The incorporation of hydrophobic ingredients, such as resveratrol (a fat-soluble phytochemical), in nanoemulsions can increase the water solubility and stability of these hydrophobic ingredients. The nanodelivery of resveratrol can result in a marked improvement in the bioavailability of this health-promoting ingredient. The current study hypothesized that resveratrol can bind to caprine casein, which may result in the preservation of the biological properties of resveratrol. The fluorescence spectra provided proof of this complex formation by demonstrating that resveratrol binds to caprine casein in the vicinity of tryptophan amino acid residues. The caprine casein/resveratrol complex is stabilized by hydrophobic interactions and hydrogen bonds. Hence, to study the rate of resveratrol degradation during processing/storage, resveratrol losses were determined by reversed-phase high performance liquid chromatography (RP-HPLC) in nanoemulsions stabilized by bovine and caprine caseins individually and in combination with polysorbate-20. At 48 h oxidation, 88.33% and 89.08% was left of resveratrol in the nanoemulsions stabilized by caprine casein (αs1
-I)/polysorbate-20 complex and caprine (αs1
-II)/polysorbate-20 complex, while there was less resveratrol left in the nanoemulsions stabilized by bovine casein/polysorbate-20 complex, suggesting that oxygen degradation was involved. The findings of this study are crucial for the food industry since they imply the potential use of caprine casein/polysorbate-20 complex to preserve the biological properties of resveratrol.
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