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Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.

Identifieur interne : 000572 ( PubMed/Checkpoint ); précédent : 000571; suivant : 000573

Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.

Auteurs : Attilio Converti [Italie] ; Adriana Del Borghi ; Raffaella Gandolfi ; Alessandra Lodi ; Francesco Molinari ; Emilio Palazzi

Source :

Biotechnology and bioengineering [ 0006-3592 ] ; 2002.

RBID : pubmed:11753931

English descriptors

KwdEn :
- Aspergillus oryzae (enzymology), Carboxylesterase, Carboxylic Ester Hydrolases (metabolism), Catalysis, Enzyme Stability, Esterification, Kinetics, Mycelium (enzymology).
MESH :
- chemical , metabolism : Carboxylic Ester Hydrolases.
- chemical : Carboxylesterase.
- enzymology : Aspergillus oryzae, Mycelium.
- Catalysis, Enzyme Stability, Esterification, Kinetics.

Abstract

The reactivity and thermostability of a novel mycelium-bound carboxylesterase from lyophilized cells of Aspergillus oryzae are explored in organic solvent. Ethanol acetylation was selected as reference esterification reaction. High carboxylesterase activity cells were used as biocatalyst in batch esterification tests at 12.5 < S(o) < 125 mmol L(-1), 5.0 < X(o) < 30 g L(-1), 0.49 < log P < 4.5 and 30 < T < 80 degrees C, as well as in residual activity tests after incubation at 40 < T < 90 degrees C. The starting rates of product formation were used to estimate with the Arrhenius model the apparent activation enthalpies of the enzymatic reaction (29-33 kJ mol(-1)), the reversible unfolding (56-63 kJ mol(-1)), and the irreversible denaturation (22 kJ mol(-1)) of the biocatalyst.

PubMed: 11753931

Affiliations:

Italie

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Le document en format XML

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<author><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemical and Process Engineering G.B. Bonino, University of Genoa, via Opera Pia 15, I-16145 Genoa, Italy. converti@unige.it</nlm:affiliation>
<country xml:lang="fr">Italie</country>
<wicri:regionArea>Department of Chemical and Process Engineering G.B. Bonino, University of Genoa, via Opera Pia 15, I-16145 Genoa</wicri:regionArea>
<wicri:noRegion>I-16145 Genoa</wicri:noRegion>
</affiliation>
</author>
<author><name sortKey="Del Borghi, Adriana" sort="Del Borghi, Adriana" uniqKey="Del Borghi A" first="Adriana" last="Del Borghi">Adriana Del Borghi</name>
</author>
<author><name sortKey="Gandolfi, Raffaella" sort="Gandolfi, Raffaella" uniqKey="Gandolfi R" first="Raffaella" last="Gandolfi">Raffaella Gandolfi</name>
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<author><name sortKey="Lodi, Alessandra" sort="Lodi, Alessandra" uniqKey="Lodi A" first="Alessandra" last="Lodi">Alessandra Lodi</name>
</author>
<author><name sortKey="Molinari, Francesco" sort="Molinari, Francesco" uniqKey="Molinari F" first="Francesco" last="Molinari">Francesco Molinari</name>
</author>
<author><name sortKey="Palazzi, Emilio" sort="Palazzi, Emilio" uniqKey="Palazzi E" first="Emilio" last="Palazzi">Emilio Palazzi</name>
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<sourceDesc><biblStruct><analytic><title xml:lang="en">Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.</title>
<author><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name>
<affiliation wicri:level="1"><nlm:affiliation>Department of Chemical and Process Engineering G.B. Bonino, University of Genoa, via Opera Pia 15, I-16145 Genoa, Italy. converti@unige.it</nlm:affiliation>
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<wicri:regionArea>Department of Chemical and Process Engineering G.B. Bonino, University of Genoa, via Opera Pia 15, I-16145 Genoa</wicri:regionArea>
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<author><name sortKey="Del Borghi, Adriana" sort="Del Borghi, Adriana" uniqKey="Del Borghi A" first="Adriana" last="Del Borghi">Adriana Del Borghi</name>
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<author><name sortKey="Gandolfi, Raffaella" sort="Gandolfi, Raffaella" uniqKey="Gandolfi R" first="Raffaella" last="Gandolfi">Raffaella Gandolfi</name>
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<author><name sortKey="Lodi, Alessandra" sort="Lodi, Alessandra" uniqKey="Lodi A" first="Alessandra" last="Lodi">Alessandra Lodi</name>
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<author><name sortKey="Molinari, Francesco" sort="Molinari, Francesco" uniqKey="Molinari F" first="Francesco" last="Molinari">Francesco Molinari</name>
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<author><name sortKey="Palazzi, Emilio" sort="Palazzi, Emilio" uniqKey="Palazzi E" first="Emilio" last="Palazzi">Emilio Palazzi</name>
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<series><title level="j">Biotechnology and bioengineering</title>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aspergillus oryzae (enzymology)</term>
<term>Carboxylesterase</term>
<term>Carboxylic Ester Hydrolases (metabolism)</term>
<term>Catalysis</term>
<term>Enzyme Stability</term>
<term>Esterification</term>
<term>Kinetics</term>
<term>Mycelium (enzymology)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Carboxylic Ester Hydrolases</term>
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<keywords scheme="MESH" type="chemical" xml:lang="en"><term>Carboxylesterase</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Aspergillus oryzae</term>
<term>Mycelium</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Catalysis</term>
<term>Enzyme Stability</term>
<term>Esterification</term>
<term>Kinetics</term>
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<front><div type="abstract" xml:lang="en">The reactivity and thermostability of a novel mycelium-bound carboxylesterase from lyophilized cells of Aspergillus oryzae are explored in organic solvent. Ethanol acetylation was selected as reference esterification reaction. High carboxylesterase activity cells were used as biocatalyst in batch esterification tests at 12.5 < S(o) < 125 mmol L(-1), 5.0 < X(o) < 30 g L(-1), 0.49 < log P < 4.5 and 30 < T < 80 degrees C, as well as in residual activity tests after incubation at 40 < T < 90 degrees C. The starting rates of product formation were used to estimate with the Arrhenius model the apparent activation enthalpies of the enzymatic reaction (29-33 kJ mol(-1)), the reversible unfolding (56-63 kJ mol(-1)), and the irreversible denaturation (22 kJ mol(-1)) of the biocatalyst.</div>
</front>
</TEI>
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<DateCreated><Year>2001</Year>
<Month>12</Month>
<Day>25</Day>
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<DateCompleted><Year>2002</Year>
<Month>02</Month>
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<DateRevised><Year>2006</Year>
<Month>11</Month>
<Day>15</Day>
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<Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-3592</ISSN>
<JournalIssue CitedMedium="Print"><Volume>77</Volume>
<Issue>2</Issue>
<PubDate><Year>2002</Year>
<Month>Jan</Month>
<Day>20</Day>
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<Title>Biotechnology and bioengineering</Title>
<ISOAbbreviation>Biotechnol. Bioeng.</ISOAbbreviation>
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<ArticleTitle>Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.</ArticleTitle>
<Pagination><MedlinePgn>232-7</MedlinePgn>
</Pagination>
<Abstract><AbstractText>The reactivity and thermostability of a novel mycelium-bound carboxylesterase from lyophilized cells of Aspergillus oryzae are explored in organic solvent. Ethanol acetylation was selected as reference esterification reaction. High carboxylesterase activity cells were used as biocatalyst in batch esterification tests at 12.5 < S(o) < 125 mmol L(-1), 5.0 < X(o) < 30 g L(-1), 0.49 < log P < 4.5 and 30 < T < 80 degrees C, as well as in residual activity tests after incubation at 40 < T < 90 degrees C. The starting rates of product formation were used to estimate with the Arrhenius model the apparent activation enthalpies of the enzymatic reaction (29-33 kJ mol(-1)), the reversible unfolding (56-63 kJ mol(-1)), and the irreversible denaturation (22 kJ mol(-1)) of the biocatalyst.</AbstractText>
<CopyrightInformation>Copyright 2002 John Wiley & Sons, Inc.</CopyrightInformation>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Converti</LastName>
<ForeName>Attilio</ForeName>
<Initials>A</Initials>
<AffiliationInfo><Affiliation>Department of Chemical and Process Engineering G.B. Bonino, University of Genoa, via Opera Pia 15, I-16145 Genoa, Italy. converti@unige.it</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Del Borghi</LastName>
<ForeName>Adriana</ForeName>
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<Author ValidYN="Y"><LastName>Gandolfi</LastName>
<ForeName>Raffaella</ForeName>
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<Author ValidYN="Y"><LastName>Lodi</LastName>
<ForeName>Alessandra</ForeName>
<Initials>A</Initials>
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<Author ValidYN="Y"><LastName>Molinari</LastName>
<ForeName>Francesco</ForeName>
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<Author ValidYN="Y"><LastName>Palazzi</LastName>
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<Language>eng</Language>
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<PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType>
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<MedlineJournalInfo><Country>United States</Country>
<MedlineTA>Biotechnol Bioeng</MedlineTA>
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<Chemical><RegistryNumber>EC 3.1.1.1</RegistryNumber>
<NameOfSubstance UI="D043182">Carboxylesterase</NameOfSubstance>
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<CitationSubset>IM</CitationSubset>
<MeshHeadingList><MeshHeading><DescriptorName MajorTopicYN="N" UI="D001236">Aspergillus oryzae</DescriptorName>
<QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D043182">Carboxylesterase</DescriptorName>
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<MeshHeading><DescriptorName MajorTopicYN="N" UI="D002265">Carboxylic Ester Hydrolases</DescriptorName>
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<MeshHeading><DescriptorName MajorTopicYN="N" UI="D004795">Enzyme Stability</DescriptorName>
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<MeshHeading><DescriptorName MajorTopicYN="N" UI="D004951">Esterification</DescriptorName>
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<MeshHeading><DescriptorName MajorTopicYN="N" UI="D007700">Kinetics</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName MajorTopicYN="N" UI="D025282">Mycelium</DescriptorName>
<QualifierName MajorTopicYN="Y" UI="Q000201">enzymology</QualifierName>
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<affiliations><list><country><li>Italie</li>
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<tree><noCountry><name sortKey="Del Borghi, Adriana" sort="Del Borghi, Adriana" uniqKey="Del Borghi A" first="Adriana" last="Del Borghi">Adriana Del Borghi</name>
<name sortKey="Gandolfi, Raffaella" sort="Gandolfi, Raffaella" uniqKey="Gandolfi R" first="Raffaella" last="Gandolfi">Raffaella Gandolfi</name>
<name sortKey="Lodi, Alessandra" sort="Lodi, Alessandra" uniqKey="Lodi A" first="Alessandra" last="Lodi">Alessandra Lodi</name>
<name sortKey="Molinari, Francesco" sort="Molinari, Francesco" uniqKey="Molinari F" first="Francesco" last="Molinari">Francesco Molinari</name>
<name sortKey="Palazzi, Emilio" sort="Palazzi, Emilio" uniqKey="Palazzi E" first="Emilio" last="Palazzi">Emilio Palazzi</name>
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<country name="Italie"><noRegion><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name>
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Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.

Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.

Source :

English descriptors

Abstract

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Links to Exploration step

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Pour manipuler ce document sous Unix (Dilib)

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Pour générer des pages wiki