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Biocatalytic synthesis of short-chain flavor esters with high substrate loading by a whole-cell lipase from Aspergillus oryzae

Paper ID Volume ID Publish Year Pages File Format Full-Text
49741 46764 2014 4 PDF Available
Title
Biocatalytic synthesis of short-chain flavor esters with high substrate loading by a whole-cell lipase from Aspergillus oryzae
Abstract

•First report on the synthesis of various short-chain flavor esters by AOL.•AOL displayed a strong tolerance for high substrate concentration.•AOL exhibited high esterification activities toward a series of acids and alcohols.

A lipase from Aspergillus oryzae WZ007 exhibited high esterification activities toward a series of short-chain acids and alcohols. Moreover, it displayed a strong tolerance for high substrate concentration of up to 2.0 M and presented a highest initial rate of 276 mmol·L− 1·h− 1 at this concentration. After a reaction time of 48 h, the conversion rates of acids were higher than 80% for the synthesis of a majority of heptanoic acid esters, some octanoic acid esters and n-propyl hexanoate. These results implied that A. oryzae WZ007 lipase was a promising biocatalyst in the production of flavor esters.

Keywords
Biocatalytic synthesis; Short-chain flavor esters; High substrate loading; Lipase; Aspergillus oryzae
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Biocatalytic synthesis of short-chain flavor esters with high substrate loading by a whole-cell lipase from Aspergillus oryzae
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Publisher
Database: Elsevier - ScienceDirect
Journal: Catalysis Communications - Volume 45, 5 February 2014, Pages 59–62
Authors
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Subjects
Physical Sciences and Engineering Chemical Engineering Catalysis
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