Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus.
An extracellular alkaline serine protease (called DHAP), produced by a Bacillus pumilus strain, demonstrates significant dehairing function. This protease is purified by hydrophobic interaction chromatography, ion exchange, and gel filtration. DHAP had a pI of 9.0 and a molecular weight of approximately 32,000 Dalton. It shows maximal activity at pH 10 and with a temperature of 55 degrees C; the enzyme activity can be completely inhibited by phenylmethylsulfonyl fluoride (PMSF) and diisopropyl fluorophosphates (DFP). The first 20 amino acid residues of the purified DHAP have been determined with a sequence of AQTVPYGIPQIKAPAVHAQG. Alignment of this sequence with other alkaline protease demonstrates its high homology with protease from another B. pumilus strain.
Huang
Qing
Q
College of Life Science, Center for Green Chemistry and Technology, Sichuan University, Sichuan Key Laboratory of Molecular Biology and Biotechnology, Chengdu 610064, People's Republic of China.
Peng
Yong
Y
Li
Xin
X
Wang
Haifeng
H
Zhang
Yizheng
Y
D000595:Amino Acid Sequence; D001407:Bacillus / Q000145:classification / Q000201:enzymology*; D006863:Hydrogen-Ion Concentration; D007477:Ions / Q000378:metabolism; D007526:Isoelectric Point; D007700:Kinetics; D008969:Molecular Sequence Data; D008970:Molecular Weight; D011480:Protease Inhibitors / Q000378:metabolism; D017385:Sequence Homology; D012697:Serine Endopeptidases / Q000737:chemistry* / Q000302:isolation & purification* / Q000378:metabolism; D013696:Temperature
D007477:Ions; D011480:Protease Inhibitors; D012697:Serine Endopeptidases; C032923:microbial serine proteinases