ArticleFoods (Basel, Switzerland)2023
Enhanced Gel Properties of Duck Myofibrillar Protein by Plasma-Activated Water: Through Mild Structure Modifications.
Article in Foods (Basel, Switzerland), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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Who cites it
7 citing papers in PubMed, 17 citations in OpenAlex.
- Impact of Novel and Emerging Nonthermal Technologies on the Functionality and Digestibility of Poultry-Derived Proteins.Foods (Basel, Switzerland) · 2026Review
- Influence of plasma-activated water treatment on the cold storage stability and flavor profile of duck fillets.Food chemistry: X · 2025Article
- Effects of Selective Enzymatic Hydrolysis on Structural Properties and Gel Properties of Soybean Protein Isolate.Foods (Basel, Switzerland) · 2025Article
- Exploring the Effects of Novel Food Processing Methods on Food Proteins: A Review.Food science & nutrition · 2025Review
- Effect of Low-Temperature Plasma Activated Water with Different Treatment Times on Myofibrillar Proteins of Thawed Pork.Foods (Basel, Switzerland) · 2025Article
- Effects of plasma-activated water on structural and functional properties of PSE-like chicken protein isolate.Current research in food science · 2025Article
- Effects of Pulsed Electric Field on the Physicochemical and Structural Properties of Micellar Casein.Polymers · 2023Article
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
Abstract
This study assessed the gel properties and conformational changes of duck myofibrillar protein (DMP) affected by plasma-activated water (PAW) generated at various discharge times (0 s, 10 s, 20 s, 30 s, and 40 s). With the treatment of PAW-20 s, the gel strength and water-holding capacity (WHC) of DMP gels were significantly increased when compared to the control group. Throughout the heating process, dynamic rheology revealed that the PAW-treated DMP had a higher storage modulus than the control. The hydrophobic interactions between protein molecules were significantly improved by PAW, resulting in a more ordered and homogeneous gel microstructure. The increased sulfhydryl and carbonyl content in DMP indicated a higher degree of protein oxidation with PAW treatment. Additionally, the circular dichroism spectroscopy demonstrated that PAW induced α-helix and β-turn transformed to β-sheet in DMP. Surface hydrophobicity, fluorescence spectroscopy, and UV absorption spectroscopy suggested that PAW altered DMP's tertiary structure, although the electrophoretic pattern indicated that the primary structure of DMP was mostly unaffected. These results suggest that PAW can improve the gel properties of DMP through mild alteration in its conformation.
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Registered trials
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