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首页> 外文期刊>Biophysical Chemistry: An International Journal Devoted to the Physical Chemistry of Biological Phenomena >Cosolvent and pressure effects on enzyme-catalysed hydrolysis reactions
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Cosolvent and pressure effects on enzyme-catalysed hydrolysis reactions

机译：酶催化水解反应的共溶剂和压力影响

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摘要

Thermodynamics and kinetics of biochemical reactions depend not only on temperature, but also on pressure and on the presence of cosolvents in the reaction medium. Understanding their effects on biochemical processes is a crucial step towards the design and optimization of industrially relevant enzymatic reactions. Such reactions typically do not take place in pure water. Cosolvents might be present as they are either required as stabilizer, as solubilizer, or in their function to overcome thermodynamic or kinetic limitations. Further, a vast number of enzymes has been found to be piezophilic or at least pressure-tolerant, meaning that nature has adapted them to high-pressure conditions. In this manuscript, we review existing data and we additionally present some new data on the combined cosolvent and pressure influence on the kinetics of biochemical reactions. In particular, we focus on cosolvent and pressure effects on Michaelis constants and catalytic constants of α-CT-catalysed peptide hydrolysis reactions. Two different substrates were considered in this work, N-succinyl-L-phenylalanine-p-nitroanilide and H-phenylalanine-p-nitroanilide. Urea, trimethyl-N-amine oxide, and dimethyl sulfoxide have been under investigation as these cosolvents are often applied in technical as well as in demonstrator systems. Pressure effects have been studied from ambient pressure up to 2 kbar. The existing literature data and the new data show that pressure and cosolvents must not be treated as independent effects. Non-additive interactions on a molecular level lead to a partially compensatory effect of cosolvents and pressure on the kinetic parameters of the hydrolysis reactions considered.
机译：生物化学反应的热力学和动力学不仅取决于温度，还取决于压力和在反应介质中的阳离子存在。理解他们对生化过程的影响是朝着工业上相关的酶促反应的设计和优化的关键步骤。这种反应通常不会发生在纯水中。共溶剂可能存在，因为它们需要作为稳定剂，作为溶解剂，或克服热力学或动力学限制的功能。此外，已发现大量酶被用压叠或至少耐腐蚀性，这意味着性质使它们适应高压条件。在本手稿中，我们审查了现有数据，我们还在对生物化学反应动力学进行了综合的共溶剂和压力影响的一些新数据。特别是，我们专注于对迈克莱斯常数和α-CT催化肽水解反应的迈克莱斯常数和催化常数的压力影响。在该工作中考虑了两种不同的底物，N-琥珀酰-1-苯丙氨酸-P-硝基苯胺和H-苯丙氨酸-P-硝基烷。尿素，三甲基-N-胺氧化物和二甲基亚甲醚已经进行了研究，因为这些助剂通常在技术以及演示系统中应用。已经从环境压力中研究了压力效应，高达2 kbar。现有的文献数据和新数据表明，压力和助理不得被视为独立效应。分子水平上的非添加剂相互作用导致诸如考虑的水解反应的动力学参数的部分补偿效果和压力。

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