ArticleFoods (Basel, Switzerland)2025
Emulsifying Properties of Oat Protein/Casein Complex Prepared Using Atmospheric Cold Plasma with pH Shifting.
Article in Foods (Basel, Switzerland), 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 1 paper.
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Who cites it
1 citing paper in PubMed.
- Roles of Cold Plasma Treatment on the Functional Properties of Plant-Based Proteins.International journal of food science · 2026Review
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9 authors.
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Abstract
An oat protein isolate is an ideal raw material for producing a wide range of plant-based products. However, oat protein exhibits weak functional properties, particularly in emulsification. Casein-based ingredients are commonly employed to enhance emulsifying properties as a general practice in the food industry. pH-shifting processing is a straightforward method to partially unfold protein structures. This study modified a mixture of an oat protein isolate (OPI) and casein by combining a pH adjustment (adjusting the pH of two solutions to 12, mixing them at a 3:7 ratio, and maintaining the pH at 12 for 2 h) with an atmospheric cold plasma (ACP) treatment to improve the emulsifying properties. The results demonstrated that the ACP treatment significantly enhanced the solubility of the OPI/casein mixtures, with a maximum solubility of 82.63 ± 0.33%, while the ζ-potential values were approximately -40 mV, indicating that all the samples were fairly stable. The plasma-induced increase in surface hydrophobicity supported greater protein adsorption and redistribution at the oil/water interface. After 3 min of treatment, the interfacial pressure peaked at 8.32 mN/m. Emulsions stabilized with the modified OPI/casein mixtures also exhibited a significant droplet size reduction upon extending the ACP treatment to 3 min, decreasing from 5.364 ± 0.034 μm to 3.075 ± 0.016 μm. The resulting enhanced uniformity in droplet size distribution signified the formation of a robust interfacial film. Moreover, the ACP treatment effectively enhanced the emulsifying activity of the OPI/casein mixtures, reaching (179.65 ± 1.96 m
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