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Intrinsic effects of solvent polarity on enzymic activation energies
Author(s) -
Kim Jungbae,
Clark Douglas S.,
Dordick Jonathan S.
Publication year - 2000
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(20000105)67:1<112::aid-bit13>3.0.co;2-e
Subject(s) - subtilisin , chemistry , polarity (international relations) , activation energy , catalysis , polar , solvent , solubility , transesterification , solvent effects , enzyme catalysis , saturation (graph theory) , organic solvent , substrate (aquarium) , organic chemistry , thermodynamics , enzyme , chemical engineering , biochemistry , oceanography , engineering , geology , physics , mathematics , combinatorics , astronomy , cell
The effect of organic solvents on subtilisin Carlsberg catalysis has been investigated with the aid of a thermodynamic analysis. Saturation solubility experiments were performed to provide a quantitative measure of substrate desolvation from the reaction medium. This enabled calculation of the intrinsic enzymic activation energy and resulted in a linear free energy relationship with respect to solvent polarity. The results indicate that the intrinsic activation energy of subtilisin catalysis is lowest in polar organic solvents, which may be due to transition state stabilization of the enzyme's polar transition state for transesterification. © 2000 John Wiley & Sons, Inc. Biotechnol Bioeng 67: 112–116, 2000.