2021
DOI: 10.1016/j.foodchem.2021.129617
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Interaction mechanism of flavonoids with whey protein isolate: A spectrofluorometric and theoretical investigation

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Cited by 38 publications
(12 citation statements)
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“…In this process, the maximum peak of fluorescence spectrum changed slightly, indicating that the microenvironment around tyrosine residue and tryptophan residue changed. Similar results had previously been reported that whey protein changed its molecular conformation through interaction with puerarin, rutin and phloridin (Li et al, 2021).…”
Section: Synchronous Fluorescence Analysissupporting
confidence: 90%
“…In this process, the maximum peak of fluorescence spectrum changed slightly, indicating that the microenvironment around tyrosine residue and tryptophan residue changed. Similar results had previously been reported that whey protein changed its molecular conformation through interaction with puerarin, rutin and phloridin (Li et al, 2021).…”
Section: Synchronous Fluorescence Analysissupporting
confidence: 90%
“…3D uorescence is oen utilized to investigate the structural changes in proteins bound to small molecules (HYP), and it shows the changes in protein Trp and Tyr residues. 41 Fig. 2(C and D) reveals that with the expansion of the HYP concentrations, the uorescence intensities of Peak 1 and 2 decreased.…”
Section: Synchronous and 3d Uorescence Spectrummentioning
confidence: 94%
“…For static quenching, the binding constant (Ka) and binding site number (n) were computed using the double-logarithm equation [23]:…”
Section: Fluorescence Experimentsmentioning
confidence: 99%