Characterization of affinity-purified trypsin from hybrid tilapia (Tilapia nilotica aurea)

Trypsin was extracted from the intestines of tilapia and purified 136-fold on the basis of amidase activity by a sequence of ammonium sulfate fractionation, acetone precipitation and affinity chromatography on soybean trypsin inhibitor bound to 4.0% beaded agarose. The purified trypsin exhibited higher esterase than amidase activity at its optimum pH of 9.0. The enzyme was stable in the range of pH 7-9. The optimum temperature for enzyme activity was 40C and the Q(10) for enzyme activity was 1.7 from 20C-30C and 30C-40C. The Arrhenius energy of activation was 8.9 and 8.7 kcal./mol respectively, for the ranges of 20C-30C and 30C-40C.