2019
DOI: 10.1016/j.ultsonch.2018.10.026
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Conformational and physicochemical properties of quinoa proteins affected by different conditions of high-intensity ultrasound treatments

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Cited by 98 publications
(51 citation statements)
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“…These results are similar to chitosan‐starch and gallic acid films, and higher than gelatin based films containing oily tomato extract and gelatin‐chitosan based films loaded with active compounds . The increase in antioxidant activity could be related to the exposure of residues during protein unfolding, a phenomenon that has previously been reported for proteins during ultrasonic pulses …”
Section: Resultssupporting
confidence: 83%
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“…These results are similar to chitosan‐starch and gallic acid films, and higher than gelatin based films containing oily tomato extract and gelatin‐chitosan based films loaded with active compounds . The increase in antioxidant activity could be related to the exposure of residues during protein unfolding, a phenomenon that has previously been reported for proteins during ultrasonic pulses …”
Section: Resultssupporting
confidence: 83%
“…In the films with ultrasound‐pulsed gelatin added, whilst the surface appears smoother, some agglomeration is present. Although several studies show excellent compatibility of chitosan and gelatin materials, the overexposure of hydrophobic residues in gelatin, due to cavitation, can produce repulsive interactions that cause the polymeric chains to rewind and create an aggregation phenomenon . Also, during cavitation, molecules can be affected depending on their proximity to the ultrasonic probe, causing differences in the size and shape of these aggregates.…”
Section: Resultsmentioning
confidence: 99%
“…The increase in the solubility of proteins has been related to changes in conformation that are caused by cavitation (as mentioned above), by the exposure of more internal hydrophilic residues to the water surface, by the interruption of hydrophobic interactions in insoluble aggregates, and also by changes in the electronic environment of the acid residues related to the effect of pH. This behavior in protein solubility has been previously reported in HIU studies, although it has also been reported that the prolongation of these treatments can generate insoluble aggregates [5,9,10,22].…”
Section: Protein Solubilitymentioning
confidence: 66%
“…As mentioned before, the amide I and II peaks are the leading indicators of changes in the secondary structure, and it is assumed that the displacement of these bands is a product of the changes and disorder in the conformations of the secondary structures when increasing the intensity of the ultrasonic pulses [10,25,27]. These results may be related to the results in the previous section, where it was shown that the different treatments caused significant changes in the proportions of the α-helix and the β-sheet in the UPG.…”
Section: Fourier-transform Infrared Spectramentioning
confidence: 99%
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