Purification and pH stability characterization of a chymotrypsin inhibitor from Schizolobium parahyba seeds

descriptionPublicationkeyboard_double_arrow_right Article 01 Apr 2004 English Publisher:Elsevier BVJournal:Phytochemistry, volume 65, pages 793-799 (issn: 0031-9422,

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Authors: Rozeni C L, Teles; Elizabeth M T, de Souza; Leonardo de A, Calderon; Sonia M, de Freitas;

doi: 10.1016/j.phytochem.2004.02.002

pmid: 15081278

Purification and pH stability characterization of a chymotrypsin inhibitor from Schizolobium parahyba seeds

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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.

Related Organizations

University of Brasília
Brazil

Keywords

Serine Proteinase Inhibitors, Thermolysin, Hydrogen-Ion Concentration, Chromatography, Ion Exchange, Substrate Specificity, Spectrometry, Fluorescence, Drug Stability, Seeds, Chymotrypsin, Electrophoresis, Polyacrylamide Gel, Rosales, Plant Proteins

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