2000•Korean Journal of Food Science and TechnologyRequires access

Characteristics of Protease Produced by Bacillus subtilis PCA 20-3 isolated from Korean Traditional Meju

Seong‐Il Lim, Hyun-Kyu Kim, Jin-Young Yoo

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Abstract

Protease production and its characteristics were investigated with Bacillus subtilis PCA20-3 which was isolated from Korean traditional meju. The optimum culture conditions of Bacillus subtilis PCA20-3 for the production of the protease were as follow: 0.2% soytone, 2% starch, 0.1% and 20 hrs. The optimum pH and temperature for enzyme activity of protease producing Bacillus subtilis PCA20-3 were pH 8.0-10.0 and , respectively. The enzyme was relatively stable at pH and at temperature below . The activity of the enzyme was inhibited by . 2 mM phenymethanesulfonyl fluoride inhibited 89.2% of enzyme activity. This indicates that the enzyme is serine protease. The value was . This enzyme hydrolyzed casein more rapidly than bovine serum albumin.

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What this paper is about

Protease production and its characteristics were investigated with Bacillus subtilis PCA20-3 which was isolated from Korean traditional meju. The optimum culture conditions of Bacillus subtilis PCA20-3 for the production of the protease were as follow: 0.2% soytone, 2% starch, 0.1% and 20 hrs. The optimum pH and temperature for enzyme activity of protease producing Bacillus subtilis PCA20-3 were pH 8.0-10.0 and , respectively. The enzyme was relatively stable at pH and at temperature below . The activity of the enzyme was inhibited by . 2 mM phenymethanesulfonyl fluoride inhibited 89.2% of enzyme activity. This indicates that the enzyme is serine protease. The value was . This enzyme hydrolyzed casein more rapidly than bovine serum albumin.

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Available abstract

Protease production and its characteristics were investigated with Bacillus subtilis PCA20-3 which was isolated from Korean traditional meju. The optimum culture conditions of Bacillus subtilis PCA20-3 for the production of the protease were as follow: 0.2% soytone, 2% starch, 0.1% and 20 hrs. The optimum pH and temperature for enzyme activity of protease producing Bacillus subtilis PCA20-3 were pH 8.0-10.0 and , respectively. The enzyme was relatively stable at pH and at temperature below . The activity of the enzyme was inhibited by . 2 mM phenymethanesulfonyl fluoride inhibited 89.2% of enzyme activity. This indicates that the enzyme is serine protease. The value was . This enzyme hydrolyzed casein more rapidly than bovine serum albumin.

Key concepts: Bacillus subtilis, Protease, Enzyme, Casein, Serine protease, Chemistry, Hydrolysis, Biochemistry

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