Fava bean (Vicia faba L.) is a promising source of proteins and has a potential in industrial food applications. Processing of fava ingredients modifies proteins and their functional properties. This study established the complexity of the relationship between fava protein-associated reactions (protein hydrolysis and aggregation), physico-chemical properties (electric charge, solubility, and intrinsic fluorescence, thermal integrity) and functional properties (foam and emulsion). For this study, an air-classified fava protein concentrate (65% w/w protein d. B.) was processed using pH (2, 4, 6.4 and 11), temperature (55, 75 and 95°C) and duration of treatment (30 and 360 min) to produce 36 modified fava concentrates. Processing resulted in protein hydrolysis at pH < 4, and protein aggregation at pH ≥ 6.4 at temperatures above 75°C, which influenced foaming and emulsification distinctly owing to the differences in their stabilizing mechanisms. Despite these modifications, their physico-chemical and functional properties were primarily governed by...

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