Literature DB >> 16794319

A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization.

Sirilak Namwong1, Kazumi Hiraga, Katsumi Takada, Masahiko Tsunemi, Somboon Tanasupawat, Kohei Oda.   

Abstract

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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Year:  2006        PMID： 16794319     DOI： 10.1271/bbb.50658

Source DB:  PubMed          Journal:  Biosci Biotechnol Biochem        ISSN： 0916-8451            Impact factor:   2.043


  11 in total

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