Author(s): Namwong S, Hiraga K, Takada K, Tsunemi M, Tanasupawat S,
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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.
This article was published in Biosci Biotechnol Biochem
and referenced in Journal of Bioremediation & Biodegradation