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  • Title: Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: purification, characterization and potential application as a laundry detergent additive.
    Author: Haddar A, Agrebi R, Bougatef A, Hmidet N, Sellami-Kamoun A, Nasri M.
    Journal: Bioresour Technol; 2009 Jul; 100(13):3366-73. PubMed ID: 19269812.
    Abstract:
    Two detergent stable alkaline serine-proteases (BM1 and BM2) from Bacillus mojavensis A21 were purified. The molecular weights of BM1 and BM2 enzymes determined by SDS-PAGE were approximately 29,00 Da and 15,50 Da, respectively. The optimum pH values of BM1 and BM2 proteases were shown to be 8.0-10.0 and 10.0, respectively. Both enzymes exhibited maximal activity at 60 degrees C, using casein as a substrate. The N-terminal amino acid sequences of BM1 and BM2 proteases were AQSVPYGISQIKA and AIPDQAATTLL, respectively. Both proteases showed high stability towards non-ionic surfactants. The enzymes were found to be relatively stable towards oxidizing agents. In addition, both enzymes showed excellent stability and compatibility with a wide range of commercial liquid and solid detergents. These properties and the high activity in high alkaline pH make these proteases an ideal choice for application in detergent formulations.
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