Characteristics of an extracellular protease isolated from<Emphasis Type="Italic">Bacillus subtilis</Emphasis> AG-1 and its performance in relation to detergent components |
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Authors: | Email author" target="_blank">Afia?GhafoorEmail author Shahida?Hasnain |
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Institution: | 1.Department of Microbiology and Molecular Genetics, Quaid-e-Azam Campus,University of the Punjab,Lahore,Pakistan |
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Abstract: | An extracellular protease isolated fromBacillus subtilis AG-1 was investigated with respect to various detergents and formulation components. The enzyme had optimum at pH 8.0 and 60 °C temperature while zymographic study revealed two activity bands of 24.9 and 18 kDa. It showed high stability towards non-ionic (Tween 20, Tween 80, Triton X-100) and anionic surfactants sodium dodycyl sulfate (SDS), retaining 100 and 71% of its original activity. Another distinctive feature of the enzyme was its efficient stability towards hydrogen peroxide (H2O2) and sodium perborate and different commercial detergent brands. AG-1 protease was also examined for its activity/performance in combination with different stabilizers like glycerol, propylene glycol and polyethylene glycol (PEG). Enzyme showed a promising activity in the presence of this polyols especially PEG (8000). Whilst its compatibility with different commercially available powder and liquid detergents was also very interesting. These results suggest AG-1 protease as a good detergent compatible and can be utilized in the formulation of an environment friendly bio-detergent. |
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