Abstract

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.

Full Text
Paper version not known

Talk to us

Join us for a 30 min session where you can share your feedback and ask us any queries you have

Schedule a call

Disclaimer: All third-party content on this website/platform is and will remain the property of their respective owners and is provided on "as is" basis without any warranties, express or implied. Use of third-party content does not indicate any affiliation, sponsorship with or endorsement by them. Any references to third-party content is to identify the corresponding services and shall be considered fair use under The CopyrightLaw.