Chang_2001_J.Agric.Food.Chem_49_2619

Various flavor esters were obtained by using recombinant lipases from Staphylococcus epidermidis as a catalyst in an aqueous environment. These esters were enzymatically synthesized to overcome the problems associated with chemical processes. This study showed that the S. epidermidis lipases could catalyze ester synthesis from decyl alcohol and fatty acids of different chain length. The wild-type and mutant lipases (M419A and V649I) could efficiently catalyze the synthesis of decyl alcohol esters of unsaturated fatty acids. In contrast, the yield of decyl laurate was better by wild-type and mutant enzyme V6491, but mutant enzyme M419A only favored the synthesis of decyl myristate. The esterification of oleic acid and various carbon-chain-length alcohols from ethanol to hexadecanol increased up to decanol by wild-type and M419A mutant enzymes and reached an optimum for dodecanol by V6491 mutant enzyme. The enzyme is potentially useful in food industries such as dairy product flavoring.