ISSN:
0006-3592
Keywords:
baroenzymology
;
reversed micelles
;
α-chymotrypsin
;
catalytic activity and stability
;
effect of pressure, temperature, and glycerol
;
Chemistry
;
Biochemistry and Biotechnology
Source:
Wiley InterScience Backfile Collection 1832-2000
Topics:
Biology
,
Process Engineering, Biotechnology, Nutrition Technology
Notes:
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.
Additional Material:
4 Ill.
Type of Medium:
Electronic Resource
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