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Purification and some properties of a thermostable metal proteinase produced by Thermomicrobium sp. KN-22 strain.

Authors
  • Murao, S
  • Nomura, Y
  • Nagamatsu, K
  • Hirayama, K
  • Iwahara, M
  • Shin, T
Type
Published Article
Journal
Agricultural and biological chemistry
Publication Date
Jul 01, 1991
Volume
55
Issue
7
Pages
1739–1744
Identifiers
PMID: 1368714
Source
Medline
License
Unknown

Abstract

An extreme thermophile that produces a heat-stable proteinase was isolated from hot-spring water and classified as Thermomicrobium sp. KN-22 (growth temperature, 50-83 degrees C; and optimum growth temperature, 70 degrees C). The proteinase was purified from the culture broth of this strain by fractionation with ammonium sulfate, chromatography on columns of DEAE-cellulose and CM-Sepharose CL-6B, and HPLC on TSKgel CM-5PW. The purified enzyme gave a single band on SDS-polyacrylamide gel electrophoresis and a single peak after HPLC (yield 8.8%). The enzyme had maximum activity at pH 8.5 and at 75 degrees C and it was stable up to 60 degrees C. The molecular weight of the enzyme was 35,000 by SDS-PAGE. Since the enzymatic activity was completely inhibited by EDTA, o-phenanthroline, and phosphoramidon, it appears that the enzyme is a metal proteinase.

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