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• W1999265929 abstract "Bacillus subtilis JM-3 was isolated from anchovy sauce naturally fermented in an underground cellar at 15 ± 3C for 3 years. The activity of the B. subtilis protease was highest in the 40–60% ammonium sulfate fraction. The yield of the purified protease was 5.3%, and its purification ratio was 35.6 folds. The molecular weight of the B. subtilis protease was 17.1 kDa, and its Km and Vmaxvalues were 1.75 μg/mL and 318 μM 1/min, respectively. The optimal temperature for protease activity was 60C, but optimal stability temperature was 30C. The optimal pH for protease activity and stability was 5.5. Therefore, the B. subtilis JM-3 protease was classified as an acid protease. The relative activities of the B. subtilis JM-3 protease were 69, 21 and 1.3% at 10, 20 and 30% NaCl concentrations, respectively. The best substrate for the B. subtilis JM-3 protease was benzyloxycarbonyl-glycine-p-nitrophenyl ester followed by bovine serum albumin. p-Toluene-sulfonyl-L-lysine chloromethylketone was the strongest inhibitor followed by soybean trypsin inhibitor, but N-ethylmaleimide did not inhibit this enzyme. The B. subtilis JM-3 protease was therefore presumed to be a trypsin-like serine protease." @default.
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• W1999265929 date "2005-10-01" @default.
• W1999265929 modified "2023-09-25" @default.
• W1999265929 title "PURIFICATION AND CHARACTERIZATION OF BACILLUS SUBTILIS JM-3 PROTEASE FROM ANCHOVY SAUCE" @default.
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• W1999265929 doi "https://doi.org/10.1111/j.1745-4514.2005.00041.x" @default.
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