A fibrinolytic, alkaline and thermostable metalloprotease from the newly isolated Serratia sp RSPB11

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• 作者：P. Lakshmi Bhargavi ; R.S. Prakasham
• 关键词：Serralysin ; Serratia sp ; Purification ; Characterization ; Fibrinolysis
• 刊名：International Journal of Biological Macromolecules
• 出版年：2013
• 出版时间：October, 2013
• 年：2013
• 卷：61
• 期：Complete
• 页码：479-486
• 全文大小：1326 K

文摘

This study shows the purification and characterization of metalloprotease (serralysin) with fibrin and fibrinogenolytic property, from the newly isolated Serratia marcescens RSPB11. This protein macro molecule was more stable over a wide range of pH (6-10) and the temperatures up to 60 ¡ãC. It showed optimum enzyme activity at pH 9.0 and at a temperature of 37 ¡ãC. Inhibitory analysis revealed that this enzyme is metalloprotease and its enzyme activity could be regained by the addition of Co²⁺, Cu²⁺, Fe²⁺, Mg²⁺and Zn²⁺ ions after chelation of ions with EDTA. This enzyme showed the Michaelis-Menten's constant K_m (1.261 mg/ml) for its substrate, casein and the observed maximum attainable velocity was V_max (24,842 U/min). The purified enzyme showed an apparent molecular mass of approximately 50 kDa in SDS-PAGE. The results also suggested that this serralysin is having potential application thrombolytic therapy.