HIGH-PRESSURE STABILIZATION OF ALPHA-CHYMOTRYPSIN ENTRAPPED IN REVERSED MICELLES OF AEROSOL OT IN OCTANE AGAINST THERMAL INACTIVATION

Citation
Rv. Rariy et al., HIGH-PRESSURE STABILIZATION OF ALPHA-CHYMOTRYPSIN ENTRAPPED IN REVERSED MICELLES OF AEROSOL OT IN OCTANE AGAINST THERMAL INACTIVATION, FEBS letters, 364(1), 1995, pp. 98-100
Citations number
16
Categorie Soggetti
Biophysics,Biology
Journal title
ISSN journal
00145793
Volume
364
Issue
1
Year of publication
1995
Pages
98 - 100
Database
ISI
SICI code
0014-5793(1995)364:1<98:HSOAEI>2.0.ZU;2-Q
Abstract
alpha-Chymotrypsin (CT) solubilized in reversed micelles of sodium bis -(2-ethylhexyl)-sulfosuccinate (AOT) undergoes thermal inactivation an d the enzyme stability decreases significantly when temperature increa ses (25-40 degrees C). The half-life of CT in micelles shows a bell-sh aped dependence on the degree of hydration of AOT (w(o)) analogous to the previously obtained dependence on w(o) for the enzyme activity. Th e optima of catalytic activity and thermal stability have been observe d under conditions where the diameter of the inner aqueous cavity of t he micelle is close to the size of the enzyme molecule (w(o) = 10). Ap plication of high hydrostatic pressure in the range of 1-1500 atm (bar ) stabilizes CT against thermal inactivation at all hydration degrees (w(o)) from 7 to 20; the stabilization effect is most pronounced under the experimental conditions being far from the optimum for catalytic activity.