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Solubility−Digestibility Relationship of Legume Proteins
216
Citations
22
References
1997
Year
NutritionEngineeringFood AnalysisFood BiophysicsProtein PurificationFood ChemistryLegume ProteinsProtein FoldingBioanalysisLegume ScienceProtein SolubilityChromatographyProtein ChemistryFood CompositionBiochemistryIn Vitro FermentationAlternative Protein SourceDry BeanBiomolecular EngineeringSeed StorageSolubility−digestibility RelationshipMedicinePlant FoodsSeed Processing
They measured the solubility of raw and cooked faba bean, lentil, chickpea, and dry bean proteins across pH 1–13 in water and NaCl. Solubility in water rises on both sides of pH 4, but cooking reduces solubility up to pH 10; only raw dry bean solubility improves in NaCl; the soluble fraction after cooking is enriched in charged residues and low in hydrophobic amino acids, high‑molecular‑weight peaks in raw faba bean and lentil suggest stronger association, and cooking does not enhance digestibility of faba bean and lentil, indicating that basic residues stabilize heat‑induced aggregates and limit digestibility. Keywords: legumes, globulins, solubility, digestibility.
Protein solubility of raw and cooked faba bean, lentil, chickpea, and dry bean was tested in water and in NaCl in the pH range 1.0−13.0. The solubility of all legume proteins in water typically increased on both sides of pH 4.0. In NaCl, only solubility of raw dry bean proteins was improved. A marked reduction in protein solubility was observed after cooking of all legumes up to pH 10.0, where solubilization occurred, suggesting that it was dependent on deprotonation of lysine and arginine. Amino acid analysis showed that the protein fraction that retained solubility in water (pH 6.5) after cooking had a high amount of arginine and glutamic acid, low levels of hydrophobic amino acids, and, therefore, a much higher charge density than proteins in the whole flour. The SE-HPLC profiles indicated that water-soluble raw faba bean and lentil had main protein peaks of a higher molecular weight than those of dry bean or chickpea, thus suggesting a higher trend toward association. In vitro protein digestibility of faba bean and lentil, unlike that of chickpea and dry bean, was not improved upon cooking. The results indicate that, in addition to hydrophobic forces, basic residues are involved in the stabilization of heat-induced aggregates of legume proteins, possibly contributing to their low digestibility. Keywords: Legumes; globulins; solubility; digestibility
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