Premium
High‐pressure stabilization of α‐chymotrypsin entrapped in reversed micelles of aerosol OT in octane against thermal inactivation
Author(s) -
Rariy Roman V.,
Bec Nicole,
Saldana J.-L.,
Nametkin Sergey N.,
Mozhaev Vadim V.,
Klyachko Natalia L.,
Levashov Andrey V.,
Balny Claude
Publication year - 1995
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(95)00344-9
Subject(s) - micelle , chemistry , chymotrypsin , aerosol , octane , biophysics , chromatography , trypsin , biochemistry , organic chemistry , enzyme , biology , aqueous solution
α‐Chymotrypsin (CT) solubilized in reversed micelles of sodium bis‐(2‐ethylhexyl)‐sulfosuccinate (AOT) undergoes thermal inactivation and the enzyme stability decreases significantly when temperature increases (25–40°C). The half‐life of CT in micelles shows a bell‐shaped dependence on the degree of hydration of AOT ( w 0 ) analogous to the previously obtained dependence on w 0 for the enzyme activity. The optima of catalytic activity and thermal stability have been observed under conditions where the diameter of the inner aqueous cavity of the micelle is close to the size of the enzyme molecule ( w 0 = 10). Application of high hydrostatic pressure in the range of 1–1500 atm (bar) stabilizes CT against thermal inactivation at all hydration degrees ( w 0 ) from 7 to 20; the stabilization effect is most pronounced under the experimental conditions being far from the optimum for catalytic activity.