Abstract Whey proteins are usually sensitive to ionic strength, pH change, and heat treatment, which may affect their functional properties. Maillard conjugation could be a facile approach to improve whey protein functionality. In this study, whey protein isolate (WPI; 0.6%, w/v) was conjugated to low acyl gellan gum (0.1, 0.2, and 0.3%, w/v) through the Maillard reaction at 90 °C for 90 min. The conjugate formation was confirmed by pH decrement, glycation degree (up to 9.44%), browning index, sodium dodecyl sulphate-polyacrylamide gel electrophoresis, and Fourier transform infrared spectroscopy. The surface hydrophobicity of WPI increased up to 2-fold upon conjugation, which led to a solubility decrease. However, the conjugated WPI had an improved interfacial activity, emulsifying activity (∼6%), foaming capacity (up to 63.64%), thickening ability (up to 24.67-fold), reducing power (up to 28.86-fold), and iron chelating activity (up to 3.31-fold). These findings may widen the industrial application of whey proteins.

中文翻译：

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乳清蛋白分离物-低酰基结冷胶基于美拉德的偶联物，具有定制的技术功能和抗氧化活性

摘要 乳清蛋白通常对离子强度、pH 变化和热处理敏感，这可能会影响其功能特性。美拉德共轭可能是一种改善乳清蛋白功能的简便方法。在本研究中，乳清蛋白分离物（WPI；0.6%，w/v）通过美拉德反应在 90 °C 下与低酰基结冷胶（0.1、0.2 和 0.3%，w/v）结合 90 分钟。通过 pH 值降低、糖化度（高达 9.44%）、褐变指数、十二烷基硫酸钠-聚丙烯酰胺凝胶电泳和傅里叶变换红外光谱证实了共轭物的形成。结合后，WPI 的表面疏水性增加了 2 倍，导致溶解度降低。然而，共轭 WPI 具有改进的界面活性、乳化活性（~6%）、发泡能力（高达 63.64%）、增稠能力（高达 24.67 倍）、还原能力（高达 28.86 倍）和铁螯合活性（高达 3.31 倍）。这些发现可能会拓宽乳清蛋白的工业应用。