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Updated: Aug 18, 2026
Unraveling Entropic Rate Acceleration Induced by Solvent Dynamics in Membrane Enzymes
Published on: January 16, 2016
Enzyme release from heat-stressed cell membranes as a function of hydrophobicity evaluated by using aqueous two-phase
1Department of Chemical Science and Engineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Japan.
Abstract:
The release behavior of a periplasmic enzyme, acid phosphatase, from heat-stressed Escherichia coli cells was characterized by using kinetic analyses when the cells were treated by Triton X-100-EDTA. The hydrophobicity of the cell surface and the release-rate of the enzyme were not influenced by heat treatment at temperatures between 30 and 50 degrees C. However, these values varied above 55 degrees C. The release-rate constants were found to correspond to the net and local hydrophobicity of the outer membrane surface, evaluated by aqueous two-phase partitioning.
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