2019
DOI: 10.1016/j.foodchem.2019.01.129
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Effects of high pressure processing on the interaction of α-lactalbumin and pelargonidin-3-glucoside

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Cited by 31 publications
(14 citation statements)
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“…As shown in Figure 1 , the fluorescence intensity of α-La was reduced with the increasing anthocyanin concentration due to the fluorescence quenching effect. Additionally, the maximum intensity wavelength at different thermal treatments changed little, indicating that the protein structures were not significantly affected by thermal treatments in the experimental conditions, and a similar result was found for HPP [ 22 ].…”
Section: Resultsmentioning
confidence: 56%
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“…As shown in Figure 1 , the fluorescence intensity of α-La was reduced with the increasing anthocyanin concentration due to the fluorescence quenching effect. Additionally, the maximum intensity wavelength at different thermal treatments changed little, indicating that the protein structures were not significantly affected by thermal treatments in the experimental conditions, and a similar result was found for HPP [ 22 ].…”
Section: Resultsmentioning
confidence: 56%
“…Fluorescence intensity and wavelength shift could provide information about tryptophan, tyrosine, and phenylalanine residues; the tryptophan residue was found to be dominant in absorbing the longest wavelength, displaying the largest extinction coefficient and being highly sensitive to the local environment [ 32 ]. The docking results obtained that the tryptophan residue in the binding site of α-La could be quenched by proton transfer from nearby anthocyanin [ 22 ]. In this experiment, the fluorescence spectra of α-La and P3G solutions subjected to different thermal treatments were recorded to examine the binding reaction.…”
Section: Resultsmentioning
confidence: 99%
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