Abstract
Production characterization of serratiopeptidase (STP) enzyme by Serratia marcescens was the aim of this study. Serratia marcescens was allowed to grow in Tryptone Yeast Extract Glucose broth culture for the purpose of inducing STP (serrapeptase or serratiopeptidase) enzyme. The optimal conditions for STP production by Serratia marcescens were; 0.5 % substrate(Gelatin) concentration; 24 h incubation period; 32ºC incubation temperature and 6.0 pH ; the best buffer for production of STP enzyme was phosphate buffer. The best broth ingredient was tryptone; An optimum carbon sources was glucose; an optimum nitrogen source for STP enzyme production was tryptone; Valine was the best amino acids for the production of STP enzyme; the utilization of organic acids, acetic, citric, lactic acid decreased STP enzyme production at different concentrations above 3.0%. The STP enzyme was partially purified by ammonium sulfate precipitation and dialysis. The enzyme was found to have 52 KDa molecular weight by SDS – PAGE analysis. The STP enzyme activity increased as the increase in enzyme concentration. The data obtained emphasizes the possibility of production and purification of the microbial STP enzyme for application under industrial scale.
Highlights
The proteolytic enzymes in common use today is derived from bacteria, plants, and animal sources
The gelatin clearing zone (GCZ) exhibited by the STP produced from Serratia marcescens showed maximum STP enzyme production with a clearing zone of 36mm at an incubation period of 24 h (Table 1.0)
The present study indicated that the optimum incubation period for STP production was 24 h (Table 1.0)
Summary
The proteolytic enzymes in common use today is derived from bacteria (serrapeptase grown from Serratia marcescens cultures), plants (bromelain from pineapple stem and papain from papaya), and animal sources (trypsin and chymotrypsin from hogs or cattle). They’re all generally useful, but for many applications serrapeptase appears to be the most useful of them all. Serrapeptase was compared to trypsin, chymotrypsin, and pronase (another microbial peptidase) in a rat model of scalding, which is known to induce abnormal activation of fibrinolysis. Serrapeptase was far more effective than any other enzyme in repressing fibrinolysis in this model, in agreement with its documented clinical efficacy as an anti-inflammatory agent (Braun and Sutherland, 2003). Serratiopeptidase is a proteolytic enzyme available for clinical use more than a decade. The knowledge of production, purification and characterization of serratiopeptidase is very important for improvising the activity and the commercial value of the enzyme
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