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

Overview

Journal Biosci Biotechnol Biochem

Publisher Oxford University Press

Specialties Biochemistry
Biotechnology

Date 2006 Jun 24

PMID 16794319

Citations 14

Authors

Sirilak Namwong

Kazumi Hiraga

Katsumi Takada

Masahiko Tsunemi

Somboon Tanasupawat

Kohei Oda

Affiliations

Soon will be listed here.

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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