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Preparation and characterization of proteases from Thermoactinomyces vulgaris V. Investigations on autolysis and thermostability of the purified protease
Author(s) -
Behnke U.,
Ruttloff H.,
Kleine R.
Publication year - 1982
Publication title -
zeitschrift für allgemeine mikrobiologie
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.58
H-Index - 54
eISSN - 1521-4028
pISSN - 0044-2208
DOI - 10.1002/jobm.19820220802
Subject(s) - thermostability , proteases , autolysis (biology) , protease , biochemistry , chemistry , alkaline protease , enzyme
Thermitase, the main component of the proteases of the culture medium from Thermactinomyces vulgaris , is degraded by autolyses (increase of liberated amino groups) and thereby inactivated especially at elevated temperature, at alkaline pH‐values and in the absence of added substrates. As shown by polyacrylamide gel electrophoresis autolysis is an essential part during heat inactivation (complete disappearance of the thermitase band after heating the enzyme at 85°C for 5 min). The quantitative comparison of autolysis and heat inactivation as well as the kinetics of reversible inhibition of the enzyme by HgCl 2 at different temperatures showed that above 60°C thermal denaturation of the enzyme protein contributes to thermitase inactivation. Ca 2+ ‐ions (20 mM) have a stabilizing effect against both autolysis and thermal denaturation (inactivation) of thermitase.