Relationship between surface hydrophilicity of a protein and its stability against denaturation by organic solvents
- 24 June 1991
- journal article
- Published by Wiley in FEBS Letters
- Vol. 284 (2) , 267-269
- https://doi.org/10.1016/0014-5793(91)80700-d
Abstract
The stability of α‐chymotrypsin covalently modified with a strongly hydrophilic modifier, pyromellitic dianhydride, against solvent‐induced denaturation in water—organic solvent binary mixtures has been studied. It was found that the hydrophilization results in a strong stabilization of the enzyme against denaturation by organic solvents. The stabilizing effect is explained in terms of the enhanced ability of the hydrophilized enzyme to keep its hydration shell, which is indispensable for supporting the native protein conformation, from denaturing stripping by organic solventsKeywords
This publication has 15 references indexed in Scilit:
- Enzyme stabilization by bilayer “encagement”Enzyme and Microbial Technology, 1989
- Engineering biocatalytic systems in organic media with low water contentEnzyme and Microbial Technology, 1988
- Circular dichroism and fluorescence of polyethylene glycol‐subtilisin in organic solventsFEBS Letters, 1988
- On the importance of the support material for bioorganic synthesisEuropean Journal of Biochemistry, 1988
- Preparation and properties of soluble–insoluble immobilized proteasesBiotechnology & Bioengineering, 1987
- Micellar enzymologyEuropean Journal of Biochemistry, 1986
- Polyethylene glycol-modified enzymes trap water on their surface and exert enzymic activity in organic solventsBiotechnology Letters, 1984
- Water and globular proteinsTrends in Biochemical Sciences, 1983
- Cryoenzymology in mixed solvents without cosolvent effects on enzyme specific activity.Proceedings of the National Academy of Sciences, 1977
- Hydration of Proteins and PolypeptidesAdvances in Protein Chemistry, 1974