Mg. Elshemy et Re. Levin, CHARACTERIZATION OF AFFINITY-PURIFIED TRYPSIN FROM HYBRID TILAPIA (TILAPIA-NILOTICA AUREA), Journal of food biochemistry, 21(2), 1997, pp. 163-175
Trypsin was extracted from the intestines of tilapia and purified 136-
fold on the basis of amidase activity by a sequence of ammonium sulfat
e fractionation, acetone precipitation and affinity chromatography on
soybean trypsin inhibitor bound to 4.0% beaded agarose. The purified t
rypsin 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 t
emperature for enzyme activity was 40C and the Q(10) for enzyme activi
ty was 1.7 from 20C-30C and 30C-40C. The Arrhenius energy of activatio
n was 8.9 and 8.7 kcal./mol respectively, for the ranges of 20C-30C an
d 30C-40C.