Gelation profiles of pulse proteins: Implications of dry and wet extraction of faba and mung bean

In this study, heat-induced gelation was used as a model process to compare the functional properties of pulse protein concentrates extracted using dry fractionation, and isolates from wet fractionation. Faba bean and mung bean protein with contrasting storage protein compositions, particularly different legumin – to – vicilin ratios were examined. From molecular analysis of the protein, faba bean was identified to be rich in legumin – like protein and mung bean was high in vicilin – like proteins. Rheological temperature ramp measurements revealed isolates that exhibited lower critical gelation temperatures and stronger gel strength than concentrates. For the first time, to our knowledge, we attempted to characterise the critical gelation point of dry fractionated pulse protein, utilized Generalised Fractional Kelvin-Voigt viscoelastic solid model to elaborate viscoelasticity, and Herschel-Bulkley model to flow behaviour of the gels. Faba bean may form more weakly connected heterogeneous gel structures than mung bean. Regarding pasting profiles, concentrates underwent continuous viscosity changes compared to the isolates, owing to the presence of carbohydrates. Faba bean isolate gel strength was higher than mung bean isolate at 120°C, but at 90°C, mung bean isolate gel was firmer due to the different denaturation temperature of the dominant storage proteins; ∼80°C for vicilin and ∼100°C for legumin. Concentrates led to comparable final gel strength between the two pulses. These findings can assist to expand the potential use of pulse proteins in industrial applications such as meat analogues or bakery products for isolates or as thickening agents for concentrates.