Physicochemical properties and gelling behaviour of Bambara groundnut protein isolates and protein-enriched fractions.

Plant proteins, and specifically those from legume crops, are increasingly recognised as sustainable and functional food ingredients. In this study, we expand on the knowledge of Bambara groundnut (Vigna subterranea (L.) Verdc.) [BGN] proteins, by characterising the composition, microstructure and rheological properties of BGN protein isolates obtained via wet extraction and protein-enriched fractions obtained via dry fractionation. The BGN protein isolates were compared in the context of the major storage protein, vicilin, as previously identified. Molecular weight analysis performed with gel electrophoresis and size-exclusion chromatography coupled to light-scattering, revealed some major bands (190 kDa) and elution patterns with molecular weights (205.6-274.1 kDa) corresponding to that of BGN vicilin, whilst the thermal denaturation temperature (Tp 91.1 °C, pH 7) of BGN protein isolates also coincided to that of the vicilin fraction. Furthermore, the concentration dependence of the elastic modulus G' of the BGN protein isolates, closely resembled that of BGN vicilin (both upon NaCl addition); suggesting that vicilin is the main component responsible for gelation. Confocal laser scanning and scanning electron micrographs revealed inhomogeneous aggregate structures, which implies that fractal scaling were better suited for description of the BGN protein isolate gel networks. Concerning the BGN protein-enriched fractions, both rotor and impact milling with air jet sieving and air classification, respectively, were successfully applied to separate these fractions from those high in starch; as evident from compositional analysis, particle size distributions and microscopic imaging. When considering sustainability aspects, dry fractionation could thus be a viable alternative for producing BGN protein-enriched fractions.