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On enzymatic activity in organic solvents as a function of enzyme history
Author(s) -
Ke Tao,
Klibanov Alexander M.
Publication year - 1998
Publication title -
biotechnology and bioengineering
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.136
H-Index - 189
eISSN - 1097-0290
pISSN - 0006-3592
DOI - 10.1002/(sici)1097-0290(19980320)57:6<746::aid-bit12>3.0.co;2-5
Subject(s) - enzyme , chemistry , function (biology) , organic chemistry , enzyme inhibition , biochemistry , biology , evolutionary biology
Catalytic activities of α‐chymotrypsin and subtilisin Carlsberg in various hydrous organic solvents were measured as a function of how the enzyme suspension had been prepared. In one method, lyophilized enzyme was directly suspended in the solvent containing 1% water. In another, the enzyme was precipitated from its aqueous solution by a 100‐fold dilution with an anhydrous solvent. In most cases, the reaction rate in a given nonaqueous enzymatic system strongly (up to an order of magnitude) depended on the mode of enzyme preparation. The magnitude of this dependence was markedly affected by the nature of the solvent and enzyme. A mechanistic hypothesis proposed to explain the observed dependencies was verified in additional experiments in which the water contents and enzyme history were further varied. © 1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 746–750, 1998