Enzyme release from heat-stressed cell membranes as a function of hydrophobicity evaluated by using aqueous two-phase systems.
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.
Department of Chemical Science and Engineering, Graduate School of Engineering Science, Osaka University, Toyonaka, Japan.
H
H
Umakoshi
R
R
Kuboi
D000135:Acid Phosphatase / Q000302:isolation & purification*; D002462:Cell Membrane / Q000201:enzymology*; D002623:Chemistry Techniques, Analytical / Q000379:methods*; D004492:Edetic Acid; D004926:Escherichia coli / Q000201:enzymology*; D006358:Hot Temperature; D017830:Octoxynol; D014867:Water
D014867:Water; D017830:Octoxynol; D004492:Edetic Acid; D000135:Acid Phosphatase