• Title/Summary/Keyword: Bacillus subtilis PANH765

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Isolation and Characterization of Pretense Producing Bacteria from Soil (토양으로부터 Protease 생산 세균의 분리 및 특성)

  • 김관필;이창호;우철주;김남형;배동호
    • Journal of the Korean Society of Food Science and Nutrition
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    • v.31 no.5
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    • pp.754-759
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    • 2002
  • In order to develope a new pretense applicable to industries, a bacterium which produces a remarkable amount of extracellular pretense were isolated from soil. About 10 bacterial strains producing pretense were isolated from samples of soil, and strain PANH765 showed the highest activity of pretense production among them. The strain was identified as Bacillus subtilis according to the Bergey's Manual of Systematic Bacteriology based on its morphological, cultural and physiological characteristics. B. subtilis PANH765 showed the maximal production of pro-tease in the medium containing 2.0% glucose, 1.0% yeast extract, 0.2% ammonium nitrate, 0.02% ferrous sulfate and 0.02% dipotassium hydrogen phosphate. Under the optimal condition with temperature of 3$0^{\circ}C$, initial pH of 7.0 and shaking speed of 150 rpm, the pretense production reached a maximum level with 36 hr cultivation (6.34 U).

Purification and Characterization of Protease from Bacillus subtilis PANH765 (Bacillus subtilis PANH765가 생산하는 Protease의 정제 및 특성)

  • 이창호;우철주;베동호;김관필
    • Food Science and Preservation
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    • v.10 no.2
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    • pp.246-251
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    • 2003
  • Pretense produced by Bacillus subtilis PANH765 was purified from culture supernatant by using ammonium sulfate fractionation DEAE-cellulose ion exchange chromatography, and gel filtration with Sephacryl S 200 HR and Sepharose CL-6B. DEAE-cellulose ion exchange column chromatography, separated the pretense into one fraction. This fraction was further purified using Sephacryl S 200 HR and Sepharose CL-6B gel titration. The molecular mass of pretense was estimated to be 35.0 kDa by the SDS-PAGE and gel filtration using Sepharose CL-6B. The results indicated that the purified pretense are monomeric proteins. Specific activity and purification folds of pretense were 657 U/mg and 4.35, respectively. The optimum temperature, optimum pit stable at a temperature range and pH ranges for the purified protease were 65$^{\circ}C$, 7.05, 50 ∼ 75$^{\circ}C$ and 6.0 ∼ 7.5, respectively. The pretense activity was decreased by the presence of PMSF and DFP, which the protease activity was increased by the presence of Na$\^$+/, K$\^$+/, Mg$\^$2+/ and NH$_4$$\^$+/ ions.