| Autor: |
Zamost, Bruce L., Brantley, Quintin I., Elm, Dana D., Beck, Carol M. |
| Zdroj: |
Journal of Industrial Microbiology and Biotechnology; July 1990, Vol. 5 Issue: 5 p303-312, 10p |
| Abstrakt: |
Summary An asporogenous mutant ofBacillus stearothermophilus (TPM-8) which produces 4-fold higher levels of a thermostable neutral protease than does wild-type strain 308-1 was obtained by mutagenesis with ethyl methanesulfonate. The protease produced by both the mutant and wild-type strain is a metalloprotease requiring Zn2+ and Ca2+ for activity and thermostability, respectively. It has a temperature optimum of 80°C at pH 7.0 and is highly thermostable, retaining 60% of its activity after 60 min at 85°C. The properties of the enzyme are similar to those of thermolysin. |
| Databáze: |
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