Premium
Mass Transfer Studies of Cell Permeabilization and Recovery of Alkaline Phosphatase from Escherichia coli by Reverse Micellar Solutions
Author(s) -
BansalMutalik Ritu,
Gaikar Vilas G.
Publication year - 2004
Publication title -
biotechnology progress
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.572
H-Index - 129
eISSN - 1520-6033
pISSN - 8756-7938
DOI - 10.1021/bp049911t
Subject(s) - alkaline phosphatase , chemistry , ionic strength , enzyme , escherichia coli , chromatography , phosphatase , enzyme assay , mass transfer , biochemistry , aqueous solution , organic chemistry , gene
Transfer of alkaline phosphatase (AP) directly from Escherichia coli cells into reverse micellar solutions (RMS) was studied by varying the water content, pH, and ionic strength of RMS. Prior to the mass transfer studies, the optimum conditions for the activity of alkaline phosphatase in reverse micellar solutions were determined. The maximum enzyme activity could be detected at higher pH and water content, indicating the ionization of p‐ nitrophenol to be crucial in the enzyme activity. The transfer of AP from E. coli followed a two‐step process with most of the recovery being achieved in the first 3–10 min beyond which it slowed. A model suggesting separate locations for the enzyme in the cell wall has been proposed.