Effect of the solvent on enzyme enantioselectivity

Research output: Chapter in Book/Report/Conference proceedingChapter

7 Citations (Scopus)


The Candida cylindracea lipase catalyzed enantioselective esterification of 2-chloropropionic acid was studied in different solvents with constant initial water content in the reaction mixture. The effect of solvents and solvent mixtures with different hydrophobicity (e.g. log P value) on the activity and enantioselectivity of the enzyme was investigated. The log P values showed a linear correlation with the initial reaction rate as well as with the enantioselectivity. The rate increased while the enantioselectivity slightly decreased with increasing log P values. In solvent mixtures the activity of the enzyme was generally determined by the solvent with the lowest hydrophobicity while the correlation between the average log P value and the enantioselectivity was linear.

Original languageEnglish
Title of host publicationProgress in Biotechnology
Number of pages7
Publication statusPublished - Jan 1 1992

Publication series

NameProgress in Biotechnology
ISSN (Print)0921-0423


ASJC Scopus subject areas

  • Biotechnology

Cite this

Gubicza, L. (1992). Effect of the solvent on enzyme enantioselectivity. In Progress in Biotechnology (C ed., pp. 497-503). (Progress in Biotechnology; Vol. 8, No. C). https://doi.org/10.1016/B978-0-444-89046-7.50073-4