Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.
Identifieur interne : 002004 ( Main/Exploration ); précédent : 002003; suivant : 002005Reactivity and stability of mycelium-bound carboxylesterase from Aspergillus oryzae.
Auteurs : Attilio Converti [Italie] ; Adriana Del Borghi ; Raffaella Gandolfi ; Alessandra Lodi ; Francesco Molinari ; Emilio PalazziSource :
- Biotechnology and bioengineering [ 0006-3592 ] ; 2002.
English descriptors
- KwdEn :
- 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:
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Le document en format XML
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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></author><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></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="2002">2002</date><idno type="RBID">pubmed:11753931</idno><idno type="pmid">11753931</idno><idno type="wicri:Area/PubMed/Corpus">000629</idno><idno type="wicri:Area/PubMed/Curation">000629</idno><idno type="wicri:Area/PubMed/Checkpoint">000572</idno><idno type="wicri:Area/Ncbi/Merge">000091</idno><idno type="wicri:Area/Ncbi/Curation">000091</idno><idno type="wicri:Area/Ncbi/Checkpoint">000091</idno><idno type="wicri:doubleKey">0006-3592:2002:Converti A:reactivity:and:stability</idno><idno type="wicri:Area/Main/Merge">002079</idno><idno type="wicri:Area/Main/Curation">002004</idno><idno type="wicri:Area/Main/Exploration">002004</idno></publicationStmt><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><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></author><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></author></analytic><series><title level="j">Biotechnology and bioengineering</title><idno type="ISSN">0006-3592</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><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></keywords><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></keywords></textClass></profileDesc></teiHeader><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><affiliations><list><country><li>Italie</li></country></list><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></noCountry><country name="Italie"><noRegion><name sortKey="Converti, Attilio" sort="Converti, Attilio" uniqKey="Converti A" first="Attilio" last="Converti">Attilio Converti</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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