Discriminating between dispersion and lyoprotection effects in biocatalysis in organic media
- 1 June 2002
- journal article
- Published by Canadian Science Publishing in Canadian Journal of Chemistry
- Vol. 80 (6) , 551-554
- https://doi.org/10.1139/v02-026
Abstract
The increment of activity and solubility in 1,4-dioxane of lipase B from Candida antarctica, lipase from Pseudomonas cepacia, and subtilisin, were investigated as a function of the methoxypoly(ethylene glycol)–protein (PEG–protein) ratio employed during lyophilization. Both activity and solubility markedly increased as the PEG–protein ratio was increased. The increment of activity at low PEG–protein ratios, however, was much higher than that of solubility. These data suggest that the PEG-induced activation effect is due mainly to a lyoprotection effect rather than to relaxation of diffusional limitations.Key words: hydrolases, activity, dispersion, lyoprotection, circular dichroism.Keywords
This publication has 19 references indexed in Scilit:
- Chemical modification probes accessibility to organic phase: proteins on surfaces are more exposed than in lyophilized powdersEnzyme and Microbial Technology, 2000
- Why are enzymes less active in organic solvents than in water?Trends in Biotechnology, 1997
- Lyophilization-induced reversible changes in the secondary structure of proteins.Proceedings of the National Academy of Sciences, 1995
- A Lipid-Coated Lipase as an Enantioselective Ester Synthesis Catalyst in Homogeneous Organic SolventsThe Journal of Organic Chemistry, 1995
- Mechanism of extraction of chymotrypsin into isooctane at very low concentrations of aerosol OT in the absence of reversed micellesBiotechnology & Bioengineering, 1994
- Salts dramatically enhance activity of enzymes suspended in organic solventsJournal of the American Chemical Society, 1994
- Effects of water activity on Vmax and KM of lipase catalyzed transesterification in organic mediaBiotechnology Letters, 1993
- Dramatic enhancement of enzymatic activity in organic solvents by lyoprotectantsBiotechnology & Bioengineering, 1993
- Solvent variation inverts substrate specificity of an enzymeJournal of the American Chemical Society, 1993
- Effect of the enzyme form on the activity, stability and enantioselectivity of lipoprotein lipase in tolueneBiotechnology Letters, 1992