Abstract

Faba bean (high- and low-tannin) protein isolates were water extracted followed by dialysis or micellization in comparison to concentrates from conventional alkali extraction + acid precipitation, and salt-based extraction (1% NaCl) + dialysis. Protein fractions were characterised for secondary structure conformational changes, crystalline structure, particle size distribution in aqueous suspension and thermal properties. Mild water or salt extraction did not influence particle size distribution. Based on XRD, FTIR and CD, β-sheet structures were the most abundant secondary structures and water extraction + dialysis had minimal impact on their native conformation. DSC results showed an association between protein purity, glass transition temperature and endothermic enthalpy. High melting temperature above glass transition confirms the suitability of faba bean proteins for thermal/extrusion processing. Fractionation method was a more significant determinant of physicochemical characteristics compared to the cultivar. Further exploration of the techno-functional characteristics of faba bean proteins is essential for value-added food applications.

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