Asian Journal of Microbiology, Biotechnology & Environmental Sciences Paper

Vol 8, Issue 3, 2006; Page No.(615-616)

EXTRACTION OF SERINE PROTEASE FROM PERIONYX EXCAVATUS

S. SUBHATRA, A. GNANAMANI AND A. MARY VIOLET CHRISY

Abstract

Proteolytic enzymes or proteases catalyze the cleavage of peptide bonds in proteins. Peptide bond cleavage is one of the most frequent enzymatic modifications of proteins. Recent studies of proteolytic enzymes have focused on the regulatory roles in the variety of physiological processes. Serine proteases are characterized by the presence of a serine group in their active site. Earthworms secrete proteases which degrade casein, gelatin, fibrin and the lyphoilized powder of earthworms have long been used for antipyretic and diuretic purpose. So in the present research programme it has been planned to extract the enzyme serine protease and analyze their fibrinolytic activity, molecular weight and zymogram activity from perionyx excavatus. The maximum fibrinolytic activity of the serine protease was observed in the zone of lysis. The molecular weight determination was in the range between 23-35kDa. Further confirmation by zyrnogram using two types of substrates (Bovine serum albumin and casein) substantiates the purity of the enzyme extracted.

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