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CHARACTERIZATION OF AFFINITY‐PURIFIED TRYPSIN FROM HYBRID TILAPIA (TILAPIA NILOTICA/AUREA)
Author(s) -
ELSHEMY M.G.,
LEVIN R.E.
Publication year - 1997
Publication title -
journal of food biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.507
H-Index - 47
eISSN - 1745-4514
pISSN - 0145-8884
DOI - 10.1111/j.1745-4514.1997.tb00221.x
Subject(s) - benzamidine , ammonium sulfate precipitation , chemistry , chromatography , trypsin , affinity chromatography , enzyme , esterase , ammonium sulfate , enzyme assay , acetone , biochemistry , size exclusion chromatography
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.