Cost effective characterization process and molecular dynamic simulation of detergent compatible alkaline protease from Bacillus pumilus strain MP27
A psychrothermotolerant alkaline protease isolated from Bacillus pumilus MP27 with a
molecular mass∼ 53 kDa was isolated from Southern ocean water samples. It was partially
purified by single step TPP with purity fold of 16.65. The enzyme was found to be widely
stable within a range of temperature and pH, maintaining 52.25% of its activity at 50° C and
92% at pH 12. The enzyme exhibited an exceptional activity along with tested detergents,
showing 98% stability with SDS (10 mg/ml) and ̴ 99% stability with Tide detergent (7 …
molecular mass∼ 53 kDa was isolated from Southern ocean water samples. It was partially
purified by single step TPP with purity fold of 16.65. The enzyme was found to be widely
stable within a range of temperature and pH, maintaining 52.25% of its activity at 50° C and
92% at pH 12. The enzyme exhibited an exceptional activity along with tested detergents,
showing 98% stability with SDS (10 mg/ml) and ̴ 99% stability with Tide detergent (7 …
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