The Potential of Peroxidases Extracted from the Spent Mushroom (Flammulina velutipes) Substrate Significantly Degrade Mycotoxin Deoxynivalenol

Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of Fusarium graminearum KR1 and the degradation of DO...

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Published inToxins Vol. 13; no. 1; p. 72
Main Authors Tso, Ko-Hua, Lumsangkul, Chompunut, Ju, Jyh-Cherng, Fan, Yang-Kwang, Chiang, Hsin-I
Format Journal Article
LanguageEnglish
Published Switzerland MDPI AG 19.01.2021
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Abstract Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of Fusarium graminearum KR1 and the degradation of DON by MnP and LiP extracted from SMS. The results from the 7-day treatment period showed that mycelium inhibition of F. graminearum KR1 by MnP and LiP were 23.7% and 74.7%, respectively. Deoxynivalenol production in the mycelium of F. graminearum KR1 was undetectable after treatment with 50 U/mL of MnP or LiP for 7 days. N-acetyl-D-glucosamine (GlcNAc) content and chitinase activity both increased in the hyphae of F. graminearum KR1 after treatment with MnP and LiP for 1, 3, and 6 h, respectively. At 12 h, only the LiP-treated group had higher chitinase activity and GlcNAc content than those of the control group (p < 0.05). However, more than 60% of DON degradabilities (0.5 mg/kg, 1 h) were observed under various pH values (2.5, 4.5, and 6.5) in both MnP (50 U/g) and LiP (50 U/g) groups, while DON degradability at 1 mg/kg was 85.5% after 50 U/g of LiP treatment for 7 h in simulated pig gastrointestinal tracts. Similarly, DON degradability at 5 mg/kg was 67.1% after LiP treatment for 4.5 h in simulated poultry gastrointestinal tracts. The present study demonstrated that SMS-extracted peroxidases, particularly LiP, could effectively degrade DON and inhibit the mycelium growth of F. graminearum KR1.
AbstractList Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of Fusarium graminearum KR1 and the degradation of DON by MnP and LiP extracted from SMS. The results from the 7-day treatment period showed that mycelium inhibition of F. graminearum KR1 by MnP and LiP were 23.7% and 74.7%, respectively. Deoxynivalenol production in the mycelium of F. graminearum KR1 was undetectable after treatment with 50 U/mL of MnP or LiP for 7 days. N-acetyl-D-glucosamine (GlcNAc) content and chitinase activity both increased in the hyphae of F. graminearum KR1 after treatment with MnP and LiP for 1, 3, and 6 h, respectively. At 12 h, only the LiP-treated group had higher chitinase activity and GlcNAc content than those of the control group (p < 0.05). However, more than 60% of DON degradabilities (0.5 mg/kg, 1 h) were observed under various pH values (2.5, 4.5, and 6.5) in both MnP (50 U/g) and LiP (50 U/g) groups, while DON degradability at 1 mg/kg was 85.5% after 50 U/g of LiP treatment for 7 h in simulated pig gastrointestinal tracts. Similarly, DON degradability at 5 mg/kg was 67.1% after LiP treatment for 4.5 h in simulated poultry gastrointestinal tracts. The present study demonstrated that SMS-extracted peroxidases, particularly LiP, could effectively degrade DON and inhibit the mycelium growth of F. graminearum KR1.
Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of Fusarium graminearum KR1 and the degradation of DON by MnP and LiP extracted from SMS. The results from the 7-day treatment period showed that mycelium inhibition of F. graminearum KR1 by MnP and LiP were 23.7% and 74.7%, respectively. Deoxynivalenol production in the mycelium of F. graminearum KR1 was undetectable after treatment with 50 U/mL of MnP or LiP for 7 days. N -acetyl-D-glucosamine (GlcNAc) content and chitinase activity both increased in the hyphae of F. graminearum KR1 after treatment with MnP and LiP for 1, 3, and 6 h, respectively. At 12 h, only the LiP-treated group had higher chitinase activity and GlcNAc content than those of the control group ( p < 0.05). However, more than 60% of DON degradabilities (0.5 mg/kg, 1 h) were observed under various pH values (2.5, 4.5, and 6.5) in both MnP (50 U/g) and LiP (50 U/g) groups, while DON degradability at 1 mg/kg was 85.5% after 50 U/g of LiP treatment for 7 h in simulated pig gastrointestinal tracts. Similarly, DON degradability at 5 mg/kg was 67.1% after LiP treatment for 4.5 h in simulated poultry gastrointestinal tracts. The present study demonstrated that SMS-extracted peroxidases, particularly LiP, could effectively degrade DON and inhibit the mycelium growth of F. graminearum KR1.
Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of Fusarium graminearum KR1 and the degradation of DON by MnP and LiP extracted from SMS. The results from the 7-day treatment period showed that mycelium inhibition of F. graminearum KR1 by MnP and LiP were 23.7% and 74.7%, respectively. Deoxynivalenol production in the mycelium of F. graminearum KR1 was undetectable after treatment with 50 U/mL of MnP or LiP for 7 days. N-acetyl-D-glucosamine (GlcNAc) content and chitinase activity both increased in the hyphae of F. graminearum KR1 after treatment with MnP and LiP for 1, 3, and 6 h, respectively. At 12 h, only the LiP-treated group had higher chitinase activity and GlcNAc content than those of the control group (p < 0.05). However, more than 60% of DON degradabilities (0.5 mg/kg, 1 h) were observed under various pH values (2.5, 4.5, and 6.5) in both MnP (50 U/g) and LiP (50 U/g) groups, while DON degradability at 1 mg/kg was 85.5% after 50 U/g of LiP treatment for 7 h in simulated pig gastrointestinal tracts. Similarly, DON degradability at 5 mg/kg was 67.1% after LiP treatment for 4.5 h in simulated poultry gastrointestinal tracts. The present study demonstrated that SMS-extracted peroxidases, particularly LiP, could effectively degrade DON and inhibit the mycelium growth of F. graminearum KR1.Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of Fusarium graminearum KR1 and the degradation of DON by MnP and LiP extracted from SMS. The results from the 7-day treatment period showed that mycelium inhibition of F. graminearum KR1 by MnP and LiP were 23.7% and 74.7%, respectively. Deoxynivalenol production in the mycelium of F. graminearum KR1 was undetectable after treatment with 50 U/mL of MnP or LiP for 7 days. N-acetyl-D-glucosamine (GlcNAc) content and chitinase activity both increased in the hyphae of F. graminearum KR1 after treatment with MnP and LiP for 1, 3, and 6 h, respectively. At 12 h, only the LiP-treated group had higher chitinase activity and GlcNAc content than those of the control group (p < 0.05). However, more than 60% of DON degradabilities (0.5 mg/kg, 1 h) were observed under various pH values (2.5, 4.5, and 6.5) in both MnP (50 U/g) and LiP (50 U/g) groups, while DON degradability at 1 mg/kg was 85.5% after 50 U/g of LiP treatment for 7 h in simulated pig gastrointestinal tracts. Similarly, DON degradability at 5 mg/kg was 67.1% after LiP treatment for 4.5 h in simulated poultry gastrointestinal tracts. The present study demonstrated that SMS-extracted peroxidases, particularly LiP, could effectively degrade DON and inhibit the mycelium growth of F. graminearum KR1.
Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin peroxidase (LiP) and its potential. The present study investigated the growth inhibition of KR1 and the degradation of DON by MnP and LiP extracted from SMS. The results from the 7-day treatment period showed that mycelium inhibition of KR1 by MnP and LiP were 23.7% and 74.7%, respectively. Deoxynivalenol production in the mycelium of KR1 was undetectable after treatment with 50 U/mL of MnP or LiP for 7 days. -acetyl-D-glucosamine (GlcNAc) content and chitinase activity both increased in the hyphae of KR1 after treatment with MnP and LiP for 1, 3, and 6 h, respectively. At 12 h, only the LiP-treated group had higher chitinase activity and GlcNAc content than those of the control group ( < 0.05). However, more than 60% of DON degradabilities (0.5 mg/kg, 1 h) were observed under various pH values (2.5, 4.5, and 6.5) in both MnP (50 U/g) and LiP (50 U/g) groups, while DON degradability at 1 mg/kg was 85.5% after 50 U/g of LiP treatment for 7 h in simulated pig gastrointestinal tracts. Similarly, DON degradability at 5 mg/kg was 67.1% after LiP treatment for 4.5 h in simulated poultry gastrointestinal tracts. The present study demonstrated that SMS-extracted peroxidases, particularly LiP, could effectively degrade DON and inhibit the mycelium growth of KR1.
Author Lumsangkul, Chompunut
Fan, Yang-Kwang
Tso, Ko-Hua
Chiang, Hsin-I
Ju, Jyh-Cherng
AuthorAffiliation 1 Department of Animal Science, National Chung Hsing University, Taichung 40227, Taiwan; d100037004@mail.nchu.edu.tw
5 Department of Bioinformatics and Medical Engineering, College of Information and Electrical Engineering, Asia University, Taichung 41354, Taiwan
2 Department of Animal and Aquatic Sciences, Faculty of Agriculture, Chiang Mai University, Chiang Mai 50200, Thailand; chompunut.lum@cmu.ac.th
3 Graduate Institute of Biomedical Sciences, China Medical University, Taichung 40402, Taiwan
4 Translational Medicine Research Center, China Medical University Hospital, Taichung 40402, Taiwan
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– name: 3 Graduate Institute of Biomedical Sciences, China Medical University, Taichung 40402, Taiwan
– name: 1 Department of Animal Science, National Chung Hsing University, Taichung 40227, Taiwan; d100037004@mail.nchu.edu.tw
– name: 5 Department of Bioinformatics and Medical Engineering, College of Information and Electrical Engineering, Asia University, Taichung 41354, Taiwan
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Cites_doi 10.1007/978-1-4615-0629-4_29
10.3390/jof4030091
10.1007/s00253-011-3401-5
10.3390/toxins2030353
10.1080/19440040903571747
10.3390/toxins11100566
10.1080/02757540.2015.1094465
10.1016/j.heliyon.2020.e03170
10.1007/s002530100756
10.1186/s12896-017-0338-5
10.1007/s11274-005-9078-0
10.3390/ijms9030371
10.1590/S1517-83822014005000026
10.1080/00039420400020066
10.1099/mic.0.029546-0
10.3168/jds.2019-17561
10.1111/j.1472-765X.2010.02803.x
10.3390/molecules15063775
10.1590/S1516-89132006000600002
10.1111/j.1574-6968.2010.02158.x
10.1111/jam.13542
10.1021/jf061008g
10.1016/j.fct.2006.07.028
10.1371/journal.pone.0088028
10.3390/toxins12010049
10.1155/2013/714639
10.3390/toxins9020063
10.1007/s00253-010-2857-z
10.1098/rsif.2010.0131
10.3390/ijms14024283
10.1002/jobm.200510014
10.1080/02652030500058403
10.1016/j.enzmictec.2004.09.006
10.3390/toxins8040094
10.1080/10408398.2019.1658570
10.1007/s00294-009-0258-6
10.3390/foods9020137
10.1016/S1872-2040(15)60794-0
10.1080/03601234.2017.1356672
10.20944/preprints201811.0116.v1
10.1590/S0101-20612011000100030
10.1016/S0141-0229(01)00528-2
10.1016/j.funbio.2016.02.002
10.1016/j.tifs.2018.03.008
10.3390/toxins11100599
10.1021/jf200767q
10.1080/02652030110091154
10.1128/AEM.03227-12
10.1007/s12550-016-0260-z
10.1007/s10532-008-9185-3
10.5053/ejobios.2009.3.0.8
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Keywords deoxynivalenol
lignin peroxidase
Fusarium graminearum
detoxification
manganese peroxidase
Language English
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References Schalchli (ref_34) 2017; 123
Cho (ref_51) 2013; 14
Wang (ref_15) 2015; 43
ref_12
ref_11
ref_10
ref_53
Hofrichter (ref_28) 2002; 30
Kihal (ref_16) 2020; 103
Asgher (ref_41) 2008; 19
Wang (ref_29) 2011; 314
Ikunaga (ref_22) 2011; 89
Kumar (ref_27) 2020; 6
Parra (ref_6) 2011; 8
Feltrin (ref_32) 2017; 52
Shi (ref_52) 2008; 9
Zhang (ref_39) 2016; 120
Akyuz (ref_33) 2009; 10
ref_24
Tychanowicz (ref_49) 2006; 46
Bansal (ref_40) 2013; 2013
Gardiner (ref_4) 2009; 155
Kim (ref_38) 2009; 55
Awad (ref_20) 2010; 27
Ito (ref_23) 2013; 79
Dakovic (ref_17) 2000; 50
Eskola (ref_2) 2020; 60
Springler (ref_9) 2017; 33
ref_30
Leontievsky (ref_48) 2001; 57
Bretz (ref_13) 2006; 54
Doll (ref_14) 2004; 58
(ref_19) 2010; 15
ref_37
Li (ref_3) 2011; 59
Karlovsky (ref_26) 2011; 91
Kupski (ref_31) 2011; 31
Rocha (ref_8) 2005; 22
cr-split#-ref_18.1
Vinale (ref_36) 2010; 50
cr-split#-ref_18.2
Tychanowicz (ref_50) 2006; 49
Magan (ref_5) 2010; 2
Christian (ref_47) 2005; 36
ref_46
Schalchli (ref_35) 2015; 31
ref_43
ref_42
ref_1
Young (ref_21) 2007; 45
Yehia (ref_44) 2014; 45
Fuchs (ref_25) 2002; 19
Park (ref_54) 2002; 504
Couto (ref_45) 2006; 22
Moretti (ref_7) 2019; 84
References_xml – volume: 504
  start-page: 277
  year: 2002
  ident: ref_54
  article-title: US perspective on mycotoxin regulatory issues
  publication-title: Mycotoxins Food Saf.
  doi: 10.1007/978-1-4615-0629-4_29
– ident: ref_37
  doi: 10.3390/jof4030091
– volume: 91
  start-page: 491
  year: 2011
  ident: ref_26
  article-title: Biological detoxification of the mycotoxin deoxynivalenol and its use in genetically engineered crops and feed additives
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-011-3401-5
– volume: 2
  start-page: 353
  year: 2010
  ident: ref_5
  article-title: Environmental factors and interactions with mycobiota of grain and grapes: Effects on growth, deoxynivalenol and ochratoxin production by Fusarium culmorum and Aspergillus carbonarius
  publication-title: Toxins
  doi: 10.3390/toxins2030353
– volume: 27
  start-page: 510
  year: 2010
  ident: ref_20
  article-title: Decontamination and detoxification strategies for the Fusarium mycotoxin deoxynivalenol in animal feed and the effectiveness of microbial biodegradation
  publication-title: Food Addit. Contam. Part A Chem. Anal. Control. Expo. Risk Assess.
  doi: 10.1080/19440040903571747
– ident: ref_30
  doi: 10.3390/toxins11100566
– volume: 31
  start-page: 754
  year: 2015
  ident: ref_35
  article-title: Volatiles from white-rot fungi for controlling plant pathogenic fungi
  publication-title: Chem. Ecol.
  doi: 10.1080/02757540.2015.1094465
– volume: 6
  start-page: e03170
  year: 2020
  ident: ref_27
  article-title: Ligninolytic enzymes and its mechanisms for degradation of lignocellulosic waste in environment
  publication-title: Heliyon
  doi: 10.1016/j.heliyon.2020.e03170
– volume: 57
  start-page: 85
  year: 2001
  ident: ref_48
  article-title: Transformation of 2,4,6-trichlorophenol by free and immobilized fungal laccase
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s002530100756
– ident: ref_46
  doi: 10.1186/s12896-017-0338-5
– volume: 22
  start-page: 607
  year: 2006
  ident: ref_45
  article-title: Optimum stability conditions of pH and temperature for ligninase and manganese-dependent peroxidase from Phanerochaete chrysosporium. Application to in vitro decolorization of Poly R-478 by MnP
  publication-title: World J. Microb. Biot.
  doi: 10.1007/s11274-005-9078-0
– volume: 9
  start-page: 371
  year: 2008
  ident: ref_52
  article-title: Fusarium graminearum growth inhibition due to glucose starvation caused by osthol
  publication-title: Int. J. Mol. Sci.
  doi: 10.3390/ijms9030371
– volume: 45
  start-page: 127
  year: 2014
  ident: ref_44
  article-title: Aflatoxin detoxification by manganese peroxidase purified from Pleurotus ostreatus
  publication-title: Braz. J. Microbiol.
  doi: 10.1590/S1517-83822014005000026
– volume: 58
  start-page: 419
  year: 2004
  ident: ref_14
  article-title: In vivo detoxification of Fusarium toxins
  publication-title: Arch. Anim. Nutr.
  doi: 10.1080/00039420400020066
– volume: 155
  start-page: 3149
  year: 2009
  ident: ref_4
  article-title: Low pH regulates the production of deoxynivalenol by Fusarium graminearum
  publication-title: Microbiol. Sgm.
  doi: 10.1099/mic.0.029546-0
– volume: 103
  start-page: 3125
  year: 2020
  ident: ref_16
  article-title: In vitro assessment of the capacity of certain mycotoxin binders to adsorb some amino acids and water-soluble vitamins
  publication-title: J. Dairy Sci.
  doi: 10.3168/jds.2019-17561
– volume: 50
  start-page: 380
  year: 2010
  ident: ref_36
  article-title: Secondary metabolites produced by a root-inhabiting sterile fungus antagonistic towards pathogenic fungi
  publication-title: Lett. Appl. Microbiol.
  doi: 10.1111/j.1472-765X.2010.02803.x
– ident: #cr-split#-ref_18.1
– volume: 15
  start-page: 3775
  year: 2010
  ident: ref_19
  article-title: Thiazolo[3,2-a]benzimidazoles: Synthetic strategies, chemical transformations and biological activities
  publication-title: Molecules
  doi: 10.3390/molecules15063775
– volume: 49
  start-page: 699
  year: 2006
  ident: ref_50
  article-title: Copper improves the production of laccase by the white-rot fungus Pleurotus pulmonarius in solid state fermentation
  publication-title: Braz. Arch. Biol. Technol.
  doi: 10.1590/S1516-89132006000600002
– volume: 314
  start-page: 164
  year: 2011
  ident: ref_29
  article-title: Detoxification of aflatoxin B1 by manganese peroxidase from the white-rot fungus Phanerochaete sordida YK-624
  publication-title: FEMS. Microbiol. Lett.
  doi: 10.1111/j.1574-6968.2010.02158.x
– volume: 123
  start-page: 886
  year: 2017
  ident: ref_34
  article-title: Production of ligninolytic enzymes and some diffusible antifungal compounds by white-rot fungi using potato solid wastes as the sole nutrient source
  publication-title: J. Appl. Microbiol.
  doi: 10.1111/jam.13542
– volume: 54
  start-page: 6445
  year: 2006
  ident: ref_13
  article-title: Thermal degradation of the Fusarium mycotoxin deoxynivalenol
  publication-title: J. Agric. Food Chem.
  doi: 10.1021/jf061008g
– volume: 45
  start-page: 136
  year: 2007
  ident: ref_21
  article-title: Degradation of trichothecene mycotoxins by chicken intestinal microbes
  publication-title: Food Chem. Toxicol.
  doi: 10.1016/j.fct.2006.07.028
– ident: ref_10
  doi: 10.1371/journal.pone.0088028
– volume: 50
  start-page: 23
  year: 2000
  ident: ref_17
  article-title: Adsorpton effects of mineral adsorbents; Part III: Adsorption behaviour in the presence of vitamin B6 and microelements
  publication-title: Acta. Vet. Beogr.
– ident: ref_43
  doi: 10.3390/toxins12010049
– volume: 2013
  start-page: 714639
  year: 2013
  ident: ref_40
  article-title: Peroxidase(s) in environment protection
  publication-title: Sci. World J.
  doi: 10.1155/2013/714639
– ident: #cr-split#-ref_18.2
– ident: ref_24
  doi: 10.3390/toxins9020063
– volume: 89
  start-page: 419
  year: 2011
  ident: ref_22
  article-title: Nocardioides sp. strain WSN05-2, isolated from a wheat field, degrades deoxynivalenol, producing the novel intermediate 3-epi-deoxynivalenol
  publication-title: Appl. Microbiol. Biotechnol.
  doi: 10.1007/s00253-010-2857-z
– volume: 8
  start-page: 117
  year: 2011
  ident: ref_6
  article-title: Modelling the relationship between environmental factors, transcriptional genes and deoxynivalenol mycotoxin production by strains of two Fusarium species
  publication-title: J. R. Soc. Interface
  doi: 10.1098/rsif.2010.0131
– volume: 14
  start-page: 4283
  year: 2013
  ident: ref_51
  article-title: Effect of Nanoencapsulated vitamin B1 derivative on inhibition of both mycelial growth and spore germination of Fusarium oxysporum f. sp. raphani
  publication-title: Int. J. Mol. Sci.
  doi: 10.3390/ijms14024283
– volume: 46
  start-page: 126
  year: 2006
  ident: ref_49
  article-title: Co-production of ligninolytic enzymes by Pleurotus pulmonarius on wheat bran solid state cultures
  publication-title: J. Basic Microbiol.
  doi: 10.1002/jobm.200510014
– volume: 22
  start-page: 369
  year: 2005
  ident: ref_8
  article-title: Effects of trichothecene mycotoxins on eukaryotic cells: A review
  publication-title: Food Addit. Contam.
  doi: 10.1080/02652030500058403
– ident: ref_11
– volume: 36
  start-page: 327
  year: 2005
  ident: ref_47
  article-title: Mediator role of veratryl alcohol in the lignin peroxidase-catalyzed oxidative decolorization of Remazol Brilliant Blue R
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/j.enzmictec.2004.09.006
– ident: ref_1
  doi: 10.3390/toxins8040094
– volume: 60
  start-page: 2773
  year: 2020
  ident: ref_2
  article-title: Worldwide contamination of food-crops with mycotoxins: Validity of the widely cited ‘FAO estimate’ of 25
  publication-title: Crit. Rev. Food Sci. Nutr.
  doi: 10.1080/10408398.2019.1658570
– volume: 55
  start-page: 449
  year: 2009
  ident: ref_38
  article-title: Gibberella zeae chitin synthase genes, GzCHS5 and GzCHS7, are required for hyphal growth, perithecia formation, and pathogenicity
  publication-title: Curr. Genet.
  doi: 10.1007/s00294-009-0258-6
– ident: ref_12
  doi: 10.3390/foods9020137
– volume: 43
  start-page: 1
  year: 2015
  ident: ref_15
  article-title: Liquid chromatography-tandem mass spectrometry for determination of aflatoxin B1, deoxynivalenol and zearalenone in artificial porcine gastrointestinal digestive juice
  publication-title: Chin. J. Anal. Chem.
  doi: 10.1016/S1872-2040(15)60794-0
– volume: 52
  start-page: 777
  year: 2017
  ident: ref_32
  article-title: Characterization and application of the enzyme peroxidase to the degradation of the mycotoxin DON
  publication-title: J. Environ. Sci. Health B
  doi: 10.1080/03601234.2017.1356672
– ident: ref_42
  doi: 10.20944/preprints201811.0116.v1
– volume: 31
  start-page: 198
  year: 2011
  ident: ref_31
  article-title: Deoxynivalenol (DON) degradation and peroxidase enzyme activity in submerged fermentation
  publication-title: Cienc. E. Tecnol. Alime.
  doi: 10.1590/S0101-20612011000100030
– volume: 30
  start-page: 454
  year: 2002
  ident: ref_28
  article-title: Review: Lignin conversion by manganese peroxidase (MnP)
  publication-title: Enzyme Microb. Technol.
  doi: 10.1016/S0141-0229(01)00528-2
– volume: 120
  start-page: 764
  year: 2016
  ident: ref_39
  article-title: Chitin synthase gene FgCHS8 affects virulence and fungal cell wall sensitivity to environmental stress in Fusarium graminearum
  publication-title: Fungal Biol.
  doi: 10.1016/j.funbio.2016.02.002
– volume: 84
  start-page: 38
  year: 2019
  ident: ref_7
  article-title: Mycotoxin risks under a climate change scenario in Europe
  publication-title: Trends Food Sci. Technol.
  doi: 10.1016/j.tifs.2018.03.008
– ident: ref_53
  doi: 10.3390/toxins11100599
– volume: 59
  start-page: 3441
  year: 2011
  ident: ref_3
  article-title: T-2 toxin, a trichothecene mycotoxin: Review of toxicity, metabolism, and analytical methods
  publication-title: J. Agric. Food Chem.
  doi: 10.1021/jf200767q
– volume: 19
  start-page: 379
  year: 2002
  ident: ref_25
  article-title: Structural characterization of metabolites after the microbial degradation of type A trichothecenes by the bacterial strain BBSH 797
  publication-title: Food Addit. Contam.
  doi: 10.1080/02652030110091154
– volume: 79
  start-page: 1619
  year: 2013
  ident: ref_23
  article-title: Bacterial cytochrome P450 system catabolizing the Fusarium toxin deoxynivalenol
  publication-title: Appl. Environ. Microbiol.
  doi: 10.1128/AEM.03227-12
– volume: 33
  start-page: 25
  year: 2017
  ident: ref_9
  article-title: Deoxynivalenol and its metabolite deepoxy-deoxynivalenol: Multi-parameter analysis for the evaluation of cytotoxicity and cellular effects
  publication-title: Mycotoxin Res.
  doi: 10.1007/s12550-016-0260-z
– volume: 19
  start-page: 771
  year: 2008
  ident: ref_41
  article-title: Recent developments in biodegradation of industrial pollutants by white rot fungi and their enzyme system
  publication-title: Biodegradation
  doi: 10.1007/s10532-008-9185-3
– volume: 10
  start-page: 58
  year: 2009
  ident: ref_33
  article-title: Antimicrobial activity of Pleurotus eryngii var. ferulae grown on various agro-wastes
  publication-title: Eurasia J. Biosci.
  doi: 10.5053/ejobios.2009.3.0.8
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Snippet Little is known about the degradability of mycotoxin deoxynivalenol (DON) by the spent mushroom substrate (SMS)-derived manganese peroxidase (MnP) and lignin...
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StartPage 72
SubjectTerms Animals
Cell division
Chitinase
Climate change
Degradability
Degradation
Deoxynivalenol
detoxification
Enzymes
Feeds
Food
Fungi
Fusarium graminearum
Glucosamine
Hyphae
Lignin
Lignin peroxidase
Manganese
Manganese peroxidase
Microorganisms
Morphology
Mushrooms
Mycotoxins
N-Acetylglucosamine
Peroxidase
Simulation
Substrates
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Title The Potential of Peroxidases Extracted from the Spent Mushroom (Flammulina velutipes) Substrate Significantly Degrade Mycotoxin Deoxynivalenol
URI https://www.ncbi.nlm.nih.gov/pubmed/33478106
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https://www.proquest.com/docview/2480404449
https://pubmed.ncbi.nlm.nih.gov/PMC7835844
https://doaj.org/article/38c087536da4412383d6b68be5c1d428
Volume 13
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