ArticleFoods (Basel, Switzerland)2019
Enzymatic Pea Protein Hydrolysates Are Active Trypsin and Chymotrypsin Inhibitors.
Article in Foods (Basel, Switzerland), 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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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.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
6 citing papers in PubMed, 39 citations in OpenAlex.
- Peptidomics-guided 3D structural-mechanistic investigation of bovine colostrum peptides reveals multi-targetedFood chemistry: X · 2026Article
- Enzymatic Production of Collagen Oligopeptides from Porcine Skin and Their Structure-Activity Relationships in Anti-Aging and Skin-Whitening Effect.Foods (Basel, Switzerland) · 2026Article
- A review on sustainable non-thermal approaches for pea protein: Pre-treatment, extraction, modification, and applications.Food chemistry: X · 2025Article
- Proteins from Legumes, Cereals, and Pseudo-Cereals: Composition, Modification, Bioactivities, and Applications.Foods (Basel, Switzerland) · 2024Review
- Study of amino acids absorption and gut microbiome on consumption of pea protein blended with enzymes-probiotics supplement.Frontiers in nutrition · 2024Article
- Yellow Field Pea Protein (Foods (Basel, Switzerland) · 2023Review
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
In this work, we report the potency of enzymatic hydrolysates of pea proteins against trypsin and chymotrypsin. Pea protein concentrate was digested with each of alcalase, chymotrypsin, pepsin, and trypsin, followed by membrane separation of the protein hydrolysates into peptide fractions (<1, 1-3, 3-5, and 5-10 kDa). Peptide size profiling with size-exclusion gel chromatography indicated the narrowest size range (0.85-4.98 kDa) for alcalase. Trypsin activity was strongly (
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Registered trials
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