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KMID : 0364820110470030194
Korean Journal of Microbiology
2011 Volume.47 No. 3 p.194 ~ p.199
Characterization of an Alkaline Protease from an Alkalophilic Bacillus pseudofirmus HS-54
Bang Seong-Ho

Joung In-Sil
Abstract
An alkalophilic bacterium producing alkaline protease was isolated from waste water and solar saltern sample and identified as Bacillus pseudofirmus HS-54 based on morphological, biochemical characteristics as well as 16S-rRNA gene sequencing. The HS-54 protease was purified to homogeneity using ammonium sulfate precipitation, DEAE cellulose column chromatography, and sephadex G-100 gel filtration with a 4.0 purification fold. The molecular mass of the purified enzyme was estimated by SDS-PAGE to be 27 kDa. The optimal pH and temperature for the purified protease activity were 10.0 and 50¡ÆC, respectively. The purified enzyme was relatively stable at the pH range of 6.0-11.0 and at the temperature below 50¡ÆC. This enzyme was activated by Ca2+ and Mg2+ and inhibited by Hg2+, Cu2+, Zn2+, Al3+, Ag2+. And this enzyme was strongly inhibited by PMSF, suggesting that it belongs to the serine protease superfamily.
KEYWORD
Bacillus pseudofirmus HS-54, alkaline protease, purification, serine protease
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