Thermobarostability of α-chymotrypsin in reversed micelles of aerosol OT in octane solvated by water-glycerol mixtures
✍ Scribed by Roman V. Rariy; Nicole Bec; Natalia L. Klyachko; Andrey V. Levashov; Claude Balny
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 84 KB
- Volume
- 57
- Category
- Article
- ISSN
- 0006-3592
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✦ Synopsis
Thermostability of ␣-chymotrypsin at normal pressure in reversed micelles depends on both an effective surfactant solvation degree and glycerol content in the system. The difference in ␣-chymotrypsin stability in reversed micelles at various glycerol concentrations [up to 60% (v/v)] was more pronounced at high surfactant degrees of solvation, R ജ 16. After a 1-h incubation at 40°C in ''aqueous'' reversed micelles (in the absence of glycerol), ␣-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 watermiscible cosolvent that leads to the decreasing mobility of the ␣-chymotrypsin molecule and, thus the increase of its stability. It was found that glycerol or hydrostatic pressure could be used to stabilize ␣-chymotrypsin in reversed micelles; a lower pressure is necessary to reach a given level of enzyme stability in the presence of glycerol.