Mass transfer studies of cell permeabilization and recovery of alkaline phosphatase from Escherichia coli by reverse micellar solutions.
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.
Bansal-Mutalik
Ritu
R
Institute of Chemical Technology, University of Mumbai, Matunga, Mumbai 400019, India.
Gaikar
Vilas G
VG
D000469:Alkaline Phosphatase / Q000302:isolation & purification / Q000378:metabolism*; D002463:Cell Membrane Permeability; D004926:Escherichia coli / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D008823:Micelles; D012996:Solutions; D013501:Surface-Active Agents
D008823:Micelles; D012996:Solutions; D013501:Surface-Active Agents; D000469:Alkaline Phosphatase