Effect of ultrasound treatment on interactions of whey protein isolate with rutin

• Published in: Ultrasonics sonochemistry Vol. 95; p. 106387
• Main Authors: Guo, Na, Ye, Shuang, Zhou, Ganghua, Zhang, Yimeng, Zhang, Fangyan, Xu, Jingjing, Pan, Shenyu, Zhu, Guilan, Wang, Ziying
• Format: Journal Article
• Language: English
• Published: Netherlands Elsevier B.V 01.05.2023; Elsevier
• Subjects: Covalent interaction; Original; Rutin; Ultrasound treatment; Whey protein isolate; Ultrasound treatment; Covalent interaction; Rutin; Whey protein isolate
• ISSN: 1350-4177; 1873-2828
• DOI: 10.1016/j.ultsonch.2023.106387

•The WPI-R complex was prepared by pH-driven method (pH-DM) combined with ultrasonic treatment.•The interaction between whey protein and rutin is covalent, and appropriate ultrasonic treatment could promote degree of polyphenol binding and grafting between whey protein isolate and rutin.•The ultrasonic treatment increased the WPI-R complex's solubility while decreasing its surface hydrophobicity and free sulfhydryl.•The secondary structure of the complex was improved with ultrasonic treatment, which results in three-dimensional honeycomb structures with small and uniform pore sizes. Rutin is a biologically active polyphenol, but its poor water solubility and low bioavailability limit its application to the food industry. We investigated the effect of ultrasound treatment on the properties of rutin (R) and whey protein isolate (WPI) using spectral and physicochemical analysis. The results revealed that there was covalent interaction between whey protein isolate with rutin, and the binding degree of whey isolate protein with rutin increased with ultrasound treatment. Additionally, solubility and surface hydrophobicity of WPI-R complex improved with ultrasonic treatment, and a maximum solubility of 81.9 % at 300 W ultrasonic power. The ultrasound treatment caused the complex to develop a more ordered secondary structure, resulting in a three-dimensional network structure with small and uniform pore sizes. This research could provide a theoretical reference for studying protein–polyphenol interactions and their applications in food delivery systems.