The effects of Tween 20 on the emulsification and gelation properties of peanut protein isolates (PPI) were investigated. The functional properties of different peanut protein products, including PPI, Tween 20‐assisted aqueous extraction peanut proteins (TPP), and their transglutaminase‐modified products (TG‐TPP), were then compared. The results indicate that the addition of Tween 20 to the PPI resulted in higher emulsifying activity index (EAI) and emulsion stability index (ESI) values than PPI without Tween 20; however, the emulsions produced by the PPI–Tween 20 mixtures were easier to destabilize during storage. As the amount of Tween 20 was increased, both the surface hydrophobicity and gel strength of the PPI–Tween mixtures significantly decreased. TPP (containing approximately 11% Tween 20) exhibited significantly different functional properties from PPI. Compared with PPI, TPP had higher EAI and ESI values but a weaker heat‐induced gelation ability. The protein solubility of TPP was markedly higher than that of PPI. Modification of TPP with transglutaminase (TGase) significantly enhanced their gelation and oil‐binding properties but reduced the protein solubility and ESI value. The remarkable improvement in the gelation ability of TG‐TPP was mainly attributed to the formation of high‐molecular‐weight protein aggregates and their conformational changes.

中文翻译：

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Tween 20和转谷氨酰胺酶修饰对花生蛋白功能特性的影响

研究了吐温20对花生分离蛋白（PPI）的乳化和凝胶化特性的影响。然后比较了不同花生蛋白产品的功能特性，包括PPI，Tween 20辅助水提取花生蛋白（TPP）及其转谷氨酰胺酶修饰产品（TG-TPP）。结果表明，与不含Tween 20的PPI相比，向PPI中添加Tween 20导致更高的乳化活性指数（EAI）和乳液稳定性指数（ESI）值。但是，PPI–Tween 20混合物产生的乳液在储存过程中更容易失稳。随着吐温20量的增加，PPI-吐温混合物的表面疏水性和凝胶强度均显着降低。TPP（包含约11％的Tween 20）表现出与PPI显着不同的功能特性。与PPI相比，TPP的EAI和ESI值较高，但热诱导胶凝能力较弱。TPP的蛋白质溶解度显着高于PPI。用转谷氨酰胺酶（TGase）修饰TPP可显着增强其凝胶化和油结合特性，但降低了蛋白质的溶解度和ESI值。TG-TPP凝胶化能力的显着提高主要归因于高分子量蛋白聚集体的形成及其构象变化。用转谷氨酰胺酶（TGase）修饰TPP可显着增强其凝胶化和油结合特性，但降低了蛋白质的溶解度和ESI值。TG-TPP凝胶能力的显着提高主要归因于高分子量蛋白聚集体的形成及其构象变化。用转谷氨酰胺酶（TGase）修饰TPP可显着增强其凝胶化和油结合特性，但降低了蛋白质的溶解度和ESI值。TG-TPP凝胶化能力的显着提高主要归因于高分子量蛋白聚集体的形成及其构象变化。