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Updated: Apr 29, 2026
Recombinant Protein Expression, Crystallization, and Biophysical Studies of a Bacillus-conserved Nucleotide Pyrophosphorylase, BcMazG
Published on: May 16, 2017
Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: purification, characterization and
Anissa Haddar1, Rym Agrebi, Ali Bougatef
1Laboratoire de Génie Enzymatique et de Microbiologie -Ecole Nationale d'Ingénieurs de Sfax, Sfax, Tunisia.
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.
