Interesterification and hydrolysis catalyzed by fatty acid-modified lipases

Abstract

Interesterification and hydrolysis catalyzed by fatty acid-modified lipasesNative lipases often exhibit poor interesterification activity. We previously developed a fatty acid modification method to improve the activity of lipases. In this study, we applied this fatty acid modification method to several lipases and evaluated their interesterification and hydrolytic activities. The resulting interesterification activity was strongly dependent on the modifying fatty acid used. Of the saturated fatty acids tested, stearic acid modification substantially improved the interesterification activity of three lipases. Hydrolytic activity was affected slightly by the modifying fatty acid used. Substrate specificity of the modified lipase with triglycerides was also investigated and it was found that fatty acid modification changed the substrate specificity of some lipases.

Lipase-catalyzed harvesting and/or enrichment of industrially and nutritionally important fatty acids

“…However with C. antarctica, immobilization tended to broaden the selectivity so that C6-C10 had about the same reactivity. Lipases from porcine pancreas, Rhizopus japonicus, and Chromobacterium viscosum were modified with stearic acid, and TAG hydrolyses and acidolysis reactions were conducted in media containing hexane (Entry 8; Maruyama et al, 2002). Medium chain TAG were preferred as substrates, and in acidolysis reactions with oleic acid, medium chain TAG were preferred.…”