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|Title:||Some properties of the intestinal proteases of the rabbitfish, Siganus canaliculatus (Park)|
|Authors:||Sabapathy, U. |
|Source:||Sabapathy, U., Teo, L.-H. (1995-06). Some properties of the intestinal proteases of the rabbitfish, Siganus canaliculatus (Park). Fish Physiology and Biochemistry 14 (3) : 215-221. ScholarBank@NUS Repository. https://doi.org/10.1007/BF00004312|
|Abstract:||Some properties of the intestinal proteases of the rabbitfish were examined. At 25°C, both trypsin and chymotrypsin showed pH optima of 8.0. Leucine aminopeptidase, however, displayed maximum activity in the pH range, 7.0-9.0. Leucine aminopeptidase had the highest optimum temperature (60°C), and chymotrypsin, the lowest (30°C). The optimum temperature of trypsin was 55°C. The activation energy, Ea, was found to be 8.24 for trypsin and 8.50 kcal mol-1 for chymotrypsin. The Ea for leucine aminopeptidase was 6.29 kcal mol-1 above 40°C and 1.73 kcal mol-1 below 40°C. Substrate concentration-velocity plots showed that all three enzymes followed Michaelis-Menten kinetics; the Km and Vmax were estimated for the three enzymes. The effects of various protease inhibitors on enzyme activity were also examined and confirmed the protease classes to which each enzyme belonged. The three proteases examined have similar properties to proteases in other fishes. © 1995 Kugler Publications.|
|Source Title:||Fish Physiology and Biochemistry|
|Appears in Collections:||Staff Publications|
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