COMPARATIVE STUDY ON ENZYMATIC CHARACTERISTICS OF TRYPSINS FROM THE PYLORIC CECA OF YELLOW TAIL (SERIOLA QUINQUERADIATA)

Trypsins from the pyloric ceca of two fish species, yellow tail (Seriola quinqueradiata) and brown hakeling (Physiculus japonicus) were purified by a series of chromatographic separations. Purity increased 63- and 106-fold with approximately 55 and 10 % yield for yellow tail trypsin and brown hakeling trypsin, respectively. Final enzyme preparations were homogeneous in sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and the molecular weights of both enzymes were estimated to be 24 kDa by SDS-PAGE. Yellow tail and brown hakeling trypsins had maximal activity at pH 8.0 for hydrolysis of TAME and was unstable at acidic pH. The optimum temperatures for yellow tail and brown hakeling trypsins were 60 C and 50 C, respectively. Yellow tail trypsin was stable up to 50 C, whereas brown hakeling was stable up to 40 C. Both trypsins wer