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Upscale and characterization of lignin-modifying enzymes from Marasmiellus palmivorus VE111 in a bioreactor under parameter optimization and the effect of inducers.

Identifieur interne : 000194 ( Main/Exploration ); précédent : 000193; suivant : 000195

Upscale and characterization of lignin-modifying enzymes from Marasmiellus palmivorus VE111 in a bioreactor under parameter optimization and the effect of inducers.

Auteurs : William Daniel Hahn Schneider [Brésil] ; Paula Cavion Costa [Brésil] ; Roselei Claudete Fontana [Brésil] ; Félix Gonçalves De Siqueira [Brésil] ; Aldo José Pinheiro Dillon [Brésil] ; Marli Camassola [Brésil]

Source :

RBID : pubmed:30858107

Descripteurs français

English descriptors

Abstract

Testing different pHs, dissolved oxygen concentrations and temperatures, plus the addition of inducers, to optimize ligninolytic enzyme activity, resulted in increased production of laccases, total peroxidases and manganese peroxidases on the order of 2.1-fold, 4.6-fold and 10-fold, respectively; laccases reached 6588 U/mL, total peroxidases reached 3533 U/mL and manganese peroxidase achieved 60 U/mL. Furthermore, an increase in laccase volumetric productivity and in its specific activity was verified. The addition of inducers, such as copper sulphate and manganese sulphate, improved enzymatic activity. In addition, a new previously unidentified laccase isoform was documented by zymography. The present work successfully increased the production of ligninolytic enzymes.

DOI: 10.1016/j.jbiotec.2019.03.002
PubMed: 30858107


Affiliations:


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Le document en format XML

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<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Laccase (chemistry)</term>
<term>Laccase (metabolism)</term>
<term>Lignin (chemistry)</term>
<term>Lignin (metabolism)</term>
<term>Magnesium Sulfate (metabolism)</term>
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<term>Concentration en ions d'hydrogène (MeSH)</term>
<term>Laccase (composition chimique)</term>
<term>Laccase (métabolisme)</term>
<term>Lignine (composition chimique)</term>
<term>Lignine (métabolisme)</term>
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<term>Protéines fongiques (composition chimique)</term>
<term>Protéines fongiques (métabolisme)</term>
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<term>Sulfate de cuivre (métabolisme)</term>
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<div type="abstract" xml:lang="en">Testing different pHs, dissolved oxygen concentrations and temperatures, plus the addition of inducers, to optimize ligninolytic enzyme activity, resulted in increased production of laccases, total peroxidases and manganese peroxidases on the order of 2.1-fold, 4.6-fold and 10-fold, respectively; laccases reached 6588 U/mL, total peroxidases reached 3533 U/mL and manganese peroxidase achieved 60 U/mL. Furthermore, an increase in laccase volumetric productivity and in its specific activity was verified. The addition of inducers, such as copper sulphate and manganese sulphate, improved enzymatic activity. In addition, a new previously unidentified laccase isoform was documented by zymography. The present work successfully increased the production of ligninolytic enzymes.</div>
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<name sortKey="Schneider, William Daniel Hahn" sort="Schneider, William Daniel Hahn" uniqKey="Schneider W" first="William Daniel Hahn" last="Schneider">William Daniel Hahn Schneider</name>
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<name sortKey="De Siqueira, Felix Goncalves" sort="De Siqueira, Felix Goncalves" uniqKey="De Siqueira F" first="Félix Gonçalves" last="De Siqueira">Félix Gonçalves De Siqueira</name>
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<name sortKey="Pinheiro Dillon, Aldo Jose" sort="Pinheiro Dillon, Aldo Jose" uniqKey="Pinheiro Dillon A" first="Aldo José" last="Pinheiro Dillon">Aldo José Pinheiro Dillon</name>
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