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Purification and partial characterization of chickpea 2S albumin
J Vioque1, R Sánchez-Vioque, A Clemente
1Instituto de la Grasa, Avenida Padre García Tejero 4, Sevilla, Spain.
Abstract:
A chickpea 2S albumin has been purified by solubilization in 60% methanol and ion-exchange chromatography. Under denaturing conditions it is composed of two peptides of 10 and 12 kDa. Native molecular mass determined by gel filtration chromatography is 20 kDa. Amino acid composition shows that it is rich in sulfur amino acids, mainly cysteine with 4.6% of the total. On the other hand, it has antinutritional characteristics of being allergenic for chickpea-sensitive individuals and inhibitory against porcine chymotrypsin with a lesser degree toward trypsin. The results of interest from a nutritional point of view are discussed.