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Comparative Study on Structural, Functional, and Biological Properties of Enzymatic Protein Hydrolysates from Different Legumes Native to Vietnam. | LitMetric

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Article Abstract

The growing demand for plant-based proteins reflects a consumer shift toward healthier and more sustainable lifestyles. Among these, hydrolyzed proteins have garnered attention due to their enhanced functional properties and biological activities compared to crude proteins. This study investigated the impact of enzymatic hydrolysis using Alcalase on the functional, technological, and biological properties of proteins derived from various beans, including yellow bean (Vigna radiata L.), hyacinth bean (Lablab purpureus L.), and lima bean (Phaseolus lunatus L.). The protein hydrolysates were assessed based on antioxidant activities (measured via ABTS radical scavenging and FRAP assays), foaming capacity, SDS-PAGE analysis, cytotoxicity, and anti-inflammatory properties. The results showed that the antioxidant activity of the protein hydrolysates significantly improved compared to the unhydrolyzed proteins, with hyacinth bean hydrolysates exhibiting the highest antioxidant activities, including ABTS radical scavenging activity (754.85 mg TE/L) and ferric reducing antioxidant power (80.35 mg TE/L). Meanwhile, yellow bean protein exhibited the highest degree of hydrolysis (81.38%) among the tested legumes and enzymatic hydrolysis significantly enhanced the foaming properties of yellow bean protein hydrolysates. SDS-PAGE analysis revealed that hydrolysis degraded plant-derived proteins into low-molecular-weight peptides (approximately 15-45 kDa). Additionally, the protein hydrolysates showed no cytotoxicity at concentrations below 2000 μg/mL. Legume protein hydrolysates hold significant future prospects in their promising potential as multifunctional ingredients exhibiting strong antioxidant and functional activities, which can be harnessed to develop sustainable, health-promoting food products and nutraceuticals.

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http://dx.doi.org/10.1007/s12010-025-05342-wDOI Listing

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