Department of Chemistry, Emory University, 1515 Dickey Drive, Atlanta, Georgia 30322, USA.
Biotechnol Bioeng. 2010 Jan 1;105(1):44-50. doi: 10.1002/bit.22471.
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.
脂肪酶是一类用途广泛的生物催化剂，在工业中有众多潜在的应用，包括通过酶促转酯化作用生产生物柴油。在本文中，我们研究了经回旋置换工程改造的南极假丝酵母脂肪酶 B（CALB）变体 cp283 对一系列酯以及纯和混合三酸甘油酯的催化性能。与野生型 CALB 相比，该置换酶对不同底物与 1-丁醇和乙酸乙酯作为酰基受体的 trans 和酯交换反应表现出始终更高的催化活性（2.6 至 9 倍）。观察到的野生型 CALB 和 cp283 的速率差异被认为与回旋置换导致催化循环的速率决定步骤发生变化有关。
