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

• 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.