Improved triglyceride transesterification by circular permuted Candida antarctica lipase B

Authors

  • Ying Yu,

    1. Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322; telephone: 404-712-2170; fax: 404-727-6586
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  • Stefan Lutz

    Corresponding author
    1. Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322; telephone: 404-712-2170; fax: 404-727-6586
    • Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322; telephone: 404-712-2170; fax: 404-727-6586.
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Abstract

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. Biotechnol. Bioeng. 2010;105: 44–50. © 2009 Wiley Periodicals, Inc.

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