在非常规介质中酶酯化过程中,水活性在酶活性和对映选择性方面的作用

IF 0.5 Q4 ENGINEERING, CHEMICAL
Piroska Lajtai-Szabó, N. Nemestóthy, L. Gubicza
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引用次数: 1

摘要

在非常规介质中的酶促酯化过程中,反应介质的含水量显著影响酶的活性和对映选择性,反应介质中的含水量随着酯化过程中产生的水而不断变化。为了提供恒定的反应参数,水的活性应该保持恒定。通常使用的盐水合物对可能难以应用,并且经常阻碍酶活性。在外消旋2-溴丙酸在各种溶剂(有机溶剂、离子液体)中的对映选择性酯化过程中,已证明可以在不使用任何盐或盐水合物对的情况下提供与动力学检查所需的最佳含水量有关的条件。这一结论是基于这样一种认识,即可以通过首先确定在给定溶剂中实现最大反应速率所需的初始水含量来设定最佳水活性。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
The Role of Water Activity in Terms of Enzyme Activity and Enantioselectivity during Enzymatic Esterification in Non-conventional Media
During enzymatic esterification in non-conventional media, the activity and enantioselectivity of the enzyme is significantly influenced by the water content of the reaction medium, which continuously changes as water is produced during the esterification. To provide constant reaction parameters, water activity should be kept constant. The commonly used salt hydrate pairs may be difficult to apply and often hinder enzyme activity. During the enantioselective esterification of racemic 2-bromopropanoic acid in various solvents (organic solvents, ionic liquids), it was proven that the conditions related to the optimal water content required for kinetic examinations can be provided without using any salt or salt hydrate pairs. This conclusion is based on the realization that the optimal water activity can be set by first determining the initial water content that is necessary to achieve the maximum reaction rate in the given solvent.
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自引率
50.00%
发文量
9
审稿时长
6 weeks
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