Thermobarostability of α-chymotrypsin in reversed micelles of aerosol OT in octane solvated by water-glycerol mixtures

Publisher Website
Google Scholar
Abstract
Thermostability of α-chymotrypsin at normal pressure in reversed micelles depends on both an effective surfactant solvation degree and glycerol content in the system. The difference in α-chymotrypsin stability in reversed micelles at various glycerol concentrations [up to 60% (v/v)] was more pronounced at high surfactant degrees of solvation, R ⩾ 16. After a 1-h incubation at 40°C in “aqueous” reversed micelles (in the absence of glycerol), α-chymotrypsin retained only 1% of initial catalytic activity and 10, 22, 59, and 48% residual activity in glycerol-solvated micelles with 20, 30, 50, and 60% (v/v) glycerol, respectively. The explanation of the observed effects is given in the frames of micellar matrix structural order increasing in the presence of glycerol as a water-miscible cosolvent that leads to the decreasing mobility of the α-chymotrypsin molecule and, thus the increase of its stability. It was found that glycerol or hydrostatic pressure could be used to stabilize α-chymotrypsin in reversed micelles; a lower pressure is necessary to reach a given level of enzyme stability in the presence of glycerol. ©1998 John Wiley & Sons, Inc. Biotechnol Bioeng 57: 552-556, 1998.

This publication has 20 references indexed in Scilit: