Studies on proteolytic activity in the midgut homogenate of the blowfly Chrysomia chloropyga (Wied.) (Diptera: Calliphoridae)

Abstract

Hydrolysis of the substrate Hide Powder Azure was accelerated by increasing concentration of the midgut enzyme extract of Chrysomyia chloropyga. A linear relationship between proteolytic activity and substrate concentration was established. Optimum temperature of substrate hydrolysis at pH 7.9 was shown to be 400C and activity at different temperatures and at various incubation periods did not alter the optimum. At the pH range (3 to 11) and at temperatures of 350, 450 and 550C, the pH activity of the enzyme extract showed two peaks, a low peak at pH 5 and a high one at pH 8. The crude enzyme extract was resolved into six protein ‘bands by polyacrylamide gel electrophoresis. The partially-purified proteolytic fractions hydrolysed N -p- Tosyl-L-arginine methylester (TAME) and N-Benzoyl-L-tyrosine ethylester (BTEE) at pH 8.0. Trypsin and Chymotrypsin were demonstrated in the enzyme preparation