ArticleJournal of food science2025
Structures, antioxidant, and angiotensin I-converting enzyme (ACE)-inhibitory activities of peptides derived from protein hydrolysates of three phenolics-rich legume genera.
Article in Journal of food science, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 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
3 citing papers in PubMed.
- Plant Protein-Derived Bioactive Peptides: From Mechanistic Promise to Health-Promoting Functional Foods.Nutrients · 2026Review
- Recent Approaches for Bioactive Peptides Production from Pulses and Pseudocereals.Molecules (Basel, Switzerland) · 2025Review
- Comparative Study on Structural, Functional, and Biological Properties of Enzymatic Protein Hydrolysates from Different Legumes Native to Vietnam.Applied biochemistry and biotechnology · 2025Article
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Authors and funding
3 authors.
Funding
Abstract
Lentil, black soybean, and black turtle bean are rich in phenolic antioxidants but belong to different scientific genera with different protein structures. This study's objective was to compare the characteristics of peptides derived from the protein hydrolysates of these legumes. Proteins were isolated, cooked, and subjected to in vitro digestion with pepsin, trypsin, and chymotrypsin. Hydrolyzed peptides were fractionated by ultrafiltration (UF), anion-exchange chromatography, and gel-permeation chromatography (GPC). GPC-eluted peptides of <3 kDa with high angiotensin I-converting enzyme (ACE)-inhibitory activities were sequenced. Antioxidant profiles of peptides from the three legumes analyzed by five methods did not follow the same activity patterns associated with the decreases in peptide's molecular size. Among the UF fractions, the <3 kDa fraction had the highest ACE-inhibition with approximately 45%, 42%, and 39% at 100 µg/mL. Stepwise purifications of the hydrolysates enhanced the ACE-inhibitory capacity (IC
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