Rodríguez-Muñoz, Adlin R.

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    Purification and kinetic characterization of trypsin from the intestine and pyloric caeca of the white grunt, Haemulon plumierii, (Lacepède, 1801)
    (2004) Rodríguez-Muñoz, Adlin R.; Uscian, John M.; College of Arts and Sciences - Sciences; Navas, Vivian; Bunkley-Williams, Lucy; Department of Biology; Kubaryk, John
    Trypsin is one of several animal digestive proteases whose activities collectively breakdown ingested proteins to facilitate gut amino acid absorption. The goals of this research were to purify and characterize trypsin from intestinal and pyloric caecal tissues of white grunt, Haemulon plumierii (Lacepède, 1801). Trypsin was purified 11-fold from intestinal and pyloric caecal tissues of the white grunt, through the sequential application of ammoniun sulfate fractionation, size exclusion chromatography, and affinity chromatography. The enzyme displayed optimal activity at pH 8 and 40 oC. It was completely inhibited by the presence of soybean trypsin inhibitor at a concentration of 100 %. SDS-PAGE analysis of the purified enzyme revealed a single band with an estimated molecular weight of 24 kDa. This white grunt trypsin was similar to those from other fishes in terms of its molecular weight, kinetic properties, and response to the presence of soybean Trypsin is one of several animal digestive proteases whose activities collectively breakdown ingested proteins to facilitate gut amino acid absorption. The goals of this research were to purify and characterize trypsin from intestinal and pyloric caecal tissues of white grunt, Haemulon plumierii (Lacepède, 1801). Trypsin was purified 11-fold from intestinal and pyloric caecal tissues of the white grunt, through the sequential application of ammoniun sulfate fractionation, size exclusion chromatography, and affinity chromatography. The enzyme displayed optimal activity at pH 8 and 40 oC. It was completely inhibited by the presence of soybean trypsin inhibitor at a concentration of 100 %. SDS-PAGE analysis of the purified enzyme revealed a single band with an estimated molecular weight of 24 kDa. This white grunt trypsin was similar to those from other fishes in terms of its molecular weight, kinetic properties, and response to the presence of soybean trypsin inhibitor.