| Autor: |
Tsuchida, Osamu, Yamagata, Yohei, Ishizuka, Takehiko, Arai, Teruyoshi, Yamada, Jun-Ichi, Takeuchi, Michio, Ichishima, Eiji |
| Zdroj: |
Current Microbiology; January 1986, Vol. 14 Issue: 1 p7-12, 6p |
| Abstrakt: |
An alkaline serine proteinase was purfied from the culture broth of an alkalophilicBacillus sp. NKS-21. The molecular weight was estimated to be 22,000 by a gel filtration method and 31,000 by SDS-polyacrylamide gel electrophoresis. The isoelectric point was determined to be 8.2. The amino acid composition and CD spectrum were determined. The alkaline proteinase had a pH optimum at 10–11 for milk casein digestion. The specific activity of the alkaline proteinase was 0.35 katal/kg of protein at pH 10.0 for milk casein hydrolysis. |
| Databáze: |
Supplemental Index |
| Externí odkaz: |
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