Characterization of globulin from <i>Phaseolus angularis</i> (red bean)

Abstract

Abstract Phaseolus angularis (red bean) seeds contain about 25% protein (dry basis), almost half of which is globulin. Similar to globulins from other Phaseolus species, 7S vicilin is the major fraction of red bean globulin (RBG), with 11S legumin as a minor component. The amino acid profile of RBG met or exceeded the FAO/WHO standard. Circular dichroism measurements indicate that RBG is a protein rich in α-helical and β-turn structures. RBG exhibited higher protein solubility than Supro 610, a commercial soy protein isolate, especially at acidic pHs, with minimal solubility at around pH 5.0. Compared to Supro 610, RBG had lower water hydration capacity and comparable fat binding capacity, which might be because of its lower surface hydrophobicity. RBG had higher emulsifying activity index and emulsion stability than Supro 610, but with poorer foaming properties.