Effect of ultrasound treatment on interactions of whey protein isolate with rutin
•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 ultraso...
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| Published in | Ultrasonics sonochemistry Vol. 95; p. 106387 |
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| Main Authors | , , , , , , , , |
| Format | Journal Article |
| Language | English |
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Netherlands
Elsevier B.V
01.05.2023
Elsevier |
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| Abstract | •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. |
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| AbstractList | 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. •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. • 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. 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. |
| ArticleNumber | 106387 |
| Author | Zhu, Guilan Pan, Shenyu Wang, Ziying Zhou, Ganghua Zhang, Fangyan Guo, Na Xu, Jingjing Zhang, Yimeng Ye, Shuang |
| Author_xml | – sequence: 1 givenname: Na orcidid: 0000-0002-2161-8059 surname: Guo fullname: Guo, Na email: yiyanghot@126.com organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 2 givenname: Shuang surname: Ye fullname: Ye, Shuang organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 3 givenname: Ganghua surname: Zhou fullname: Zhou, Ganghua organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 4 givenname: Yimeng surname: Zhang fullname: Zhang, Yimeng organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 5 givenname: Fangyan surname: Zhang fullname: Zhang, Fangyan organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 6 givenname: Jingjing surname: Xu fullname: Xu, Jingjing organization: School of Food and Biological Engineering, Hefei University of Technology, Hefei, Anhui 230009, China – sequence: 7 givenname: Shenyu surname: Pan fullname: Pan, Shenyu organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 8 givenname: Guilan surname: Zhu fullname: Zhu, Guilan email: zhuguilan13@126.com organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China – sequence: 9 givenname: Ziying surname: Wang fullname: Wang, Ziying organization: Department of Life Science, Hefei Normal University, Hefei, Anhui 230061, China |
| BackLink | https://www.ncbi.nlm.nih.gov/pubmed/37030074$$D View this record in MEDLINE/PubMed |
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| Keywords | Ultrasound treatment Covalent interaction Rutin Whey protein isolate |
| Language | English |
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| Snippet | •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... Rutin is a biologically active polyphenol, but its poor water solubility and low bioavailability limit its application to the food industry. We investigated... • 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,... |
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| SubjectTerms | Covalent interaction Original Rutin Ultrasound treatment Whey protein isolate |
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| Title | Effect of ultrasound treatment on interactions of whey protein isolate with rutin |
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