| Literature DB >> 19269812 |
Anissa Haddar1, Rym Agrebi, Ali Bougatef, Noomen Hmidet, Alya Sellami-Kamoun, Moncef Nasri.
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.Entities:
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Year: 2009 PMID： 19269812 DOI： 10.1016/j.biortech.2009.01.061
Source DB: PubMed Journal: Bioresour Technol ISSN： 0960-8524 Impact factor: 9.642