Characterization of Partial Purified Trypsin and Chymotrypsin from Viscera of Nile Tilapia (Oreochromis niloticus Linneaus)
Keywords:
tilapia, Oreochromis niloticus, protease, trypsin, chymotrypsinAbstract
The tryptic and chymotryptic activities of extraction of spleen, liver, stomach, intestine and mixed viscera of Nile tilapia (Oreochromis niloticus Linneaus) were compared. Intestine was the best sources for trypsin and chymotrypsin. Trypsin and chymotrypsin fractions were extracted from intestine of Nile tilapia by 30-70% saturated ammonium sulfate precipitation, dialyzed, acetone precipitation and separated by SBTI affinity chromatography column. Specific activities of trypsin and chymotrypsin were 0.529 and 0.380 unit/mg protein, respectively. The purities of trypsin and chymotrypsin fraction were increased by 5.56 and 3.62 folds, respectively. The optimum temperature and pH of trypsin fraction were 80°C and pH 9.0. The optimum temperature and pH of chymotrypsin fraction were 60°C and pH 9.0. Trypsin fraction was stable at 0-60°C and chymotrypsin was stable at 0-50°C for 30 min at pH 8.0.
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online 2452-316X print 2468-1458/Copyright © 2022. This is an open access article under the CC BY-NC-ND license (http://creativecommons.org/licenses/by-nc-nd/4.0/),
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