Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus

被引：115

作者：

Huang, Q ^{[1
]}

Peng, Y ^{[1
]}

Li, X ^{[1
]}

Wang, HF ^{[1
]}

Zhang, YZ ^{[1
]}

机构：

[1] Sichuan Univ, Sichuan Key Lab Mol Biol Biotechnol, Coll Life Sci, Ctr Green Chem & Technol, Chengdu 610064, Peoples R China

来源：

CURRENT MICROBIOLOGY | 2003年 / 46卷 / 03期

关键词：

D O I：

10.1007/s00284-002-3850-2

中图分类号：

Q93 [微生物学];

学科分类号：

071005 ; 100705 ;

摘要：

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 55degreesC; 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.

引用

页码：169 / 173

页数：5

共 16 条

[1] Sequence of the gene encoding an alkaline serine proteinase of Bacillus pumilus TYO-67 [J].