title: A fibrinolytic, alkaline and thermostable metalloprotease from the newly isolated Serratia sp RSPB11.
abstract: 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 °C. It showed optimum enzyme activity at pH 9.0 and at a temperature of 37 °C. Inhibitory analysis revealed that this enzyme is metalloprotease and its enzyme activity could be regained by the addition of Co(2+), Cu(2+), Fe(2+), Mg(2+)and Zn(2+) ions after chelation of ions with EDTA. This enzyme showed the Michaelis-Menten's constant Km (1.261 mg/ml) for its substrate, casein and the observed maximum attainable velocity was Vmax (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.
authors.affiliation: Bioengineering and Environmental Centre, Indian Institute of Chemical Technology, Tarnaka, Hyderabad 500607, India.
authors.forename: P
authors.initials: P
authors.lastname: Lakshmi Bhargavi
authors.forename: R S
authors.initials: RS
authors.lastname: Prakasham
mesh_terms: D004789:Enzyme Activation / Q000187:drug effects; D004795:Enzyme Stability; D005337:Fibrin / Q000737:chemistry; D006863:Hydrogen-Ion Concentration; D007477:Ions / Q000737:chemistry; D007700:Kinetics; D008666:Metalloendopeptidases / Q000737:chemistry; D045726:Metalloproteases / Q000737:chemistry* / Q000302:isolation & purification; D008670:Metals / Q000737:chemistry; D011480:Protease Inhibitors / Q000494:pharmacology; D012705:Serratia / Q000737:chemistry* / Q000201:enzymology; D013696:Temperature
chemical_list: D007477:Ions; D008670:Metals; D011480:Protease Inhibitors; D005337:Fibrin; D045726:Metalloproteases; D008666:Metalloendopeptidases; C095666:serralysin
keywords: Characterization; Fibrinolysis; Purification; Serralysin; Serratia sp