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  • Title: A halophilic serine proteinase from Halobacillus sp. SR5-3 isolated from fish sauce: purification and characterization.
    Author: Namwong S, Hiraga K, Takada K, Tsunemi M, Tanasupawat S, Oda K.
    Journal: Biosci Biotechnol Biochem; 2006 Jun; 70(6):1395-401. PubMed ID: 16794319.
    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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