International Journal of Molecular Sciences · 2019 · 22 citations · 38 references
AgricultureBiochemistryFood ScienceFood AnalysisFood ChemistryProtein BiochemistryEnzymatic BrowningHeat Transfer In FoodsMilk ProteinsProtein AnalysisProteins In FoodsWhey ProteinsCircular DichroismDry Heat TreatmentFar-ultraviolet Circular DichroismFourier Transform Infrared SpectroscopyHydrophobicityProtein Structural ChangesWhey Protein InteractionsWhey Protein Molecular Interactions
Whey protein and inulin at various weight ratios were dry heated at 60 °C for 5 days under relative humidity of 63%. The heated mixtures were found to have significant changes in browning intensity and zeta-potential compared to untreated mixture. Heated samples showed significantly lower surface hydrophobicity than untreated mixtures. Compared with untreated samples, dry-heated samples showed significantly higher 2,2-Diphenyl-1-Picrylhydrazyl (DPPH) scavenging ability with whey protein to inulin mass ratios of 1:2 and 1:3 and significantly higher 2,2'-Azinobis(2-Ethylbenzothiazoline-6-Sulfonate) (ABTS) scavenging abilities and oxygen radical absorbance capacity (ORAC) at all weight ratios. Dry heat-induced interactions between whey protein and inulin was confirmed by changes in Sodium Dodecyl Sulfate Polyacrylamide Gel Electrophoresis (SDS-PAGE) protein profile, Fourier Transform Infrared Spectroscopy (FT-IR) and Far-ultraviolet Circular Dichroism (Far-UV CD) spectra. Dry heating caused physicochemical and structural changes of whey protein and therefore the complexes can be used to improve the antioxidative properties of the mixture under certain conditions.
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Blanca Hernández‐Ledesma, Alberto Dávalos, Begoña Bartolomé et al. · Journal of Agricultural and Food Chemistry · 2005 · 634 citations