Abstract Pulses are edible seeds belonging to the leguminous family and are a rich source of proteins (21%–25%), complex carbohydrates, minerals, and vitamins. The variations in techno‐functional properties and digestibility among different pulse proteins arise from differences in molecular composition, structural organization, and albumin‐to‐globulin ratio, which ultimately determine their suitability for food applications. In the present study, proteins were isolated from four pulses (pigeon pea, cowpea, pinto bean, and navy bean) and analyzed their structural, functional, thermal properties, and in vitro protein digestibility. Compared with other proteins, pinto bean protein (PBP) exhibited broader and more intense peaks across all amide regions in the FTIR spectrum. SDS–PAGE analysis showed intense bands at 33–34 kDa and 42–47 kDa, along with minor bands at 25–27 kDa, suggesting a higher proportion of vicilin and albumin fractions. PBP demonstrated superior functional properties, including high water absorption capacity (247.57 ± 4.44%), oil absorption capacity (412.34 ± 3.11%), solubility, emulsion capacity (51.10 ± 1.17%), and foaming capacity (58.67 ± 2.73%), although its digestibility was lower compared to other pulse proteins. Owing to its enhanced hydration, emulsifying, and foaming characteristics, PBP shows strong potential for application in emulsified foods, foamed products, baked goods, and high‐protein formulations.
Kumari et al. (Sun,) studied this question.