Glycerol acyl-transfer kinetics of a circular permutated Candida antarctica lipase B

摘要: Triacylglycerols containing a high abundance of unusual fatty acids, such as γ-linolenic acid, or novel arylaliphatic ferulic are useful in pharmaceutical and cosmeceutical applications. Candida antarctica lipase B (CALB) is quite often used for non-aqueous synthesis, although the wild-type enzyme can be rather slow with bulky sterically hindered acyl donor substrates. The catalytic performance circularly permutated variant CALB, cp283, various donors glycerol was examined. In comparison to butyl oleate ethyl γ-linolenate glycerolysis rates were 2.2- 4.0-fold greater, respectively. Cp283 showed substrate inhibition by glycerol, which not case version. With either ferulate vinyl donors, cp283 matched CALB. Changes active site accessibility resulting from circular permutation led increased acid esters but did overcome steric hindrance energetic limitations experienced esters.