Emulsifying Properties of Oat Protein/Casein Complex Prepared Using Atmospheric Cold Plasma with pH Shifting

Le résumé fourni par la source

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 m2/g). These findings highlight the potential application value of OPI/casein mixtures in liquid dairy products. In addition, dairy products based on oat protein are more conducive to sustainable development than traditional dairy products.

Ce résumé expose les affirmations des auteurs. BNTIC ne l’interprète pas comme une validation indépendante des résultats.