Abstract
An extracellular serine alkaline protease produced by Bacillus sp. SSR1 was purified to homogeneity by Sephadex A-50 and Sepharose 6B column chromatography. The enzyme is a monomeric protein with a molecular weight of 29 and 35 kDa as estimated by SDS–PAGE and native PAGE respectively. The purified enzyme is stable in the alkaline pH range (8.0–11.0) and retains 100% activity at its optimum temperature of 40°C even after 300 min of incubation. The presence of CaCl 2 shifts the optimum temperature to 45°C and produces a 1.3-fold increase in its activity. The enzyme remains active and stable in various detergents and is strongly activated by metal ions (Fe 3+, Ca 2+, Na +)
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