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HIGH-PRESSURE STABILIZATION OF ALPHA-CHYMOTRYPSIN ENTRAPPED IN REVERSED MICELLES OF AEROSOL OT IN OCTANE AGAINST THERMAL INACTIVATIONстатья
Информация о цитировании статьи получена из
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Web of Science
Статья опубликована в журнале из списка Web of Science и/или Scopus
Дата последнего поиска статьи во внешних источниках: 18 июля 2013 г.
- Авторы: RARIY RV, BEC N., SALDANA JL, NAMETKIN SN, MOZHAEV VV, KLYACHKO NL, LEVASHOV AV, BALNY C.
- Журнал: FEBS Letters
- Том: 364
- Номер: 1
- Год издания: 1995
- Издательство: Elsevier BV
- Местоположение издательства: Netherlands
- Первая страница: 98
- Последняя страница: 100
- DOI: 10.1016/0014-5793(95)00344-9
- Аннотация: alpha-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 degrees C). The half-life of CT in micelles shows a bell-shaped dependence on the degree of hydration of AOT (w(o)) analogous to the previously obtained dependence on w(o) 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(o) = 10). Application 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.
- Добавил в систему: Клячко Наталья Львовна