Effect of ultrasound treatment on interactions of whey protein isolate with rutin
Na Guo, Shuang Ye, Ganghua Zhou, Yimeng Zhang, Fangyan Zhang, Jingjing Xu +3 more
Ultrasonics Sonochemistry
Abstract
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.
Extracted Claims
5 claims extracted from this paper into the knowledge graph
rutin interacts covalently with whey protein isolate
“there was covalent interaction between whey protein isolate with rutin”
ultrasound treatment causes more ordered secondary structure of WPI-R complex
“the ultrasound treatment caused the complex to develop a more ordered secondary structure”
ultrasound treatment increases binding degree of whey isolate protein with rutin
“the binding degree of whey isolate protein with rutin increased with ultrasound treatment”