The mechanistic dissection of the plunge in enzymatic activity upon transition from water to anhydrous solvents

JL Schmitke, CR Wescott…

文献索引：Schmitke, Jennifer L.; Wescott, Charles R.; Klibanov, Alexander M. Journal of the American Chemical Society, 1996 , vol. 118, # 14 p. 3360 - 3365

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被引用次数: 160

摘要

Subtilisin Carlsberg dissolved in aqueous solution is several orders of magnitude more active than the enzyme suspended in anhydrous acetonitrile. In order to ascertain why, we employed crystalline subtilisin lightly cross-linked with glutaraldehyde as a catalyst in both aqueous and organic media. The structure of this crystalline enzyme in acetonitrile had been previously found to be virtually identical to that in water, thus ruling out solvent-induced ...