BioChem - DOS

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

Catalysis communications

Yan, H.D.; Zhang, Q.; Wang, Z.

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 2.0M and presented a highest initial rate of 276mmol.L<SUP>-1</SUP>.h<SUP>-1</SUP> at this concentration. After a reaction time of 48h, 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.

2014

Elsevier

1566-7367

45

pp.59-62

10.1016/j.catcom.2013.10.018

http://click.ndsl.kr/servlet/OpenAPIDetailView?keyValue=05787966&target=NART&cn=NART68281163

Biocatalytic synthesis; Short-chain flavor esters; High substrate loading; Lipase; Aspergillus oryzae