Intrinsic effects of solvent polarity on enzymic activation energies

Jungbae Kim, Douglas S. Clark, Jonathan S. Dordick

Research output: Contribution to journalArticle

37 Citations (Scopus)

Abstract

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.

Original languageEnglish
Pages (from-to)112-116
Number of pages5
JournalBiotechnology and Bioengineering
Volume67
Issue number1
DOIs
Publication statusPublished - 2000 Jan 5
Externally publishedYes

Fingerprint

Organic solvents
Catalysis
Activation energy
Subtilisins
Subtilisin
Saturation (materials composition)
Transesterification
Free energy
Enzymes
Stabilization
Solubility
Thermodynamics
Substrates
Experiments

Keywords

  • Intrinsic activation energies
  • Nonaqueous enzymology
  • Solvent polarity
  • Subtilisin catalysis

ASJC Scopus subject areas

  • Biotechnology
  • Microbiology

Cite this

Intrinsic effects of solvent polarity on enzymic activation energies. / Kim, Jungbae; Clark, Douglas S.; Dordick, Jonathan S.

In: Biotechnology and Bioengineering, Vol. 67, No. 1, 05.01.2000, p. 112-116.

Research output: Contribution to journalArticle

Kim, Jungbae ; Clark, Douglas S. ; Dordick, Jonathan S. / Intrinsic effects of solvent polarity on enzymic activation energies. In: Biotechnology and Bioengineering. 2000 ; Vol. 67, No. 1. pp. 112-116.
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