A complex metabolic network and its biomarkers regulate laccase production in white-rot fungus Cerrena unicolor 87613.
Cerrena unicolor
Fructose
Laccase production
Metabolic networks
Regulation mechanism
White rot fungi
Journal
Microbial cell factories
ISSN: 1475-2859
Titre abrégé: Microb Cell Fact
Pays: England
ID NLM: 101139812
Informations de publication
Date de publication:
08 Jun 2024
08 Jun 2024
Historique:
received:
12
03
2024
accepted:
29
05
2024
medline:
8
6
2024
pubmed:
8
6
2024
entrez:
7
6
2024
Statut:
epublish
Résumé
White-rot fungi are known to naturally produce high quantities of laccase, which exhibit commendable stability and catalytic efficiency. However, their laccase production does not meet the demands for industrial-scale applications. To address this limitation, it is crucial to optimize the conditions for laccase production. However, the regulatory mechanisms underlying different conditions remain unclear. This knowledge gap hinders the cost-effective application of laccases. In this study, we utilized transcriptomic and metabolomic data to investigate a promising laccase producer, Cerrena unicolor 87613, cultivated with fructose as the carbon source. Our comprehensive analysis of differentially expressed genes (DEGs) and differentially abundant metabolites (DAMs) aimed to identify changes in cellular processes that could affect laccase production. As a result, we discovered a complex metabolic network primarily involving carbon metabolism and amino acid metabolism, which exhibited contrasting changes between transcription and metabolic patterns. Within this network, we identified five biomarkers, including succinate, serine, methionine, glutamate and reduced glutathione, that played crucial roles in co-determining laccase production levels. Our study proposed a complex metabolic network and identified key biomarkers that determine the production level of laccase in the commercially promising Cerrena unicolor 87613. These findings not only shed light on the regulatory mechanisms of carbon sources in laccase production, but also provide a theoretical foundation for enhancing laccase production through strategic reprogramming of metabolic pathways, especially related to the citrate cycle and specific amino acid metabolism.
Sections du résumé
BACKGROUND
BACKGROUND
White-rot fungi are known to naturally produce high quantities of laccase, which exhibit commendable stability and catalytic efficiency. However, their laccase production does not meet the demands for industrial-scale applications. To address this limitation, it is crucial to optimize the conditions for laccase production. However, the regulatory mechanisms underlying different conditions remain unclear. This knowledge gap hinders the cost-effective application of laccases.
RESULTS
RESULTS
In this study, we utilized transcriptomic and metabolomic data to investigate a promising laccase producer, Cerrena unicolor 87613, cultivated with fructose as the carbon source. Our comprehensive analysis of differentially expressed genes (DEGs) and differentially abundant metabolites (DAMs) aimed to identify changes in cellular processes that could affect laccase production. As a result, we discovered a complex metabolic network primarily involving carbon metabolism and amino acid metabolism, which exhibited contrasting changes between transcription and metabolic patterns. Within this network, we identified five biomarkers, including succinate, serine, methionine, glutamate and reduced glutathione, that played crucial roles in co-determining laccase production levels.
CONCLUSIONS
CONCLUSIONS
Our study proposed a complex metabolic network and identified key biomarkers that determine the production level of laccase in the commercially promising Cerrena unicolor 87613. These findings not only shed light on the regulatory mechanisms of carbon sources in laccase production, but also provide a theoretical foundation for enhancing laccase production through strategic reprogramming of metabolic pathways, especially related to the citrate cycle and specific amino acid metabolism.
Identifiants
pubmed: 38849849
doi: 10.1186/s12934-024-02443-9
pii: 10.1186/s12934-024-02443-9
doi:
Substances chimiques
Laccase
EC 1.10.3.2
Biomarkers
0
Carbon
7440-44-0
Fructose
30237-26-4
Fungal Proteins
0
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
167Subventions
Organisme : Natural Science Foundation of Fujian Province, China
ID : 2021J01605
Organisme : Fujian Major Research Grants for Young and Middle－aged Health Professionals
ID : 2021ZQNZD012
Organisme : Foundation of Marine Bioenzyme Engineering Innovation Service Platform
ID : 2014FJPT02
Informations de copyright
© 2024. The Author(s).
Références
Lin S, Wei J, Yang B, Zhang M, Zhuo R. Bioremediation of organic pollutants by white rot fungal cytochrome P450: the role and mechanism of CYP450 in biodegradation. Chemosphere. 2022;301:134776. https://doi.org/10.1016/j.chemosphere.2022.134776 .
doi: 10.1016/j.chemosphere.2022.134776
pubmed: 35500631
Gao X, Wei M, Zhang X, Xun Y, Duan M, Yang Z, Zhu M, Zhu Y, Zhuo R. Copper removal from aqueous solutions by white rot fungus Pleurotus Ostreatus GEMB-PO1 and its potential in co-remediation of copper and organic pollutants. Bioresour Technol. 2024;395:130337. https://doi.org/10.1016/j.biortech.2024.130337 .
doi: 10.1016/j.biortech.2024.130337
pubmed: 38244937
Chen S, Zhu M, Guo X, Yang B, Zhuo R. Coupling of Fenton reaction and white rot fungi for the degradation of organic pollutants. Ecotoxicol Environ Saf. 2023;254:114697. https://doi.org/10.1016/j.ecoenv.2023.114697 .
doi: 10.1016/j.ecoenv.2023.114697
pubmed: 36889210
Chen L, Zhang X, Zhang M, Zhu YH, Zhou R. Removal of heavy-metal pollutants by white rot fungi: mechanisms, achievements, and perspectives. J Clean Prod. 2022;354:131681. https://doi.org/10.1016/j.jclepro.2022.131681 .
doi: 10.1016/j.jclepro.2022.131681
Ziaja-Soltys M, Kolodziej P, Stefaniuk D, Matuszewska A, Jaszek M, Bogucka-Kocka A. Low-molecular-weight secondary metabolites from fungi: Cerrena Unicolor as a new proposal of an effective preparation against Rhabditis nematodes. Molecules. 2022;27:1660. https://doi.org/10.3390/molecules27051660 .
doi: 10.3390/molecules27051660
pubmed: 35268762
pmcid: 8911859
Soares A, Wanderley LF, Costa Junior LM. The potential of plant and fungal proteins in the control of gastrointestinal nematodes from animals. Rev Bras Parasitol Vet. 2019;28:339–45. https://doi.org/10.1590/S1984-29612019046 .
doi: 10.1590/S1984-29612019046
pubmed: 31291435
Matuszewska A, Stefaniuk D, Jaszek M, Piet M, Zajac A, Matuszewski L, Cios I, Graz M, Paduch R, Bancerz R. Antitumor potential of new low molecular weight antioxidative preparations from the white rot fungus Cerrena unicolor against human colon cancer cells. Sci Rep. 2019;91975. https://doi.org/10.1038/s41598-018-37947-z .
Matuszewska A, Jaszek M, Stefaniuk D, Ciszewski T, Matuszewski L. Anticancer, antioxidant, and antibacterial activities of low molecular weight bioactive subfractions isolated from cultures of wood degrading fungus Cerrena Unicolor. PLoS ONE. 2018;13:e0197044. https://doi.org/10.1371/journal.pone.0197044 .
doi: 10.1371/journal.pone.0197044
pubmed: 29874240
pmcid: 5991343
Ji X, Peng X, Long X, Zhang Y, Lin J, Yin J, Zhang R, Zhao G. Laccase-mediated functionalization of natamycin by gallic acids for the therapeutic effect on aspergillus fumigatus keratitis. Eur J Pharmacol. 2022;926:175041. https://doi.org/10.1016/j.ejphar.2022.175041 .
doi: 10.1016/j.ejphar.2022.175041
pubmed: 35597265
Jaszek M, Osinska-Jaroszuk M, Janusz G, Matuszewska A, Stefaniuk D, Sulej J, Polak J, Ruminowicz M, Grzywnowicz K, Jarosz-Wilkolazka A. New bioactive fungal molecules with high antioxidant and antimicrobial capacity isolated from Cerrena Unicolor idiophasic cultures. Biomed Res Int. 2013;2013:497492. https://doi.org/10.1155/2013/497492 .
doi: 10.1155/2013/497492
pubmed: 23936810
pmcid: 3727119
Khatami SH, Vakili O, Movahedpour A, Ghesmati Z, Ghasemi H, Taheri-Anganeh M. Laccase: various types and applications. Biotechnol Appl Biochem. 2022. https://doi.org/10.1002/bab.2313 .
doi: 10.1002/bab.2313
pubmed: 36445196
Janusz G, Pawlik A, Swiderska-Burek U, Polak J, Sulej J, Jarosz-Wilkolazka A, Paszczynski A. Laccase properties, physiological functions, and evolution. Int J Mol Sci. 2020;21. https://doi.org/10.3390/ijms21030966 .
Matuszewska A, Karp M, Jaszek M, Janusz G, Osinska-Jaroszuk M, Sulej J, Stefaniuk D, Tomczak W, Giannopoulos K. Laccase purified from Cerrena unicolor exerts antitumor activity against leukemic cells. Oncol Lett. 2016;11:2009–18. https://doi.org/10.3892/ol.2016.4220 .
doi: 10.3892/ol.2016.4220
pubmed: 26998114
pmcid: 4774592
Mizerska-Dudka M, Jaszek M, Blachowicz A, Rejczak TP, Matuszewska A, Osinska-Jaroszuk M, Stefaniuk D, Janusz G, Sulej J, Kandefer-Szerszen M. Fungus Cerrena unicolor as an effective source of new antiviral, immunomodulatory, and anticancer compounds. Int J Biol Macromol. 2015;79:459–68. https://doi.org/10.1016/j.ijbiomac.2015.05.015 .
doi: 10.1016/j.ijbiomac.2015.05.015
pubmed: 26003302
Dong CD, Tiwari A, Anisha GS, Chen CW, Singh A, Haldar D, Patel AK, Singhania RR. Laccase: a potential biocatalyst for pollutant degradation. Environ Pollut. 2023;319:120999. https://doi.org/10.1016/j.envpol.2023.120999 .
doi: 10.1016/j.envpol.2023.120999
pubmed: 36608728
Zhuo R, Fan F. A comprehensive insight into the application of white rot fungi and their lignocellulolytic enzymes in the removal of organic pollutants. Sci Total Environ. 2021;778:146132. https://doi.org/10.1016/j.scitotenv.2021.146132 .
doi: 10.1016/j.scitotenv.2021.146132
pubmed: 33714829
Antosova Z, Sychrova H. Yeast hosts for the production of recombinant laccases: a review. Mol Biotechnol. 2016;58:93–116. https://doi.org/10.1007/s12033-015-9910-1 .
doi: 10.1007/s12033-015-9910-1
pubmed: 26698313
Yang J, Li W, Ng TB, Deng X, Lin J, Ye X. Laccases: production, expression regulation, and applications in pharmaceutical biodegradation. Front Microbiol. 2017;8:832. https://doi.org/10.3389/fmicb.2017.00832 .
doi: 10.3389/fmicb.2017.00832
pubmed: 28559880
pmcid: 5432550
Elisashvili V, Kachlishvili E. Physiological regulation of laccase and manganese peroxidase production by white-rot Basidiomycetes. J Biotechnol. 2009;144:37–42. https://doi.org/10.1016/j.jbiotec.2009.06.020 .
doi: 10.1016/j.jbiotec.2009.06.020
pubmed: 19559737
Bertrand B, Martinez-Morales F, Trejo-Hernandez MR. Upgrading laccase production and biochemical properties: strategies and challenges. Biotechnol Prog. 2017;33:1015–34. https://doi.org/10.1002/btpr.2482 .
doi: 10.1002/btpr.2482
pubmed: 28393483
Patel N, Shahane S, Shivam, Majumdar R, Mishra U. Mode of action, properties, production, and application of laccase: a review. Recent Pat Biotechnol. 2019;13:19–32. https://doi.org/10.2174/1872208312666180821161015 .
doi: 10.2174/1872208312666180821161015
pubmed: 30147019
Bettin F, Montanari Q, Calloni R, Gaio TA, Silveira MM, Dillon AJ. Production of laccases in submerged process by Pleurotus sajor-caju PS-2001 in relation to carbon and organic nitrogen sources, antifoams and tween 80. J Ind Microbiol Biotechnol. 2009;36:1–9. https://doi.org/10.1007/s10295-008-0463-1 .
doi: 10.1007/s10295-008-0463-1
pubmed: 18758836
Poojary H, Mugeraya G. Laccase production by Phellinus Noxius hpF17: optimization of submerged culture conditions by response surface methodology. Res Biotechnol. 2012;3:9–20.
Galhaup C, Goller S, Peterbauer CK, Strauss J, Haltrich D. Characterization of the major laccase isoenzyme from Trametes pubescens and regulation of its synthesis by metal ions. Microbiol (Reading). 2002;148:2159–69. https://doi.org/10.1099/00221287-148-7-2159 .
doi: 10.1099/00221287-148-7-2159
Eugenio ME, Carbajo JM, Martin JA, Gonzalez AE, Villar JC. Laccase production by Pycnoporus sanguineus under different culture conditions. J Basic Microbiol. 2009;49:433–40. https://doi.org/10.1002/jobm.200800347 .
doi: 10.1002/jobm.200800347
pubmed: 19322835
Revankar MS, Lele SS. Synthetic dye decolorization by white rot fungus, Ganoderma sp. WR-1. Bioresour Technol. 2007;98:775–80. https://doi.org/10.1016/j.biortech.2006.03.020 .
doi: 10.1016/j.biortech.2006.03.020
pubmed: 16730976
Hu J, Zhang Y, Xu Y, Sun Q, Liu J, Fang W, Xiao Y, Kues U, Fang Z. Gongronella sp. w5 elevates Coprinopsis Cinerea laccase production by carbon source syntrophism and secondary metabolite induction. Appl Microbiol Biotechnol. 2019;103:411–25. https://doi.org/10.1007/s00253-018-9469-4 .
doi: 10.1007/s00253-018-9469-4
pubmed: 30406450
Zhang LB, Deng ZQ, Qiu TT, Yang WWJ, Zhu F, Ye XY. Characterisation of a laccase isolated from Trametes hirsuta and its application in the oligomerisation of phenolic compounds. Fungal Biology. 2023;127:872–80. https://doi.org/10.1016/j.funbio.2022.11.005 .
doi: 10.1016/j.funbio.2022.11.005
pubmed: 36746559
Umar A, Ahmed S. Optimization, purification and characterization of laccase from Ganoderma leucocontextum along with its phylogenetic relationship. Sci Rep. 2022;12:2416. https://doi.org/10.1038/s41598-022-06111-z .
doi: 10.1038/s41598-022-06111-z
pubmed: 35165332
pmcid: 8844424
Kachlishvili E, Jokharidze T, Kobakhidze A, Elisashvili V. Enhancement of laccase production by Cerrena unicolor through fungal interspecies interaction and optimum conditions determination. Arch Microbiol. 2021;203:3905–17. https://doi.org/10.1007/s00203-021-02374-8 .
doi: 10.1007/s00203-021-02374-8
pubmed: 34014357
Zhou Z, Li R, Ng TB, Lai Y, Yang J, Ye X. A new laccase of Lac 2 from the white rot fungus Cerrena Unicolor 6884 and Lac 2-mediated degradation of aflatoxin B1. Toxins (Basel). 2020;12. https://doi.org/10.3390/toxins12080476 .
Zhang LB, Yang WW, Qiu TT. Genome-wide study of Cerrena Unicolor 87613 laccase gene family and their mode prediction in association with substrate oxidation. BMC Genomics. 2023;24:504. https://doi.org/10.1186/s12864-023-09606-9 .
doi: 10.1186/s12864-023-09606-9
pubmed: 37649000
pmcid: 10466755
Sherman BT, Hao M, Qiu J, Jiao X, Baseler MW, Lane HC, Imamichi T, Chang W. DAVID: a web server for functional enrichment analysis and functional annotation of gene lists (2021 update). Nucleic Acids Res. 2022;50:W216–21. https://doi.org/10.1093/nar/gkac194 .
doi: 10.1093/nar/gkac194
pubmed: 35325185
pmcid: 9252805
Du J, Yuan Z, Ma Z, Song J, Xie X, Chen Y. KEGG-PATH: Kyoto encyclopedia of genes and genomes-based pathway analysis using a path analysis model. Mol Biosyst. 2014;10:2441–7. https://doi.org/10.1039/c4mb00287c .
doi: 10.1039/c4mb00287c
pubmed: 24994036
Yuan M, Breitkopf SB, Yang X, Asara JM. A positive/negative ion-switching, targeted mass spectrometry-based metabolomics platform for bodily fluids, cells, and fresh and fixed tissue. Nat Protoc. 2012;7:872–81. https://doi.org/10.1038/nprot.2012.024 .
doi: 10.1038/nprot.2012.024
pubmed: 22498707
pmcid: 3685491
Wen B, Mei Z, Zeng C, Liu S. metaX: a flexible and comprehensive software for processing metabolomics data. BMC Bioinformatics. 2017;18:183. https://doi.org/10.1186/s12859-017-1579-y .
doi: 10.1186/s12859-017-1579-y
pubmed: 28327092
pmcid: 5361702
Pang Z, Zhou G, Ewald J, Chang L, Hacariz O, Basu N, Xia J. Using MetaboAnalyst 5.0 for LC-HRMS spectra processing, multi-omics integration and covariate adjustment of global metabolomics data. Nat Protoc. 2022;17:1735–61. https://doi.org/10.1038/s41596-022-00710-w .
doi: 10.1038/s41596-022-00710-w
pubmed: 35715522
Livak KJ, Schmittgen TD. Analysis of relative gene expression data using real-time quantitative PCR and the 2
doi: 10.1006/meth.2001.1262
pubmed: 11846609
Park JW, Kang HW, Ha BS, Kim SI, Kim S, Ro HS. Strain-dependent response to Cu(2+) in the expression of laccase in Pycnoporus coccineus. Arch Microbiol. 2015;197:589–96. https://doi.org/10.1007/s00203-015-1090-7 .
doi: 10.1007/s00203-015-1090-7
pubmed: 25677944
Chia AJ, Goldring CE, Kitteringham NR, Wong SQ, Morgan P, Park BK. Differential effect of covalent protein modification and glutathione depletion on the transcriptional response of Nrf2 and NF-kappaB. Biochem Pharmacol. 2010;80:410–21. https://doi.org/10.1016/j.bcp.2010.04.004 .
doi: 10.1016/j.bcp.2010.04.004
pubmed: 20416283
pmcid: 2884179
Zhang LB, Qiu TT, Qiu XG, Yang WWJ, Ye XY, Meng C. Transcriptomic and metabolomic analysis unveils a negative effect of glutathione metabolism on laccase activity in Cerrena Unicolor 87613. Microbiol Spectr. 2024;e0340523. https://doi.org/10.1128/spectrum.03405-23 .
Chen J, Ye Y, Chi Y, Hao X, Zhao Q. Transcriptomics and co-expression network analysis revealing candidate genes for the laccase activity of Trametes Gibbosa. BMC Microbiol. 2023;23:29. https://doi.org/10.1186/s12866-022-02727-3 .
doi: 10.1186/s12866-022-02727-3
pubmed: 36703110
pmcid: 9878871
Chen YH, Song F, Miao YT, He HH, Lian YY, Li XC, Li M. A novel laccase gene from Litopenaeus vannamei is involved in the immune responses to pathogen infection and oxidative stress. Dev Comp Immunol. 2020;105:103582. https://doi.org/10.1016/j.dci.2019.103582 .
doi: 10.1016/j.dci.2019.103582
pubmed: 31874194
Kaur K, Sharma A, Capalash N, Sharma P. Multicopper oxidases: biocatalysts in microbial pathogenesis and stress management. Microbiol Res. 2019;222:1–13. https://doi.org/10.1016/j.micres.2019.02.007 .
doi: 10.1016/j.micres.2019.02.007
pubmed: 30928025
Su YB, Peng B, Li H, Cheng ZX, Zhang TT, Zhu JX, Li D, Li MY, Ye JZ, Du CC, et al. Pyruvate cycle increases aminoglycoside efficacy and provides respiratory energy in bacteria. Proc Natl Acad Sci U S A. 2018;115:E1578–87. https://doi.org/10.1073/pnas.1714645115 .
doi: 10.1073/pnas.1714645115
pubmed: 29382755
pmcid: 5816162
Du X, Zhang Y, Wu H, Tan W, Huang E, Guan X, Zhang L. ROS-mediated TCA cycle is greatly related to the UV resistance of Bacillus thuringiensis. Pestic Biochem Physiol. 2023;193:105429. https://doi.org/10.1016/j.pestbp.2023.105429 .
doi: 10.1016/j.pestbp.2023.105429
pubmed: 37248007
Chen J, Chi Y, Hao X, Ma L. Metabolic regulation mechanism of Trametes Gibbosa CB1 on lignin. Int J Biol Macromol. 2023;240:124189. https://doi.org/10.1016/j.ijbiomac.2023.124189 .
doi: 10.1016/j.ijbiomac.2023.124189
pubmed: 36990410
Martinez-Moya P, Niehaus K, Alcaino J, Baeza M, Cifuentes V. Proteomic and metabolomic analysis of the carotenogenic yeast Xanthophyllomyces dendrorhous using different carbon sources. BMC Genomics. 2015;16:289. https://doi.org/10.1186/s12864-015-1484-6 .
doi: 10.1186/s12864-015-1484-6
pubmed: 25887121
pmcid: 4404605
Liu J, Peng C, Han Q, Wang M, Zhou G, Ye B, Xiao Y, Fang Z, Kues U. Coprinopsis Cinerea uses laccase Lcc9 as a defense strategy to eliminate oxidative stress during fungal-fungal interactions. Appl Environ Microbiol. 2022;88:e0176021. https://doi.org/10.1128/AEM.01760-21 .
doi: 10.1128/AEM.01760-21
pubmed: 34669425
Zhang Q, Zhao L, Li Y, Wang F, Li S, Shi G, Ding Z. Comparative transcriptomics and transcriptional regulation analysis of enhanced laccase production induced by co-culture of Pleurotus Eryngii var. Ferulae with Rhodotorula mucilaginosa. Appl Microbiol Biotechnol. 2020;104:241–55. https://doi.org/10.1007/s00253-019-10228-z .
doi: 10.1007/s00253-019-10228-z
pubmed: 31735984
Gan Z, Zhang X, Li M, Li X, Zhang X, Wang C, Xiao Y, Liu J, Fang Z. Seryl-tRNA synthetase shows a noncanonical activity of upregulating laccase transcription in Trametes Hirsuta AH28-2 exposed to copper ion. Microbiol Spectr. 2023;11:e0076823. https://doi.org/10.1128/spectrum.00768-23 .
doi: 10.1128/spectrum.00768-23
pubmed: 37395668
Cooper AJ. Biochemistry of sulfur-containing amino acids. Annu Rev Biochem. 1983;52:187–222. https://doi.org/10.1146/annurev.bi.52.070183.001155 .
doi: 10.1146/annurev.bi.52.070183.001155
pubmed: 6351723
Musatti A, Manzoni M, Rollini M. Post-fermentative production of glutathione by baker’s yeast (S. Cerevisiae) in compressed and dried forms. N Biotechnol. 2013;30:219–26. https://doi.org/10.1016/j.nbt.2012.05.024 .
doi: 10.1016/j.nbt.2012.05.024
pubmed: 22705095
Fan F, Zhuo R, Sun S, Wan X, Jiang M, Zhang X, Yang Y. Cloning and functional analysis of a new laccase gene from Trametes sp. 48424 which had the high yield of laccase and strong ability for decolorizing different dyes. Bioresour Technol. 2011;102:3126–37. https://doi.org/10.1016/j.biortech.2010.10.079 .
doi: 10.1016/j.biortech.2010.10.079
pubmed: 21094600
Hoshida H, Nakao M, Kanazawa H, Kubo K, Hakukawa T, Morimasa K, Akada R, Nishizawa Y. Isolation of five laccase gene sequences from the white-rot fungus trametes sanguinea by PCR, and cloning, characterization and expression of the laccase cDNA in yeasts. J Biosci Bioeng. 2001;92:372–80. https://doi.org/10.1263/jbb.92.372 .
doi: 10.1263/jbb.92.372
pubmed: 16233113
Levin L, Melignani E, Ramos AM. Effect of nitrogen sources and vitamins on ligninolytic enzyme production by some white-rot fungi. Dye decolorization by selected culture filtrates. Bioresour Technol. 2010;101:4554–63. https://doi.org/10.1016/j.biortech.2010.01.102 .
doi: 10.1016/j.biortech.2010.01.102
pubmed: 20153961
Liu T, Sun L, Zhang Y, Wang Y, Zheng J. Imbalanced GSH/ROS and sequential cell death. J Biochem Mol Toxicol. 2022;36:e22942. https://doi.org/10.1002/jbt.22942 .
doi: 10.1002/jbt.22942
pubmed: 34725879
Averill-Bates DA. The antioxidant glutathione. Vitam Horm. 2023;121:109–41. https://doi.org/10.1016/bs.vh.2022.09.002 .
doi: 10.1016/bs.vh.2022.09.002
pubmed: 36707132
Flohe L. The fairytale of the GSSG/GSH redox potential. Biochim Biophys Acta. 2013;1830:3139–42. https://doi.org/10.1016/j.bbagen.2012.10.020 .
doi: 10.1016/j.bbagen.2012.10.020
pubmed: 23127894
Forman HJ, Zhang H, Rinna A. Glutathione: overview of its protective roles, measurement, and biosynthesis. Mol Aspects Med. 2009;30:1–12. https://doi.org/10.1016/j.mam.2008.08.006 .
doi: 10.1016/j.mam.2008.08.006
pubmed: 18796312
Yao Y, Zhou G, Lin Y, Xu X, Yang J. A highly thermotolerant laccase produced by Cerrena unicolor strain CGMCC 5.1011 for complete and stable malachite green decolorization. AMB Express. 2020;10:178. https://doi.org/10.1186/s13568-020-01118-z .
doi: 10.1186/s13568-020-01118-z
pubmed: 33006679
pmcid: 7532254