Albumin and globulin proteins obtained after ammonium sulfate precipitation of proteins from red kidney
beans were investigated for their functional properties. Protein contents of the fractions were found to be
40 and 91.5% for albumin and globulin, respectively. Amino acid analysis showed that sulfur-containing
amino acids (cysteine and methionine) were limiting but the proteins were rich in acidic amino acids.
SDS-PAGE pattern of the globulin fraction revealed two major polypeptides (7S vicilin) with molecular weights
(MW) of ~43 and 45 kDa in addition to three minor low MW (b25 kDa) polypeptides. In contrast the albumin
had one major polypeptide with estimated MW of 27 kDa. The solubility profiles showed minimum values at
pH 4–6 for globulin but the albumin was more than 60% soluble at pH 3–9. Water holding and oil binding capacity
were, respectively, 3.4 and 2.37 mL/g for globulin, which were significantly higher (pb0.05) than the values of
2.56 and 1.87 mL/g for albumin. The least gelation concentration was 6% for globulin compared with a signifi-
cantly higher (pb0.05) 16% for albumin.