Biotransformations are becoming a more and more important method for generation of optically pure compounds and optically active polymers. Among various methods, using lipase on biocatalysis is becoming more active (Decagny et al., 1998). The industrial versatility and unique catalytic performance of Upases make Lipase-catalyzed process become more and more commercially feasible alternatives to bulk chemical routes. Ecological concerns have also favored more extensive applications of lipases, which are involved in resolution of racemate, stereo-, enantio- and regiospecific transformation, synthesis of peptides, and so on (Kosei, et al., 2001). Wax esters, long-chain esters derived from fatty acids and alcohol both with chain lengths of 12 carbons or more, have potential applications as lubricants, plasticizers, and cosmetics. Synthesis of wax esters by lipases has been investigated by a few workers. However, there were few examples in previous literatures concerning the esterification of linoleic acid and oleyl alcohol to form oleyl linoleate, which has higher unsaturation degree and fluidity than oleate. Oleyl linoleate, due to its unque prperties, will be of great commercial value and application in cosmetics and lubricants. Studies of kinetics of esterification catalyzed by immobilized lipases were relatively few and have only been actively investigated recently. In the present study, effects of carbon chain length and unsaturation degree of fatty acids on esterfication catalyzed by gelatin-immobilized Trichosporon cephaloid lipase were studied. Effects of various factors on esterifiction of linoleic acid and oleyl alcohol and kinetics of the reaction were both discussed.
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