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• W2044514976 abstract "Trypsin from viscera of Indian mackerel (Rastralliger kanagurta) was purified by ammonium sulphate precipitation and chromatographic techniques such as size exclusion, ion exchange, and affinity chromatography, with a 14.4-fold increase in specific activity and 18.7% recovery. The molecular weight of the trypsin was estimated to be approximately 26 kDa using sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE). Purified trypsin showed amidase-specific activity which was determined using benzoyl-dl-arginine-p-nitroanilide (BAPNA). The optimum pH and temperature for isolated trypsin activity were 9.0 and 50°C, respectively. The purified trypsin was strongly inhibited by soybean trypsin inhibitor (SBTI) and N-p-tosyl-1-lysine chloromethyl ketone (TLCK). Purified trypsin showed almost 40% recovery at high NaCl concentration (30%). The N-terminal amino acid sequence of the first 10 amino acids of purified trypsin was IVGGYESQPH. The Michaelis-Menten constant (Km) and catalytic constant (Kcat) of purified trypsin were 0.430 mM and 0.77 s−1, respectively, determined using BAPNA as a substrate. Purified trypsin showed digestion of casein similar to bovine trypsin by the fluorometric method." @default.
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• W2044514976 date "2013-12-18" @default.
• W2044514976 modified "2023-10-14" @default.
• W2044514976 title "Isolation, Purification, and Biochemical Characterization of Trypsin from Indian Mackerel (<i>Rastralliger kanagurta</i>)" @default.
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• W2044514976 doi "https://doi.org/10.1080/10498850.2013.777864" @default.
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