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Journal of Biological Sciences
  Year: 2011 | Volume: 11 | Issue: 4 | Page No.: 299-306
DOI: 10.3923/jbs.2011.299.306
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Purification and Some Properties of Thermo-stable Alkaline Serine Protease from Thermophilic Bacillus sp. Gs-3

U.O. George-Okafor and F.J.C. Odibo

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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How to cite this article:

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






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