Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
49741 | Catalysis Communications | 2014 | 4 Pages |
•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.