Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus
Purification and characterization of an extracellular alkaline serine protease with dehairing function from Bacillus pumilus
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DOI：
10.1007/s00284-002-3850-2
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发表时间：
2003-03-01
影响因子：
2.6
通讯作者：
Zhang, YZ
中科院分区：
文献类型：
--
作者：
Huang, Q;Peng, Y;Zhang, YZ
由短小芽孢杆菌菌株产生的胞外碱性丝氨酸蛋白酶（称为 DHAP）具有显着的脱毛功能。该蛋白酶通过疏水相互作用层析、离子交换和凝胶过滤纯化。 DHAP 的等电点为 9.0，分子量约为 32,000 道尔顿。在pH 10和温度55℃时显示最大活性；苯甲基磺酰氟（PMSF）和氟磷酸二异丙酯（DFP）可完全抑制酶活性。纯化的 DHAP 的前 20 个氨基酸残基已用 AQTVPYGIPQIKAPAVHAQG 序列确定。该序列与其他碱性蛋白酶的比对表明其与另一种短短芽孢杆菌菌株的蛋白酶具有高度同源性。
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.