Applied Microbiology and Biotechnology

, Volume 26, Issue 1, pp 1–8

Organic solvents for bioorganic synthesis

1. Optimization of parameters for a chymotrypsin catalyzed process
  • Mats Reslow
  • Patrick Adlercreutz
  • Bo Mattiasson
Biotechnology

DOI: 10.1007/BF00282141

Cite this article as:
Reslow, M., Adlercreutz, P. & Mattiasson, B. Appl Microbiol Biotechnol (1987) 26: 1. doi:10.1007/BF00282141

Summary

The influence of solvents on enzymatic activity and stability was investigated. As a model reaction the α-chymotrypsin-catalyzed esterification of N-acetyl-l-phenylalanine with ethanol was used. The enzyme was adsorbed on porous glass beads and used in various solvents. Small amounts of water were added to increase the enzymatic activity. These enzyme preparations obeyed. Michaelis-Menten kinetics. Km,app decreased slightly with the log P value of the solvent while Vapp increased markedly with the log P value. Log P values were also useful for generalizing the influence of solvents on enzyme stability. The enzyme preparations showed a markedly higher thermostability in dry solvents having log P values >0.7 than in less hydrophobic solvents.

Also the operational stability was better in the more hydrophobic solvents. The amount of water added to the enzyme preparations greatly influenced the initial reaction rates. For some solvents optimal water contents were determined. The thermostability decreased with increasing water content.

The observations are summarized in the conclusion that more hydrophobic solvents are preferable to less hydrophobic ones. The log P value gives a good guidance when selecting an organic solvent for enzymatic conversions.

Copyright information

© Springer-Verlag 1987

Authors and Affiliations

  • Mats Reslow
    • 1
  • Patrick Adlercreutz
    • 1
  • Bo Mattiasson
    • 1
  1. 1.Department of Biotechnology, Chemical CenterUniversity of LundLundSweden