Related Experiment Video
Updated: Aug 18, 2026
Purification of Hsp104, a Protein Disaggregase
Published on: September 30, 2011
Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus
Qing Huang1, Yong Peng, Xin Li
1College 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.
Abstract:
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.
