Thermally-induced protein–polyphenol co-assemblies: beta lactoglobulin-based nanocomplexes as protective nanovehicles for EGCG

Design of whey protein nanostructures for incorporation and release of nutraceutical compounds in food

“…A stable and clear nanosystem was observed at pH 6.4-7.0, and highest protection of EGCG antioxidant activity was obtained with -Lg heated at 85 o C and at the molar ratio of 1:2 (-Lg: EGCG). In the same way, Shpigelman et al have nanoentrapped EGCG after cooling and vortexing pre-heated -Lg solutions (75-85 o C, 20 min) (Shpigelman et al, 2010;Shpigelman et al, 2012). The measured association constant with the heated protein was about 3.5-fold higher than that with the native protein.…”

“…Whey proteins are also appropriate matrices for delivery of bioactive compounds, and are accordingly a remarkable component of human diet. They have thus received consider-able attention, both as potential delivery vehicles and as precursors of bioactive peptides that may form even during digestion (Zimet and Livney, 2009;Livney, 2010;Nagpal et al, 2011;Relkin and Shukat, 2012). These proteins are typically globular in nature (very susceptible to denaturation by heat), with high levels of secondary and tertiary structures in which the acidic/ basic and hydrophobic/hydrophilic amino acids are distributed in a fairly balanced way (Smilowitz et al, 2005).…”

Preparation of Complexes between Ovalbumin Nanoparticles and Retinoic Acid for Efficient Induction of Tolerogenic Dendritic Cells

“…The binding of ATRA to OVA NPs was evaluated by quenching of intrinsic fluorescence of Trp residues of OVA upon binding with ATRA. 22,23 concentrations of ATRA, respectively. The increase in the ATRA concentration resulted in a gradual decrease in the fluorescence intensity of Trp residues without a shift of the maximum emission wavelength in both OVA and OVA NPs.…”

Emerging Technologies for Bioactive Applications in Foods

“…No binding was found between naringin and BLG, probably due to the lower hydrophobicity of naringin and the steric interference of its sugar. Thermally induced protein-polyphenol co-assemblies of beta-lactoglobulinbased nanocomplexes as protective nanovehicles for EGCG were reported (Shpigelman et al 2010). Also it was reported that the genetic BLG variants A, B, and C have different numbers of binding sites for retinol (almost completely incorporated into the calyx), as well as for EGCG (exclusively bound on the surface) (Keppler et al 2014).…”