Purification of Collagenase and Specificity of Its Related Enzyme from Bacillus subtilis FS-2
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概要
- 論文の詳細を見る
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℃. The purified enzyme was stable over a wide range of pH (5-10) and lost only 15% and 35% activity after incubation at 60℃ and 65℃ 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.
- 社団法人日本農芸化学会の論文
- 2000-01-23
著者
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To Kim
Institute Of Biological And Food Technology Hanoi University Of Technology
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NAGANO Hiroko
Faculty of Education, Gifu University
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To K
Institute Of Biological And Food Technology Hanoi University Of Technology
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TO KimAnh
Center for Biotechnology, Hanoi University of Technology
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Nagano Hiroko
Faculty Of Education Gifu University
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To Kim
Center for Biotechnology, Hanoi University of Technology
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