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用于有机溶剂中酶催化水控制的盐水对的选择。

Selection of salt hydrate pairs for use in water control in enzyme catalysis in organic solvents.

机构信息

Department of Bioscience & Biotechnology, University of Strathclyde, Glasgow G1 1XW, UK.

出版信息

Biotechnol Bioeng. 1997 Jul 20;55(2):367-74. doi: 10.1002/(SICI)1097-0290(19970720)55:2<367::AID-BIT14>3.0.CO;2-E.

Abstract

The water activities (a(w)) of 13 salt hydrate pairs were determined from vapor pressure measurements; a(w) values for a subset were also estimated from a study of water transfer to isopropylether. The application of salt hydrates as water buffers was investigated in two models: (i) effect of hydration on the initial rate of subtilisincatalyzed transesterification of the nitrophenol ester of CBZ-alanine with butanol; and (ii) effect of hydrates on the equilibrium concentrations of reactants in the esterification of dodecanol and decanoic acid, catalyzed by lipase. Transfer of ions from salt to enzyme particles was also demonstrated. The implications of the results for the successful use of salt hydrates as water buffers are discussed. (c) 1997 John Wiley & Sons, Inc. Biotechnol Bioeng 55: 367-374, 1997.

摘要

从蒸汽压测量中确定了 13 对盐水合物的水活度(a(w));还从水向异丙醚转移的研究中估算了一部分 a(w)值。盐水合物作为水缓冲剂的应用在两个模型中进行了研究:(i)水合作用对枯草杆菌蛋白酶催化的苯甲酰丙氨酸 CBZ-酯与丁醇的转酯化初始速率的影响;和 (ii)水合作用对脂肪酶催化的十二醇和癸酸酯化反应中反应物平衡浓度的影响。还证明了离子从盐到酶颗粒的转移。讨论了这些结果对成功使用盐水合物作为水缓冲剂的意义。(c)1997 年 John Wiley & Sons, Inc. 生物工程 55:367-374, 1997。

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