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

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.