ArticleFood chemistry: X2026
pH-dependent effects of pepsin and trypsin on the stability and antibiofilm functionality of pea protein-stabilized carvacrol nanoemulsions.
Article in Food chemistry: X, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 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
2 citing papers in PubMed.
- Eugenol nanoemulsion protects chickens against S. Typhimurium infection by improving cecal barrier function and alleviating oxidative stress and inflammation.Poultry science · 2026Article
- Protease-assisted microencapsulation of carvacrol in pea protein systems for enhanced and durable antibiofilm activity.Current research in food science · 2026Article
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Authors and funding
5 authors.
Funding
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Abstract
This study investigated how proteolytic enzymes influence the physicochemical stability and bioactivity of pea protein isolate (PPI)-stabilized nanoemulsions encapsulating carvacrol at pH 3.5, 7.0, and 10.0. Pepsin or trypsin (0.1 wt%) was incorporated into pre-formed nanoemulsions (1 wt% PPI, 5 wt% carvacrol) to evaluate pH-dependent effects on structure and function. Under neutral and alkaline conditions, nanoemulsions showed submicron droplets (≈180-254 nm), high ζ-potentials (-26.5 to -41.9 mV), and excellent stability (4 weeks, CI < 5 %). Trypsin introduction enhanced emulsion stability through moderate interfacial hydrolysis, while pepsin caused destabilization under acidic conditions (≈1.5 μm, PDI ≈ 1.0). Carvacrol determined antibacterial activity (MIC = 312.5 μg/mL), whereas antibiofilm performance was pH- and enzyme-dependent: trypsin markedly enhanced biofilm eradication at pH 7.0-10.0, and pepsin had limited effect. Molecular docking revealed strong electrostatic pepsin-protein interactions causing destabilization, while trypsin bound non-catalytically, reinforcing interfacial cohesion.
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