A Halophilic Serine Proteinase fromHalobacillussp. SR5-3 Isolated from Fish Sauce: Purification and Characterization | Zendy

Sirilak Namwong | Zendy; Kazumi Hiraga | Zendy; Katsumi Takada | Zendy; Masahiko Tsunemi | Zendy; Somboon Tanasupawat | Zendy; Kōhei Oda | Zendy

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

Author(s) -

Sirilak Namwong,

Kazumi Hiraga,

Katsumi Takada,

Masahiko Tsunemi,

Somboon Tanasupawat,

Kōhei Oda

Publication year - 2006

Publication title -

bioscience biotechnology and biochemistry

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.509

H-Index - 116

eISSN - 1347-6947

pISSN - 0916-8451

DOI - 10.1271/bbb.50658

Subject(s) - subtilisin , halophile , serine , enzyme , chemistry , biochemistry , chymotrypsin , bacteria , microbiology and biotechnology , biology , trypsin , genetics

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 degrees 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 P(2) position of substrates. Thus, the enzyme was found to be a halophilic serine proteinase with unique substrate specificity.

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