Research Article

**Purification and Some Properties of Thermo-stable Alkaline Serine Protease from Thermophilic Bacillus sp. Gs-3**

There are limited reliable information on the commercial production and utilization of proteases for detergent and other industrial uses in Nigeria. Hence, the purification and characterization of Bacillus sp. Gs-3 protease for its potential industrial uses were investigated. The dialyzed crude enzyme was purified 17-fold in a two-step procedure involving carboxymethyl sepharose ionic-exchange chromatography and phenyl sepharose 6-fast flow hydrophobic interaction chromatography. The purified enzyme had its optimal activity at pH 9.0 and 90°C and was stable over a pH range 8.0-11.0. It readily hydrolyzed all the tested protein substrates but exhibited highest affinity for gelatin (Km 0.15 mg mL^-1). It retained at least 66.2±0.02% of its original activity in the presence of the tested local commercial detergents and removed bloodstains completely. Its activity was significantly (p>0.05) enhanced by Cu²⁺ ion but strongly inhibited (75.6±0.07%) by Phenyl-methyl Sulfonyl Fluoride (PMSF). Thus, the enzyme demonstrated desirable properties suitable for its biotechnological applications especially in detergent industry.

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U.O. George-Okafor and F.J.C. Odibo, 2011. Purification and Some Properties of Thermo-stable Alkaline Serine Protease from Thermophilic Bacillus sp. Gs-3. Journal of Biological Sciences, 11: 299-306.

DOI: 10.3923/jbs.2011.299.306

URL: https://scialert.net/abstract/?doi=jbs.2011.299.306

Journal of Biological Sciences

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Authors

U.O. George-Okafor

F.J.C. Odibo

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Research Article

**Purification and Some Properties of Thermo-stable Alkaline Serine Protease from Thermophilic Bacillus sp. Gs-3**

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