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Summary Defatted lentil seed flour proteins were separated into their constituent albumin (ALB), globulin (GLB) and glutelin (GLT) fractions followed by determination of their structural and functional properties. The GLB fraction demonstrated superior solubility (84%–100%) at acidic and alkaline pH values when compared to the lower values for ALB and GLT. Amino acid composition analysis showed lower contents of hydrophobic and sulphur‐containing residues for GLB. However, GLB had the highest in vitro protein digestibility, which may be due to lower contents of rigid secondary structure fractions like the β‐sheet and β‐turns. In contrast, water and oil holding capacities as well as gelling ability were better for GLT and ALB than GLB. The GLT fraction formed very poor emulsions at pH 3 and 5 but emulsification was significantly (p < 0.05) improved (smaller oil droplets) at pH 7 and 9. Foaming capacity was strongest for GLB, especially at pH 5, 7 and 9 where increase in protein concentration had a negative effect on foam formation. Overall, the protein type and pH of the environment had stronger effects on emulsion and foaming properties than the protein concentration.
Osemwota et al. (Fri,) studied this question.