2019
DOI: 10.1016/j.foodhyd.2018.11.030
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Liposomal vesicles-protein interaction: Influences of iron liposomes on emulsifying properties of whey protein

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Cited by 39 publications
(18 citation statements)
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“…The structures and properties of WPI could be easily influenced by other food ingredients through noncovalent interaction. It had been confirmed in our previous studies that Lips interacted with WPI via a hydrophobic force, hydrogen bond, and an electrostatic force (Yi, Zheng, Ding et al., 2019; Yi, Zheng, Pan et al., 2019). The spatial structure and emulsifying properties of WPI could be changed by the interaction between proteins and Lips.…”
Section: Introductionsupporting
confidence: 64%
“…The structures and properties of WPI could be easily influenced by other food ingredients through noncovalent interaction. It had been confirmed in our previous studies that Lips interacted with WPI via a hydrophobic force, hydrogen bond, and an electrostatic force (Yi, Zheng, Ding et al., 2019; Yi, Zheng, Pan et al., 2019). The spatial structure and emulsifying properties of WPI could be changed by the interaction between proteins and Lips.…”
Section: Introductionsupporting
confidence: 64%
“…These shifts may be attributed to the changes in interactions established within the PMAC/L sample. Namely, the peaks at 1388 cm −1 (Figure 1A) and 1386 cm −1 (Figure 1B) could be the indication of hydrogen bonds established between liposomes and casein (interactions between carbonyl group or NH group of amide II of protein and oxygen group of phospholipid nanoparticles [ 40 ] ), whereas the peaks at 1244 and 1446 cm −1 (Figure 1A), 1245 and 1444 cm −1 (Figure 1B) could be correlated with established between casein and the surface of the liposomes particles. These discrete shifts could be a consequence of poor, physical interactions established between casein and phospholipids.…”
Section: Results and Disscussionmentioning
confidence: 99%
“…For the WPI‐coated ASX‐loaded liposomes, these disappeared peaks at 2926, 2855, and 1465 cm −1 corresponded to the groups of the hydrophobic fatty acids in SPC. [ 33 ] It stated that the hydrophobic groups of SPC interacted with the hydrophobic regions of WPI after coating because of the hydrophobic force. [ 34 ] Furthermore, the disappearance of the peak at 1739 cm −1 might account for the limited stretching and bending of the vibration in lipid bilayer when bound to the WPI.…”
Section: Resultsmentioning
confidence: 99%