Parallel comparison of functional and physicochemical properties of common pulse proteins

The demand for more functional plant-based proteins has greatly increased. objective of this study was to provide a systematic understanding the properties and physicochemical features protein isolates extracted from common pulses. Chickpea (ChPI) much less soluble compared other proteins. Pigeon pea (PiPI) lab soybean (SPI) possessed excellent emulsification capacity stability 0.71–0.73 0.70–0.71 cm/cm, respectively. Most had foaming capacities greater than 1.20 mL/mL, except ChPI. Lentil (LPI-W), protein, PiPI showed water absorption 4.9, 3.5, 3.6 g/g good oil capacity. greatest gelation capacity, with least concentration 80 g/L. ChPI higher thermal denaturation peak temperature (169 °C) (145–154 °C). Commercial SPI SPI, which due intensive during commercial processing. amino acid profiles, SDS-PAGE patterns, secondary structure composition, relative surface hydrophobicity were analyzed help elucidate features. This provides useful information in selecting appropriate sources achieve desirable applications.