus supplement the Rovabio enzyme cocktail for the degradation of soybean meal for animal feed publication-title: J Fungi doi: 10.3390/jof7040278 contributor: fullname: Berrin, J-G – volume: 111 start-page: 6287 year: 2014 end-page: 6292 ident: B57 article-title: Discovery of LPMO activity on hemicelluloses shows the importance of oxidative processes in plant cell wall degradation publication-title: Proc Natl Acad Sci USA doi: 10.1073/pnas.1323629111 contributor: fullname: Westereng, B – volume: 15 start-page: 74 year: 2015 ident: B45 article-title: Identification and characterization of laccase-type multicopper oxidases involved in dye-decolorization by the fungus Leptosphaerulina sp publication-title: BMC Biotechnol doi: 10.1186/s12896-015-0192-2 contributor: fullname: Camarero, S – volume: 43 start-page: 77 year: 2018 end-page: 86 ident: B22 article-title: Recent advances in enzymatic oxidation of alcohols publication-title: Curr Opin Chem Biol doi: 10.1016/j.cbpa.2017.12.001 contributor: fullname: Li, Z – volume: 45 start-page: 368 year: 2019 end-page: 373 ident: B37 article-title: Exoenzymes as a pathogenicity factor for Colletotrichum gloeosporioides associated with coffee plants publication-title: Summa Phytopathol doi: 10.1590/0100-5405/191071 contributor: fullname: de Abreu, MS – volume: 19 start-page: 1580 year: 2015 end-page: 1589 ident: B41 article-title: Process requirements of galactose oxidase catalyzed oxidation of alcohols publication-title: Org Process Res Dev doi: 10.1021/acs.oprd.5b00278 contributor: fullname: Woodley, JM – volume: 11 year: 2016 ident: B46 article-title: Comparative analysis of secretome profiles of manganese(II)-oxidizing ascomycete fungi publication-title: PLoS One doi: 10.1371/journal.pone.0157844 contributor: fullname: Hansel, CM – volume: 141 start-page: 107845 year: 2021 ident: B52 article-title: Spectroelectrochemical investigation of the glyoxal oxidase activation mechanism publication-title: Bioelectrochemistry doi: 10.1016/j.bioelechem.2021.107845 contributor: fullname: Ludwig, R – volume: 79 start-page: 49 year: 2014 end-page: 84 ident: B70 article-title: The Colletotrichum destructivum species complex—hemibiotrophic pathogens of forage and field crops publication-title: Stud Mycol doi: 10.1016/j.simyco.2014.09.003 contributor: fullname: Crous, PW – volume: 13 start-page: 686 year: 1965 end-page: 693 ident: B47 article-title: Effect of culture conditions on the production of d-galactose oxidase by Dactylium dendroides publication-title: Appl Microbiol doi: 10.1128/am.13.5.686-693.1965 contributor: fullname: Avigad, G – year: 2021 ident: B20 article-title: Unravelling the role of alcohol copper radical oxidases in fungal plant pathogens publication-title: Res Square doi: 10.21203/rs.3.rs-493001/v1 contributor: fullname: Berrin, J-G – volume: 16 year: 2020 ident: B64 article-title: A secreted LysM effector protects fungal hyphae through chitin-dependent homodimer polymerization publication-title: PLoS Pathog doi: 10.1371/journal.ppat.1008652 contributor: fullname: Thomma, BPHJ – volume: 30 start-page: 620 year: 2002 end-page: 650 ident: B63 article-title: Oxidation of biological systems: oxidative stress phenomena, antioxidants, redox reactions, and methods for their quantification publication-title: Toxicol Pathol doi: 10.1080/01926230290166724 contributor: fullname: Nyska, A – volume: 237 start-page: 2736 year: 1962 end-page: 2743 ident: B17 article-title: The d-galactose oxidase of Polyporus circinatus publication-title: J Biol Chem doi: 10.1016/S0021-9258(18)60220-0 contributor: fullname: Horecker, BL – start-page: 117 year: 2007 end-page: 134 ident: B27 article-title: Citrus Flavour publication-title: Flavours and fragrances: chemistry, bioprocessing and sustainability. ;Springer ;Berlin, Germany contributor: fullname: Berger, RG – year: 2013 ident: B28 article-title: Aldehydes, aliphatic publication-title: Ullmann’s encyclopedia of industrial chemistry. ;Wiley-VCH ;Weinheim, Germany contributor: fullname: Frey, GD – volume: 9 start-page: 1976 year: 2018 ident: B31 article-title: Effect of Huanglongbing or greening disease on orange juice quality, a review publication-title: Front Plant Sci contributor: fullname: Gloria, MBA – volume: 7 start-page: 5 year: 2020 ident: B4 article-title: Growing a circular economy with fungal biotechnology: a white paper publication-title: Fungal Biol Biotechnol doi: 10.1186/s40694-020-00095-z contributor: fullname: Wösten, HAB – volume: 98 start-page: 7457 year: 2014 end-page: 7469 ident: B55 article-title: Comparative analyses of Podospora anserina secretomes reveal a large array of lignocellulose-active enzymes publication-title: Appl Microbiol Biotechnol doi: 10.1007/s00253-014-5698-3 contributor: fullname: Record, E – ident: e_1_3_3_11_2 doi: 10.1186/s13068-019-1394-y – ident: e_1_3_3_48_2 doi: 10.1128/am.13.5.686-693.1965 – ident: e_1_3_3_24_2 doi: 10.1002/anie.201800343 – ident: e_1_3_3_10_2 doi: 10.3390/jof7040278 – ident: e_1_3_3_41_2 doi: 10.1007/s10295-007-0203-y – ident: e_1_3_3_72_2 doi: 10.3389/fmicb.2015.01002 – ident: e_1_3_3_70_2 doi: 10.1007/s00438-004-1085-6 – ident: e_1_3_3_34_2 doi: 10.1039/C9OB02757B – ident: e_1_3_3_50_2 doi: 10.1038/s41598-018-25016-4 – ident: e_1_3_3_62_2 doi: 10.1016/j.micres.2019.02.007 – ident: e_1_3_3_58_2 doi: 10.1073/pnas.1323629111 – ident: e_1_3_3_17_2 doi: 10.1016/S0021-9258(18)70223-8 – ident: e_1_3_3_53_2 doi: 10.1016/j.bioelechem.2021.107845 – ident: e_1_3_3_42_2 doi: 10.1021/acs.oprd.5b00278 – ident: e_1_3_3_25_2 doi: 10.1002/9783527693153 – ident: e_1_3_3_5_2 doi: 10.1186/s40694-020-00095-z – ident: e_1_3_3_8_2 doi: 10.1038/s41598-020-75217-z – volume: 2 start-page: 28 year: 2011 ident: e_1_3_3_39_2 article-title: Amylolytic enzymes produced by the fungus Colletotrichum gloeosporioides in rice semi-solid fermentation publication-title: J Yeast Fungal Res contributor: fullname: Onofre SB – ident: e_1_3_3_23_2 doi: 10.1016/j.cbpa.2017.12.001 – ident: e_1_3_3_54_2 doi: 10.1016/s0014-5793(99)01416-7 – ident: e_1_3_3_28_2 doi: 10.1007/978-3-540-49339-6_6 – ident: e_1_3_3_33_2 doi: 10.1016/j.biotechadv.2021.107787 – ident: e_1_3_3_63_2 doi: 10.1016/s0300-483x(03)00159-8 – ident: e_1_3_3_61_2 doi: 10.1016/j.cub.2019.07.060 – ident: e_1_3_3_14_2 doi: 10.1017/S0953756202006494 – ident: e_1_3_3_60_2 doi: 10.1038/s41589-019-0437-9 – ident: e_1_3_3_37_2 doi: 10.1006/fgbi.1999.1143 – ident: e_1_3_3_19_2 doi: 10.1038/ncomms10197 – ident: e_1_3_3_9_2 doi: 10.1186/1471-2164-13-57 – ident: e_1_3_3_47_2 doi: 10.1371/journal.pone.0157844 – ident: e_1_3_3_13_2 doi: 10.1046/j.1365-2672.2003.01879.x – ident: e_1_3_3_27_2 doi: 10.1201/9781439847503 – ident: e_1_3_3_3_2 doi: 10.1016/j.nbt.2017.06.005 – ident: e_1_3_3_40_2 doi: 10.1271/bbb.60.1598 – ident: e_1_3_3_2_2 doi: 10.1016/j.nbt.2020.11.006 – ident: e_1_3_3_22_2 doi: 10.1021/acssuschemeng.0c07406 – ident: e_1_3_3_32_2 doi: 10.3389/fpls.2018.01976 – ident: e_1_3_3_16_2 doi: 10.1093/nar/gkt1178 – ident: e_1_3_3_20_2 doi: 10.1016/j.enzmictec.2019.02.009 – ident: e_1_3_3_21_2 doi: 10.21203/rs.3.rs-493001/v1 – ident: e_1_3_3_15_2 doi: 10.1186/1754-6834-6-41 – ident: e_1_3_3_45_2 doi: 10.1021/acscatal.9b04727 – ident: e_1_3_3_46_2 doi: 10.1186/s12896-015-0192-2 – ident: e_1_3_3_7_2 doi: 10.1146/annurev-micro-092611-150044 – ident: e_1_3_3_69_2 doi: 10.1007/s11274-017-2254-1 – ident: e_1_3_3_38_2 doi: 10.1590/0100-5405/191071 – ident: e_1_3_3_30_2 doi: 10.1007/s11743-016-1867-y – ident: e_1_3_3_36_2 doi: 10.1038/ng.2372 – ident: e_1_3_3_55_2 doi: 10.1038/nchem.1536 – ident: e_1_3_3_73_2 doi: 10.1128/AEM.02826-17 – ident: e_1_3_3_52_2 doi: 10.1021/bi00677a003 – ident: e_1_3_3_26_2 doi: 10.1021/acs.jafc.9b01131 – ident: e_1_3_3_4_2 doi: 10.1016/j.nbt.2017.07.005 – ident: e_1_3_3_18_2 doi: 10.1016/S0021-9258(18)60220-0 – ident: e_1_3_3_66_2 doi: 10.1007/s00294-014-0471-9 – ident: e_1_3_3_67_2 doi: 10.1111/nph.13994 – ident: e_1_3_3_57_2 doi: 10.1016/j.biortech.2012.03.009 – ident: e_1_3_3_12_2 doi: 10.1007/s00253-008-1596-x – ident: e_1_3_3_31_2 doi: 10.1021/jf9031958 – ident: e_1_3_3_64_2 doi: 10.1080/01926230290166724 – ident: e_1_3_3_59_2 doi: 10.1038/s41589-019-0438-8 – ident: e_1_3_3_44_2 doi: 10.1128/AEM.01383-17 – ident: e_1_3_3_51_2 doi: 10.1186/s13068-014-0143-5 – ident: e_1_3_3_49_2 doi: 10.3390/cells7090128 – ident: e_1_3_3_43_2 doi: 10.1073/pnas.87.8.2936 – ident: e_1_3_3_68_2 doi: 10.1007/s12010-008-8174-7 – ident: e_1_3_3_6_2 doi: 10.3390/jof7030185 – ident: e_1_3_3_29_2 doi: 10.1002/14356007.a01_321.pub3 – ident: e_1_3_3_71_2 doi: 10.1016/j.simyco.2014.09.003 – ident: e_1_3_3_35_2 doi: 10.1186/s12864-016-2917-6 – ident: e_1_3_3_56_2 doi: 10.1007/s00253-014-5698-3 – ident: e_1_3_3_65_2 doi: 10.1371/journal.ppat.1008652 |
| SSID | ssj0004068 |
| Score | 2.5022745 |
| Snippet | Copper radical alcohol oxidases (CRO-AlcOx), which have been recently discovered among fungal phytopathogens, are attractive for the production of fragrant... In the context of the industrial shift toward greener processes, the biocatalytic production of aldehydes is of utmost interest owing to their importance for... |
| SourceID | pubmedcentral hal proquest crossref asm2 pubmed |
| SourceType | Open Access Repository Aggregation Database Index Database |
| StartPage | e0152621 |
| SubjectTerms | Alcohol oxidase Alcohols Aldehydes Biochemistry, Molecular Biology Biotechnology Carbohydrates Colletotrichum Colletotrichum - enzymology Colletotrichum - genetics Copper Ethanol Fatty Acids - biosynthesis Fungal Proteins - genetics Fungal Proteins - metabolism Fungi Genomics Life Sciences Manganese Microbiology and Parasitology Mimicry Mycology Oxidoreductases - genetics Oxidoreductases - metabolism Proteins Proteomics Secretion Secretome Spotlight Spotlight Selection |
| Title | Identification of Copper-Containing Oxidoreductases in the Secretomes of Three Colletotrichum Species with a Focus on Copper Radical Oxidases for the Biocatalytic Production of Fatty Aldehydes |
| URI | https://www.ncbi.nlm.nih.gov/pubmed/34613753 https://journals.asm.org/doi/10.1128/AEM.01526-21 https://www.proquest.com/docview/2606198927/abstract/ https://search.proquest.com/docview/2580016880 https://hal.science/hal-03619439 https://pubmed.ncbi.nlm.nih.gov/PMC8612266 |
| Volume | 87 |
| hasFullText | 1 |
| inHoldings | 1 |
| isFullTextHit | |
| isPrint | |
| link | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwELfWSgh4QFBgBMZkJnh02ziJ4zxW1aryUZhgk_YW2bGtVlqSak0R_e_40zg7cVlBvPAaX2JHvvP97nwfCL2VIZyK3MQEoHBGYhoXRJhYEaVCkTKA2MYliS0-s_lV_OE6uT5Cic-FcUH7hVwNq5tyWK2WLrZyXRYjHyc2ulhMOahlUCyjHuqlUeRNdJ8MOWbcl560-spHu1M-mpwvhqD-KCPUdoiJYtBlqW2L3Bebkh5opt7SxkX-DTr_jJ28o4xmj9GjDkXiSbvaJ-hIVwN0r-0ruRug-z7deDNAD-9UHHyKfraJuabz1OHa4Gm9XutbYstUtd0i8JcfK9t_xFaCBR23wasKA0zE3yzCbOoSnsBrl8AEGju_Q1PbMv_LbYldN3sYt95dLPCsLrZAXHVz4K_C3Qq5CdyXATG7T8PKnR9pB_-DL9oitN3yZqJpdnhyo_Ryp_TmGbqanV9O56Rr4kBEzMcNMYoLixrD0FApQqUkB4hCE224ZtLQNBubwiTWmUJlbKhRTLJMMK0LOG3GInqO-lVd6RcIy5BnmgkjaAFWk4yyBIw7CYCJqkhnqQjQmd3HvJPCTe4MHMpz2Pfc7XtOwwC987ucr9uCHv-gOwMW2JPYKtzzyafcPgOlD6uNsu9AdOI55PesYCEyG4lG0wC92Q-D1NqrGFHpegs0CbdgGw7PAB23DLWfyrNlgNIDVjtYy-EICIqrDN4Jxsv_fvMVekBt0E4YEhqfoH5zu9WvAXU18hTsjfcfT52s_QJjvS0z |
| link.rule.ids | 230,315,733,786,790,891,27957,27958,53827,53829 |
| linkProvider | National Library of Medicine |
| linkToHtml | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV1bb9MwFD7aitDggUu5FQaYCR6TNm4uzmNVrSrQjol1aG-RndhqxZpUS4oov46fxrETl3WIB3iNndiWPp_znZNzAXgrPJSKTPkOUuHY8amfOlz5mZNlHo9CpNjKJIlNT8Lxuf_hIrjYg8Dmwpig_VQs3Pxy6eaLuYmtXC3Tro0T655OhwzVMiqW7j7cwvtKI2uk23TIXshs8UmtsWy8O2XdwfHURQVIQ4fqHjF9H7VZpBsjt3i5pDu6aX-uIyP_pJ03oyevqaPRffhiD1JHoXx115Vw0x83ajz-80kfwL2GoJJBPfwQ9mTehtt1y8pNGw5sJnPZhrvXihk-gp91zq9qnICkUGRYrFbyytEVsOpGFOTT94VubaKLzKL6LMkiJ8hAyZkmr1WxxCf42gzxJYlxaVSF7iAwXy_J2UqiGCqJdhwTTkZFusbJebMG-czNDyezgPkyknHzady5cVFt8DzktK5v22xvxKtqQwaXmZxvMlk-hvPR8Ww4dpr-EA73Wa9yVMa4JqSep6jgXpYJhuyHBlIxGQpFo7inUhVoPw0VvqIqC0UY81DKFAVZj_efQCsvcvkMiPBYLEOuOE3RIBP9OEC7USAXo1lfxhHvwJEGSNJc8DIxthNlCQIqMYBKqNeBdxY-yaquFfKXeUeIre0UXeB7PJgk-hnyCdxtP_6Gkw4t9H6visZnqIPcaNSBN9thFAj6Lw_PZbHGOQHTPB7lcgee1kjdLmXx3oFoB8M7e9kdQWSaouMNEp__95uv4WA8m06SyfuTjy_gDtWxQZ7nUP8QWtXVWr5EcleJV-Yq_wINnk4x |
| linkToPdf | http://utb.summon.serialssolutions.com/2.0.0/link/0/eLvHCXMwnV3db9MwED-xIr4e-ChfhQFmgsekjZsmzmNVVhVYR8U2aeIlsmNbrViTaEkR5a_jT-PsJKUd4mWvySW2pZ_vfnc-3wG8Ex5qRaZ9B6lw5PjUTxyufelI6fEwQIqt7SWx6XEwOfM_nQ_Ot1p92aT9RCzc9GLppou5za3Ml0m3yRPrzqYjhmYZDUs3l7q7Bzdxz9KocdSbK5G9gDUFKI3VanLeKesOD6cuGkEaONT0ien7aNFC0xy5xYsl3bFPe3OTHfkv9byaQbllksYP4FuzmCoT5bu7KoWb_LpS5_Faq30I92uiSoaVyCO4odI23KpaV67bcKe50Vy04d5WUcPH8Lu6-6vrYCDJNBllea4uHVMJq2pIQb78XJgWJ6bYLJrRgixSgkyUnBgSW2ZLfIKfnSLOFLGhjTIznQTmqyU5yRWqo4KYADLhZJwlKxRO6zHIV24PnuwA9s9Iyu2vceY2VLXG9ZBZVee2nt6Yl-WaDC-kmq-lKp7A2fjwdDRx6j4RDvdZr3S0ZNwQU8_TVHBPSsGQBdGB0kwFQtMw6ulED0y8hgpfUy0DEUQ8UCpBhdbj_afQSrNUPQciPBapgGtOE3TMRD8aoP8okJNR2VdRyDtwYEAS1xu9iK0PRVmMoIotqGLqdeB9A6E4r2qG_EfuAPG1ETGFvifDo9g8Q16Bs-1HP1Bov4Hf31HRCQ1MshsNO_B28xoVgznt4anKVigzYIbPo37uwLMKrZuhGsx3INzB8c5cdt8gOm3x8RqNL6795Ru4Pfswjo8-Hn9-CXepSRHyPIf6-9AqL1fqFXK8Ury2u_kPZHVQsQ |
| 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=Identification+of+Copper-Containing+Oxidoreductases+in+the+Secretomes+of+Three+Colletotrichum+Species+with+a+Focus+on+Copper+Radical+Oxidases+for+the+Biocatalytic+Production+of+Fatty+Aldehydes&rft.jtitle=Applied+and+environmental+microbiology&rft.au=Ribeaucourt%2C+David&rft.au=Saker%2C+Safwan&rft.au=Navarro%2C+David&rft.au=Bissaro%2C+Bastien&rft.date=2021-11-24&rft.eissn=1098-5336&rft.volume=87&rft.issue=24&rft.spage=e0152621&rft_id=info:doi/10.1128%2FAEM.01526-21&rft_id=info%3Apmid%2F34613753&rft.externalDocID=34613753 |
| thumbnail_l | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/lc.gif&issn=0099-2240&client=summon |
| thumbnail_m | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/mc.gif&issn=0099-2240&client=summon |
| thumbnail_s | http://covers-cdn.summon.serialssolutions.com/index.aspx?isbn=/sc.gif&issn=0099-2240&client=summon |