ArticleFood chemistry: X2025
Structural, physicochemical, and functional properties of white and blue lupin vicilin and legumin fractions.
Article in Food chemistry: X, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
2 citing papers in PubMed.
- Protein digestibility and bioactive potential of commercial plant-based meat analogues.Food chemistry: X · 2026Article
- Effect of Particle Size on the Physicochemical and Functional Properties of Sweet Lupin (Foods (Basel, Switzerland) · 2026Article
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Authors and funding
3 authors.
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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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