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Purification and pH stability characterization of a chymotrypsin inhibitor from Schizolobium parahyba seeds
Rozeni C L Teles1, Elizabeth M T de Souza, Leonardo de A Calderon
1Universidade de Brasília, Depto de Biologia Celular, Laboratório de Biofísica, Campus Universitário Darcy Ribeiro, Asa norte. 70910-900, Brasília, DF, Brazil.
Abstract:
Schizolobium parahyba chymotrypsin inhibitor (SPCI) was completely purified as a single polypeptide chain with two disulfide bonds, by TCA precipitation and ion exchange chromatography. This purification method is faster and more efficient than that previously reported: SPCI is stable from pH 2 to 12 at 25 degrees C, and is highly specific for chymotrypsin at pH 7-12. It weakly inhibits elastase and has no significant inhibitory effect against trypsin and alpha-amylase. SPCI is a thermostable protein and resists thermolysin digestion up to 70 degrees C.
