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Lipase-catalyzed ethanolysis of borage oil: A kinetic study

机译:脂肪酶催化琉璃苣油的乙醇分解:动力学研究

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Ethanolysis of borage oil catalyzed by two commercial lipases (from Pseudomonas cepacia and Candida antarctica) was studied using two different methodologies. Multiresponse models derived from a generalized Michaelis-Menten mechanism were utilized to describe the rates of formation of ethyl esters of the primary fatty acids present in the precursor oil. The relative rate constants determined for each of the fatty acid residues indicated that both lipases discriminate against release of gamma-linolenic acid residues under the reaction conditions studied. However, both lipases also released some of the residues located at the sn-2 position, indicating that for the experimental conditions studied, both lipases are nonspecific. Moreover, inactivation of Novozym 435 was rapid. Because the half-life of this enzyme (ca. 2.2 h) is comparable to the half-life of the reaction, the intrinsic reaction rate and enzyme deactivation must both be considered in modeling the kinetics.
机译:使用两种不同的方法研究了两种商业脂肪酶(来自假单胞菌和南极假丝酵母)催化的琉璃苣油的乙醇分解。利用源自广义Michaelis-Menten机制的多响应模型来描述前体油中存在的伯脂肪酸乙酯的形成速率。对于每个脂肪酸残基确定的相对速率常数表明,在所研究的反应条件下,两种脂肪酶都与γ-亚麻酸残基的释放有区别。但是,两种脂肪酶也释放了位于sn-2位置的一些残基,这表明在所研究的实验条件下,两种脂肪酶都是非特异性的。此外,Novozym 435的失活很快。由于该酶的半衰期(约2.2小时)与反应的半衰期相当,因此在动力学建模中必须同时考虑固有反应速率和酶失活。

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