Improved triglyceride transesterification by circular permuted Candida antarctica lipase B.
Lipases represent a versatile class of biocatalysts with numerous potential applications in industry including the production of biodiesel via enzyme-catalyzed transesterification. In this article, we have investigated the performance of cp283, a variant of Candida antarctica lipase B (CALB) engineered by circular permutation, with a series of esters, as well as pure and complex triglycerides. In comparison with wild-type CALB, the permutated enzyme showed consistently higher catalytic activity (2.6- to 9-fold) for trans and interesterification of the different substrates with 1-butanol and ethyl acetate as acyl acceptors. Differences in the observed rates for wild-type CALB and cp283 are believe to be related to changes in the rate-determining step of the catalytic cycle as a result of circular permutation.
Yu
Ying
Y
Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322, USA.
Lutz
Stefan
S
D002175:Candida / Q000201:enzymology*; D002384:Catalysis; D004800:Enzymes, Immobilized; D004951:Esterification; D005656:Fungal Proteins; D007700:Kinetics; D008049:Lipase / Q000737:chemistry / Q000378:metabolism*; D015394:Molecular Structure; D014280:Triglycerides / Q000737:chemistry / Q000378:metabolism*
D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D014280:Triglycerides; D008049:Lipase; C431349:lipase B, Candida antarctica