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NALDC Record Details:

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

Permanent URL:
http://handle.nal.usda.gov/10113/50087
Abstract:
Triacylglycerols containing a high abundance of unusual fatty acids, such as γ-linolenic acid, or novel arylaliphatic acids, such as ferulic acid, 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 and sterically hindered acyl donor substrates. The catalytic performance of a circularly permutated variant of CALB, cp283, with various acyl donors and glycerol was examined. In comparison to wild-type CALB, butyl oleate and ethyl γ-linolenate glycerolysis rates were 2.2- and 4.0-fold greater, respectively. Cp283 showed substrate inhibition by glycerol, which was not the case with the wild-type version. With either ethyl ferulate or vinyl ferulate acyl donors, cp283 matched the performance of wild-type CALB. Changes in active site accessibility resulting from circular permutation led to increased catalytic rates for bulky fatty acid esters but did not overcome the steric hindrance or energetic limitations experienced by arylaliphatic esters.
Author(s):
Laszlo, Joseph A. , Yu, Ying , Lutz, Stefan , Compton, David L.
Subject(s):
Candida antarctica , triacylglycerol lipase , mutants , enzyme kinetics , enzyme activity , enzyme substrates , fatty acid esters , glycerol , ferulic acid , esters
Format:
p. 175-180.
Note:
Includes references
Source:
Journal of molecular catalysis. B, Enzymatic 2011 Nov., v. 72, no. 3-4
Language:
English
Year:
2011
Collection:
Journal Articles, USDA Authors, Peer-Reviewed
File:
Download [PDF File]
Rights:
Works produced by employees of the U.S. Government as part of their official duties are not copyrighted within the U.S. The content of this document is not copyrighted.