An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.
Identifieur interne : 000314 ( Main/Corpus ); précédent : 000313; suivant : 000315An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.
Auteurs : Diana Linke ; Nicole Lehnert ; Manfred Nimtz ; Ralf G. BergerSource :
- Enzyme and microbial technology [ 1879-0909 ]
English descriptors
- KwdEn :
- Alcohol Oxidoreductases (chemistry), Alcohol Oxidoreductases (genetics), Alcohol Oxidoreductases (metabolism), Amino Acid Sequence (MeSH), Base Sequence (MeSH), DNA, Fungal (genetics), Fungal Proteins (chemistry), Fungal Proteins (genetics), Fungal Proteins (metabolism), Hydrogen-Ion Concentration (MeSH), Molecular Sequence Data (MeSH), Phanerochaete (enzymology), Phanerochaete (genetics), Sequence Homology, Amino Acid (MeSH), Substrate Specificity (MeSH), Sugar Alcohol Dehydrogenases (chemistry), Sugar Alcohol Dehydrogenases (genetics), Sugar Alcohol Dehydrogenases (metabolism).
- MESH :
- chemical , chemistry : Alcohol Oxidoreductases, Fungal Proteins, Sugar Alcohol Dehydrogenases.
- chemical , genetics : Alcohol Oxidoreductases, DNA, Fungal, Fungal Proteins, Sugar Alcohol Dehydrogenases.
- chemical , metabolism : Alcohol Oxidoreductases, Fungal Proteins, Sugar Alcohol Dehydrogenases.
- enzymology : Phanerochaete.
- genetics : Phanerochaete.
- Amino Acid Sequence, Base Sequence, Hydrogen-Ion Concentration, Molecular Sequence Data, Sequence Homology, Amino Acid, Substrate Specificity.
Abstract
An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide.
DOI: 10.1016/j.enzmictec.2014.04.001
PubMed: 24910330
Links to Exploration step
pubmed:24910330Le document en format XML
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<author><name sortKey="Linke, Diana" sort="Linke, Diana" uniqKey="Linke D" first="Diana" last="Linke">Diana Linke</name>
<affiliation><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany. Electronic address: Diana.linke@lci.uni-hannover.de.</nlm:affiliation>
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<author><name sortKey="Lehnert, Nicole" sort="Lehnert, Nicole" uniqKey="Lehnert N" first="Nicole" last="Lehnert">Nicole Lehnert</name>
<affiliation><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</nlm:affiliation>
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<author><name sortKey="Nimtz, Manfred" sort="Nimtz, Manfred" uniqKey="Nimtz M" first="Manfred" last="Nimtz">Manfred Nimtz</name>
<affiliation><nlm:affiliation>Helmholtz Zentrum für Infektionsforschung, Inhoffenstrasse 7, D-38124 Braunschweig, Germany.</nlm:affiliation>
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<author><name sortKey="Berger, Ralf G" sort="Berger, Ralf G" uniqKey="Berger R" first="Ralf G" last="Berger">Ralf G. Berger</name>
<affiliation><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</nlm:affiliation>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.</title>
<author><name sortKey="Linke, Diana" sort="Linke, Diana" uniqKey="Linke D" first="Diana" last="Linke">Diana Linke</name>
<affiliation><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany. Electronic address: Diana.linke@lci.uni-hannover.de.</nlm:affiliation>
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<author><name sortKey="Lehnert, Nicole" sort="Lehnert, Nicole" uniqKey="Lehnert N" first="Nicole" last="Lehnert">Nicole Lehnert</name>
<affiliation><nlm:affiliation>Institut für Lebensmittelchemie, Leibniz Universität Hannover, Callinstraße 5, D-30167, Hannover, Germany.</nlm:affiliation>
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<author><name sortKey="Nimtz, Manfred" sort="Nimtz, Manfred" uniqKey="Nimtz M" first="Manfred" last="Nimtz">Manfred Nimtz</name>
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<author><name sortKey="Berger, Ralf G" sort="Berger, Ralf G" uniqKey="Berger R" first="Ralf G" last="Berger">Ralf G. Berger</name>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alcohol Oxidoreductases (chemistry)</term>
<term>Alcohol Oxidoreductases (genetics)</term>
<term>Alcohol Oxidoreductases (metabolism)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Base Sequence (MeSH)</term>
<term>DNA, Fungal (genetics)</term>
<term>Fungal Proteins (chemistry)</term>
<term>Fungal Proteins (genetics)</term>
<term>Fungal Proteins (metabolism)</term>
<term>Hydrogen-Ion Concentration (MeSH)</term>
<term>Molecular Sequence Data (MeSH)</term>
<term>Phanerochaete (enzymology)</term>
<term>Phanerochaete (genetics)</term>
<term>Sequence Homology, Amino Acid (MeSH)</term>
<term>Substrate Specificity (MeSH)</term>
<term>Sugar Alcohol Dehydrogenases (chemistry)</term>
<term>Sugar Alcohol Dehydrogenases (genetics)</term>
<term>Sugar Alcohol Dehydrogenases (metabolism)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Alcohol Oxidoreductases</term>
<term>Fungal Proteins</term>
<term>Sugar Alcohol Dehydrogenases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Alcohol Oxidoreductases</term>
<term>DNA, Fungal</term>
<term>Fungal Proteins</term>
<term>Sugar Alcohol Dehydrogenases</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alcohol Oxidoreductases</term>
<term>Fungal Proteins</term>
<term>Sugar Alcohol Dehydrogenases</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Phanerochaete</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Phanerochaete</term>
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<keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term>
<term>Base Sequence</term>
<term>Hydrogen-Ion Concentration</term>
<term>Molecular Sequence Data</term>
<term>Sequence Homology, Amino Acid</term>
<term>Substrate Specificity</term>
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<front><div type="abstract" xml:lang="en">An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide. </div>
</front>
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<DateCompleted><Year>2015</Year>
<Month>05</Month>
<Day>11</Day>
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<DateRevised><Year>2014</Year>
<Month>06</Month>
<Day>09</Day>
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<Title>Enzyme and microbial technology</Title>
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<ArticleTitle>An alcohol oxidase of Phanerochaete chrysosporium with a distinct glycerol oxidase activity.</ArticleTitle>
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<Abstract><AbstractText>An intracellular alcohol oxidase (AOX) was isolated from the white-rot basidiomycete Phanerochaete chrysosporium (Pch), grown on l-lactate induction medium, and purified to electrophoretic homogeneity. The dimeric protein consisted of two identical 75kDa subunits. The open reading frame of 1,956bp resulted in a monomer consisting of 651 amino acids. The enzyme showed a pI at 5.4, a pH optimum of 9, a temperature optimum at 50°C, possessed putative conserved domains of the GMC superfamily, a FAD binding domain, and showed up to 86% homology to alcohol oxidase sequences of Gloeophyllum trabeum and Coprinopsis cinerea. As was shown for the first time for an AOX from a basidiomycete, not only methanol, but also lower primary alcohols and glycerol were accepted as substrates. An assay based on aldehyde dehydrogenase confirmed d-glyceraldehyde as the product of the reaction. A bioprocess based on this enzyme could alleviate the problems associated with the huge side-stream of glycerol occurring during the manufacture of biodiesel, yielding the green oxidant hydrogen peroxide. </AbstractText>
<CopyrightInformation>Copyright © 2014 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Linke</LastName>
<ForeName>Diana</ForeName>
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<Author ValidYN="Y"><LastName>Berger</LastName>
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<Language>eng</Language>
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<KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="N">Alcohol oxidase</Keyword>
<Keyword MajorTopicYN="N">Glycerol</Keyword>
<Keyword MajorTopicYN="N">Phanerochaete chrysosporium</Keyword>
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