Rai Sudhir K, Mukherjee Ashis K
Department of Molecular Biology and Biotechnology, Tezpur University, Tezpur 784 028, Assam, India.
Bioresour Technol. 2009 May;100(9):2642-5. doi: 10.1016/j.biortech.2008.11.042. Epub 2009 Jan 10.
An organic solvent stable, alkaline serine protease (Bsubap-I) with molecular mass of 33.1 kDa, purified from Bacillus subtilis DM-04 showed optimum activity at temperature and pH range of 37-45 degrees C and 10.0-10.5, respectively. The enzyme activity of Bsubap-I was significantly enhanced in presence of Fe(2+). The thermal resistance and stability and of Bsubap-I in presence of surfactants, detergents, and organic solvents, and its dehairing activity supported its candidature for application in laundry detergent formulations, ultrafiltration membrane cleaning, peptide synthesis and in leather industry. The broad substrate specificity and differential antibacterial property of Bsubap-I suggested the natural ecological role of this enzyme for the producing bacterium.
从枯草芽孢杆菌DM - 04中纯化得到一种分子量为33.1 kDa的有机溶剂稳定型碱性丝氨酸蛋白酶（Bsubap - I），其在温度37 - 45℃和pH值10.0 - 10.5范围内分别表现出最佳活性。在Fe(2+)存在时，Bsubap - I的酶活性显著增强。Bsubap - I在表面活性剂、洗涤剂和有机溶剂存在下的耐热性和稳定性及其脱毛活性，支持了其在洗衣粉配方、超滤膜清洗、肽合成及皮革工业中的应用候选资格。Bsubap - I广泛的底物特异性和不同的抗菌特性表明了该酶对产生菌的自然生态作用。
