Interactions between puerarin/daidzein and micellar casein

Journal of Food BiochemistryVolume 46, Issue 2 e14048 ORIGINAL ARTICLE Interactions between puerarin/daidzein and micellar casein Correction(s) for this article Interactions between puerarin/daidzein and micellar casein Volume 46Issue 7Journal of Food Biochemistry First Published online: April 17, 2022 Corrigendum Volume 46Issue 9Journal of Food Biochemistry First Published online: September 8, 2022 Yucheng Wang, Yucheng Wang orcid.org/0000-0002-5344-281X College of Science, Gansu Agricultural University, Lanzhou, China Contribution: Formal analysis, ​Investigation, Writing - original draftSearch for more papers by this authorMin Yang, Corresponding Author Min Yang yummy12@163.com orcid.org/0000-0001-9491-3385 College of Science, Gansu Agricultural University, Lanzhou, China Correspondence Min Yang, College of Science, Gansu Agricultural University, Lanzhou, 730070, China. Email: yummy12@163.com Contribution: Conceptualization, Formal analysis, ​Investigation, Project administration, Supervision, Writing - review & editingSearch for more papers by this authorJuanjuan Qin, Juanjuan Qin College of Science, Gansu Agricultural University, Lanzhou, China Contribution: ​InvestigationSearch for more papers by this authorWenqiang Wa, Wenqiang Wa College of Science, Gansu Agricultural University, Lanzhou, China Contribution: ​InvestigationSearch for more papers by this author Yucheng Wang, Yucheng Wang orcid.org/0000-0002-5344-281X College of Science, Gansu Agricultural University, Lanzhou, China Contribution: Formal analysis, ​Investigation, Writing - original draftSearch for more papers by this authorMin Yang, Corresponding Author Min Yang yummy12@163.com orcid.org/0000-0001-9491-3385 College of Science, Gansu Agricultural University, Lanzhou, China Correspondence Min Yang, College of Science, Gansu Agricultural University, Lanzhou, 730070, China. Email: yummy12@163.com Contribution: Conceptualization, Formal analysis, ​Investigation, Project administration, Supervision, Writing - review & editingSearch for more papers by this authorJuanjuan Qin, Juanjuan Qin College of Science, Gansu Agricultural University, Lanzhou, China Contribution: ​InvestigationSearch for more papers by this authorWenqiang Wa, Wenqiang Wa College of Science, Gansu Agricultural University, Lanzhou, China Contribution: ​InvestigationSearch for more papers by this author First published: 03 January 2022 https://doi.org/10.1111/jfbc.14048Read the full textAboutPDF ToolsRequest permissionExport citationAdd to favoritesTrack citation ShareShare Give accessShare full text accessShare full-text accessPlease review our Terms and Conditions of Use and check box below to share full-text version of article.I have read and accept the Wiley Online Library Terms and Conditions of UseShareable LinkUse the link below to share a full-text version of this article with your friends and colleagues. Learn more.Copy URL Share a linkShare onFacebookTwitterLinkedInRedditWechat Abstract Puerarin (PUE) and daidzein (DAI) are polyphenols with extensive biological activities. In the present study, the interactions between PUE/DAI and micellar casein (MC) were investigated, and the physicochemical properties of their complexes were analyzed. The results of fluorescence spectrum analysis and molecular docking revealed that the main interactions between DAI and MC were hydrophobic forces, while that between PUE and MC was hydrogen bonding. The FTIR and XRD analyses confirmed the formation of complexes between MC and PUE/DAI. After binding to PUE/DAI, the size of MC increased. The weight loss rate of MC decreased after complexing with PUE/DAI, but its morphology was not extensively modified. The DPPH radical scavenging capacities of PUE-MC and DAI-MC complexes were higher than those of free PUE/DAI in both water and ethanol. In vitro release experiments showed that the release rate of PUE/DAI was inhibited by MC under simulated intestinal conditions. Practical applications The low water solubility and poor bioavailability of PUE and DAI limit their application. Micellar casein has high affinity for PUE and DAI. After encapsulated by micellar casein, the release rates of PUE and DAI were prolonged during simulated intestinal digestion. The results would provide useful information for improving the solubility and bioavailability of PUE and DAI, and broadening the use of them in the food and pharmaceutical industry. CONFLICT OF INTEREST The authors declared that they have no conflict of interest. Open Research DATA AVAILABILITY STATEMENT Data available on request from the authors. Supporting Information Filename Description jfbc14048-sup-0001-Supinfo.docWord document, 2.4 MB Supplementary Material Please note: The publisher is not responsible for the content or functionality of any supporting information supplied by the authors. Any queries (other than missing content) should be directed to the corresponding author for the article. Volume46, Issue2February 2022e14048 RelatedInformation