PhanerochaeteV1, Main, Corpus, bibRecord, 000E36

Immobilization as a tool for the stabilization of lignin peroxidase produced by Phanerochaete chrysosporium INA-12.

Identifieur interne : 000E36 ( Main/Corpus ); précédent : 000E35; suivant : 000E37

Immobilization as a tool for the stabilization of lignin peroxidase produced by Phanerochaete chrysosporium INA-12.

Auteurs : M. Asther ; J C Meunier

Source :

Applied biochemistry and biotechnology [ 0273-2289 ]

RBID : pubmed:8346905

English descriptors

KwdEn :
- Basidiomycota (enzymology), Cyanogen Bromide (MeSH), Enzyme Stability (MeSH), Enzymes, Immobilized (MeSH), Hot Temperature (MeSH), Hydrogen-Ion Concentration (MeSH), Kinetics (MeSH), Peroxidases (chemistry), Sepharose (analogs & derivatives), Solvents (MeSH).
MESH :
- chemical , analogs & derivatives : Sepharose.
- chemical , chemistry : Peroxidases.
- chemical : Cyanogen Bromide, Enzymes, Immobilized, Solvents.
- enzymology : Basidiomycota.
- Enzyme Stability, Hot Temperature, Hydrogen-Ion Concentration, Kinetics.

Abstract

Lignin peroxidase immobilization was achieved by covalent coupling on CNBr-Sepharose 4B. Protein immobilization yield was around 80%. For veratryl alcohol oxidation, in the presence of hydrogen peroxide, both soluble and bound enzymes exhibited the same pH profile with an optimum near 2.5. Catalytic parameters (kc and Km) were seriously affected by immobilization. On the other hand, immobilization provided a noticeable stabilization of the enzyme against acidic pH and high temperatures. A 15-20 increase in the half-inactivation times at pH 2.2 and 2.7, respectively, could be observed. Bound enzyme was also much more thermostable than soluble.

DOI: 10.1007/BF02916412
PubMed: 8346905

Links to Exploration step

pubmed:8346905

Le document en format XML

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<author><name sortKey="Asther, M" sort="Asther, M" uniqKey="Asther M" first="M" last="Asther">M. Asther</name>
<affiliation><nlm:affiliation>Laboratoire de Chimie Biologique, I.N.R.A.-C.B.A.I., Institut National Agronomique, Centre de Grignon, Thiverval-Grignon, France.</nlm:affiliation>
</affiliation>
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<author><name sortKey="Meunier, J C" sort="Meunier, J C" uniqKey="Meunier J" first="J C" last="Meunier">J C Meunier</name>
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<affiliation><nlm:affiliation>Laboratoire de Chimie Biologique, I.N.R.A.-C.B.A.I., Institut National Agronomique, Centre de Grignon, Thiverval-Grignon, France.</nlm:affiliation>
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<author><name sortKey="Meunier, J C" sort="Meunier, J C" uniqKey="Meunier J" first="J C" last="Meunier">J C Meunier</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Basidiomycota (enzymology)</term>
<term>Cyanogen Bromide (MeSH)</term>
<term>Enzyme Stability (MeSH)</term>
<term>Enzymes, Immobilized (MeSH)</term>
<term>Hot Temperature (MeSH)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Kinetics (MeSH)</term>
<term>Peroxidases (chemistry)</term>
<term>Sepharose (analogs & derivatives)</term>
<term>Solvents (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Sepharose</term>
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<front><div type="abstract" xml:lang="en">Lignin peroxidase immobilization was achieved by covalent coupling on CNBr-Sepharose 4B. Protein immobilization yield was around 80%. For veratryl alcohol oxidation, in the presence of hydrogen peroxide, both soluble and bound enzymes exhibited the same pH profile with an optimum near 2.5. Catalytic parameters (kc and Km) were seriously affected by immobilization. On the other hand, immobilization provided a noticeable stabilization of the enzyme against acidic pH and high temperatures. A 15-20 increase in the half-inactivation times at pH 2.2 and 2.7, respectively, could be observed. Bound enzyme was also much more thermostable than soluble.</div>
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<DateRevised><Year>2019</Year>
<Month>09</Month>
<Day>09</Day>
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<JournalIssue CitedMedium="Print"><Volume>38</Volume>
<Issue>1-2</Issue>
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<Title>Applied biochemistry and biotechnology</Title>
<ISOAbbreviation>Appl Biochem Biotechnol</ISOAbbreviation>
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<ArticleTitle>Immobilization as a tool for the stabilization of lignin peroxidase produced by Phanerochaete chrysosporium INA-12.</ArticleTitle>
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<Abstract><AbstractText>Lignin peroxidase immobilization was achieved by covalent coupling on CNBr-Sepharose 4B. Protein immobilization yield was around 80%. For veratryl alcohol oxidation, in the presence of hydrogen peroxide, both soluble and bound enzymes exhibited the same pH profile with an optimum near 2.5. Catalytic parameters (kc and Km) were seriously affected by immobilization. On the other hand, immobilization provided a noticeable stabilization of the enzyme against acidic pH and high temperatures. A 15-20 increase in the half-inactivation times at pH 2.2 and 2.7, respectively, could be observed. Bound enzyme was also much more thermostable than soluble.</AbstractText>
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Immobilization as a tool for the stabilization of lignin peroxidase produced by Phanerochaete chrysosporium INA-12.

Immobilization as a tool for the stabilization of lignin peroxidase produced by Phanerochaete chrysosporium INA-12.

Source :

English descriptors

Abstract

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