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Synthesis of ethyl phenylacetate by lyophilized mycelium of Aspergillus oryzae.

Identifieur interne : 001A00 ( Main/Exploration ); précédent : 001999; suivant : 001A01

Synthesis of ethyl phenylacetate by lyophilized mycelium of Aspergillus oryzae.

Auteurs : A. Converti [Italie] ; R. Gandolfi ; M. Zilli ; F. Molinari ; L. Binaghi ; P. Perego ; M. Del Borghi

Source :

Applied microbiology and biotechnology [ 0175-7598 ] ; 2005.

RBID : pubmed:15650849

English descriptors

KwdEn :
- Acylation, Aspergillus oryzae (metabolism), Biotransformation, Carboxylesterase (metabolism), Catalysis, Ethanol (metabolism), Freeze Drying, Kinetics, Mycelium (metabolism), Phenylacetates (metabolism), Rhizopus (metabolism), Temperature, Thermodynamics.
MESH :
- chemical , metabolism : Carboxylesterase, Ethanol, Phenylacetates.
- metabolism : Aspergillus oryzae, Mycelium, Rhizopus.
- Acylation, Biotransformation, Catalysis, Freeze Drying, Kinetics, Temperature, Thermodynamics.

Abstract

Lyophilized mycelia of Aspergillus oryzae CBS 102.07, Aspergillus oryzae MIM, Rhizopus oryzae CBS 112.07, Rhizopus oryzae CBS 391.34, Rhizopus oryzae CBS 260.28 and Rhizopus oryzae CBS 328.47 were tested in this study to select the best biocatalysts for ethanol acylation with phenylacetic acid. The mycelium-bound carboxylesterase activity of A. oryzae MIM, which exhibited the best performances, was initially investigated at 50 degrees C, either in 0.1 M phosphate buffer or in n-heptane to catalyse the hydrolysis or the synthesis, respectively, of ethyl phenylacetate. The results in terms of product and substrate concentrations versus time were used to estimate the maximum molar conversions at equilibrium, the equilibrium constants, and the times needed to reach half maximum conversions, thus providing sufficient information about this biotransformation. The values of the apparent equilibrium constants, estimated at 20 degrees C
DOI: 10.1007/s00253-004-1830-0
PubMed: 15650849

Affiliations:

Italie

Le document en format XML

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<author><name sortKey="Molinari, F" sort="Molinari, F" uniqKey="Molinari F" first="F" last="Molinari">F. Molinari</name>
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<author><name sortKey="Binaghi, L" sort="Binaghi, L" uniqKey="Binaghi L" first="L" last="Binaghi">L. Binaghi</name>
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<series><title level="j">Applied microbiology and biotechnology</title>
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<term>Aspergillus oryzae (metabolism)</term>
<term>Biotransformation</term>
<term>Carboxylesterase (metabolism)</term>
<term>Catalysis</term>
<term>Ethanol (metabolism)</term>
<term>Freeze Drying</term>
<term>Kinetics</term>
<term>Mycelium (metabolism)</term>
<term>Phenylacetates (metabolism)</term>
<term>Rhizopus (metabolism)</term>
<term>Temperature</term>
<term>Thermodynamics</term>
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<front><div type="abstract" xml:lang="en">Lyophilized mycelia of Aspergillus oryzae CBS 102.07, Aspergillus oryzae MIM, Rhizopus oryzae CBS 112.07, Rhizopus oryzae CBS 391.34, Rhizopus oryzae CBS 260.28 and Rhizopus oryzae CBS 328.47 were tested in this study to select the best biocatalysts for ethanol acylation with phenylacetic acid. The mycelium-bound carboxylesterase activity of A. oryzae MIM, which exhibited the best performances, was initially investigated at 50 degrees C, either in 0.1 M phosphate buffer or in n-heptane to catalyse the hydrolysis or the synthesis, respectively, of ethyl phenylacetate. The results in terms of product and substrate concentrations versus time were used to estimate the maximum molar conversions at equilibrium, the equilibrium constants, and the times needed to reach half maximum conversions, thus providing sufficient information about this biotransformation. The values of the apparent equilibrium constants, estimated at 20 degrees C</div>
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<name sortKey="Gandolfi, R" sort="Gandolfi, R" uniqKey="Gandolfi R" first="R" last="Gandolfi">R. Gandolfi</name>
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Synthesis of ethyl phenylacetate by lyophilized mycelium of Aspergillus oryzae.

Synthesis of ethyl phenylacetate by lyophilized mycelium of Aspergillus oryzae.

Source :

English descriptors

Abstract

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Le document en format XML

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