Two detergent stable alkaline serine-proteases from Bacillus mojavensis A21: purification, characterization and potential application as a laundry detergent additive.
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.
Haddar
Anissa
A
Laboratoire de Génie Enzymatique et de Microbiologie -Ecole Nationale d'Ingénieurs de Sfax, Sfax, Tunisia.
Agrebi
Rym
R
Bougatef
Ali
A
Hmidet
Noomen
N
Sellami-Kamoun
Alya
A
Nasri
Moncef
M
D000180:Acrylic Resins / Q000737:chemistry; D000595:Amino Acid Sequence; D001407:Bacillus / Q000201:enzymology*; D001709:Biotechnology / Q000379:methods*; D002364:Caseins / Q000737:chemistry; D002850:Chromatography, Gel; D002852:Chromatography, Ion Exchange / Q000379:methods; D003902:Detergents / Q000737:chemistry* / Q000494:pharmacology; D004591:Electrophoresis, Polyacrylamide Gel; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D016877:Oxidants / Q000737:chemistry; D012697:Serine Endopeptidases / Q000737:chemistry*; D013696:Temperature
D000180:Acrylic Resins; D002364:Caseins; D003902:Detergents; D016877:Oxidants; C016680:polyacrylamide gels; D012697:Serine Endopeptidases