Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
10764701 | Biochemical and Biophysical Research Communications | 2010 | 7 Pages |
Abstract
An enzyme was purified from the pyloric caecum of tambaqui (Colossoma macropomum) through heat treatment, ammonium sulfate fractionation, Sephadex® G-75 and p-aminobenzamidine-agarose affinity chromatography. The enzyme had a molecular mass of 23.9 kDa, NH2-terminal amino acid sequence of IVGGYECKAHSQPHVSLNI and substrate specificity for arginine at P1, efficiently hydrolizing substrates with leucine and lysine at P2 and serine and arginine at P1â². Using the substrate z-FR-MCA, the enzyme exhibited greatest activity at pH 9.0 and 50 °C, whereas, with BAPNA activity was higher in a pH range of 7.5-11.5 and at 70 °C. Moreover, the enzyme maintained ca. 60% of its activity after incubated for 3 h at 60 °C. The enzymatic activity significantly decreased in the presence of TLCK, benzamidine (trypsin inhibitors) and PMSF (serine protease inhibitor). This source of trypsin may be an attractive alternative for the detergent and food industry.
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Authors
Marina Marcuschi, Talita S. Espósito, MaurÃcio F.M. Machado, Izaura Y. Hirata, Marcelo F.M. Machado, Márcia V. Silva, Luiz B. Jr., Vitor Oliveira, Ranilson S. Bezerra,