Purification of collagenase and specificity of its related enzyme from Bacillus subtilis FS-2

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Abstract

A collagenase in the culture supernatant of B. subtilis FS-2, isolated from traditional fish sauce, was purified. The enzyme had a molecular mass of about 125 kDa. It degraded gelatin with maximum activity at pH 9 and a temperature of 50°C. The purified enzyme was stable over a wide range of pH (5-10) and lost only 15% and 35% activity after incubation at 60°C and 65°C for 30 min, respectively. Slightly inhibited by EDTA, soybean tripsin inhibitor, iodoacetamide, and iodoacetic acid, the enzyme was severely inhibited by 2-β-mercaptoethanol and DFP. The protease from B. subtilis FS-2 culture digested acid casein into fragments with hydrophilic and hydrophobic amino acids as C-terminals, in particular Asn, Gly, Val, and Ile.

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Nagano, H., & To, K. A. (2000). Purification of collagenase and specificity of its related enzyme from Bacillus subtilis FS-2. Bioscience, Biotechnology and Biochemistry, 64(1), 181–183. https://doi.org/10.1271/bbb.64.181

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