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- W2067854940 abstract "Proteinases from the hepatopancreas of freshwater crab Barytelphusa cunicularis were characterized with respect to their biochemical properties. Serine protease activities corresponding to trypsin and chymotrypsin were detected. A total of eight proteinase activity bands were detected in hepatopancreatic extract on X- ray film. Synthetic substrate and inhibitor studies revealed the presence of trypsin, chymotrypsin, and aminopeptidase like proteinases. Of total proteinase activity, chymotrypsin-like activity was found to be the highest. PMSF and TPCK had the highest proteinase inhibitory activity. Molecular weights of identified enzymes ranged between 7.5 kDa and 19 kDa. The pH and temperature optima for the enzyme activity were about pH 6.5 and 70° C. CHPs (Crab hepatopancreatic proteinases) retained up to 90% activity at high metal ion concentrations. Our results suggest that the presence of several CHP bands, and their activity with high temperature, metal ions and over a broad range of pH could be important when considering these enzymes as biotechnological reagents. Proteinases from B. cunicularis also have potential use in food industries for developing functional peptides." @default.
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- W2067854940 date "2011-02-16" @default.
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- W2067854940 title "Characterization and Applicability of Digestive Proteinases from Hepatopancreas ofBarytelphusa cunicularis" @default.
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- W2067854940 doi "https://doi.org/10.1080/08905436.2011.547111" @default.
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