A Halophilic Serine Proteinase from Halobacillus sp. SR5-3 Isolated from Fish Sauce: Purification and Characterization

Sirilak NAMWONG; Kazumi HIRAGA; Katsumi TAKADA; Masahiko TSUNEMI; Somboon TANASUPAWAT; Kohei ODA

doi:10.1271/bbb.50658

Biochemistry & Molecular Biology Regular Papers

A Halophilic Serine Proteinase from Halobacillus sp. SR5-3 Isolated from Fish Sauce: Purification and Characterization

Sirilak NAMWONG, Kazumi HIRAGA, Katsumi TAKADA, Masahiko TSUNEMI, Somboon TANASUPAWAT, Kohei ODA

著者情報

キーワード: moderately halophilic bacteria, Halobacillus sp., serine proteinase, fish sauce, fluorescence resonance energy transfer substrate (FRETS)

ジャーナルフリー

2006 年 70 巻 6 号 p. 1395-1401

DOI https://doi.org/10.1271/bbb.50658

詳細

抄録

A halophilic bacterium was isolated from fish sauce, classified, and named Halobacillus sp. SR5-3. A purified 43-kDa proteinase produced by this bacterium showed optimal activity at 50 °C and pH 9–10 in 20% NaCl. The activity of the enzyme was enhanced about 2.5-fold by the addition of 20–35% NaCl, and the enzyme was highly stabilized by NaCl. It was found to be a serine proteinase related to either chymotrypsin or subtilisin. It absolutely preferred Ile at the P₂ position of substrates. Thus, the enzyme was found to be a halophilic serine proteinase with unique substrate specificity.

責任著者(Corresponding author)

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