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Structural, physicochemical, and functional properties of white and blue lupin vicilin and legumin fractions
Stanley Chukwuejim1, Deepak Kadam1, Rotimi E Aluko1,2
1Department of Food and Human Nutritional Sciences, University of Manitoba, Winnipeg, Manitoba R3T 2N2, Canada.
Abstract:
The aim of this study was to isolate the vicilin and legumin protein fractions of lupin seeds and determine their physicochemical and functional properties. White lupin vicilin (WLVL) exhibited a significantly higher methionine + cysteine content (2.92 g/100 g protein) than the legumin fractions, with a corresponding amino acid score of 127 %. Blue lupin vicilin (BLVL) exhibited high surface hydrophobicity (459.12), whereas the blue lupin legumin (BLLEG) fraction had a high least gelation concentration (18 %). All fractions exhibited U-shaped solubility curves, with minimum values at pH 5, while BLLEG showed superior in vitro protein digestibility (87.47 %). BLVL demonstrated high emulsifying properties across all pH values, maintaining small droplet sizes (7-9 μm) and high stability (95-100 %). BLVL also exhibited superior foaming capacity (75-85 %), whereas WLVL showed excellent foam stability (65-80 %). These findings revealed significant species-specific and fraction-specific differences in lupin globulins, with BLVL emerging as a promising ingredient for food applications.
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