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- W2043928040 abstract "A proteolytic enzyme produced by Bacillus subtilis CHZ1 was purified using ammonium sulfate precipitation, gel filtration and cationic exchange on S-Sepharose fast flow column chromatography. Production of the protease was higher when the Bacillus strain was cultured in a synthetic medium, M162, supplemented with 0.3% (w/v) organic compared to inorganic nitrogen sources. Enzyme production was growth dependent and production was highest when tryptone was used as the nitrogen source. When run on SDS-PAGE gel, the purified enzyme gave a 35 kDa band, suggesting that it consisted of one polypeptide chain. High enzyme activity was observed in the pH range of 6–10 with a maximum value at pH 8.0 when 0.5% (w/v) azocasein was used as the substrate. Optimum temperature for protease activity was found to be 60–80C, and the enzyme had considerable thermal stability for 5.5 h retaining about 90% activity after 5.5 h. At 2.5 mM concentration, PMSF, Ag+ and Hg+ inhibited activity of the protease. Metal cofactors like Mn2+, Mg2+ and Fe2+ increased the enzyme activity by about 20%. Zn2+, Cu2+ and Ca2+ did not affect the enzyme's activity. The pH and thermal stability as well as high specific activity of this enzyme can be exploited for industrial applications." @default.
- W2043928040 created "2016-06-24" @default.
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- W2043928040 date "2001-02-01" @default.
- W2043928040 modified "2023-09-26" @default.
- W2043928040 title "PURIFICATION OF A PROTEASE FROM AN ALKALOPHlLIC BACILLUS SUBTILIS CHZ1 ISOLATED FROM A ZIMBABWEAN HOT SPRING" @default.
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- W2043928040 doi "https://doi.org/10.1111/j.1745-4514.2001.tb00721.x" @default.
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