Abstract
Serralysin is a type of metalloprotease originally isolated from digestive system of silkworm. This research shows the purification and characterization of metalloprotease (serralysin) extracted from Serratiaspisolated from soil. Out of 5 soilsamples collected, only one potent strain was observed to be an effective producer of fibrinolytic enzyme which was screened by heated plasma and skim milk agar plate assay. This species was found to have better growth in tryptosesoybroth agar and the color production of Serratia was also improved in tryptose soy agar at pH of 7. The purified enzyme demonstrated a zone of hydrolysis on heated plasma plate. 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. The purified enzyme showed an apparent molecular mass of approximately 50 kDa in SDS-PAGE. The study also suggested that this serralysin is having potential application towards thrombolytic therapy.
Published Version
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