Journal of Agricultural and Food Chemistry · 2012 · 144 citations · 39 references
AgricultureBiochemistryFood ScienceCarbohydrate ChemistryFood ChemistryFood PreservationCarbohydrates In FoodsFood AntioxidantsFood Preservation ChemistryPolysaccharide PropertiesAntioxidant Activity AssaysAntioxidant PropertiesAntioxidant TreatmentEntrapmentHeating EfficiencyParticle Size ReductionParticle Size RetentionPh Dependence
(-)-Epigallocatechin-3-gallate (EGCG) was loaded in heat treated β-lactoglobulin (β-Lg) for the preservation of antioxidant activity. The effects of pH (2.5-7.0), the heating temperature of β-Lg (30-85 °C), the molar ratio of β-Lg to EGCG (1:2-1:32), and the β-Lg concentration (1-10 mg/mL) on the properties of β-Lg-EGCG complexes were studied. All four factors significantly influenced the particle size, the ζ-potential, and the entrapment efficiency of EGCG and EGCG loading in β-Lg particles. A stable and clear solution system could be obtained at pH 6.4-7.0. The highest protection of EGCG antioxidant activity was obtained with β-Lg heated at 85 °C and the molar ratio of 1:2 (β-Lg: EGCG). β-Lg-EGCG complexes were found to have the same secondary structure as native β-Lg.
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Milk proteins as vehicles for bioactives
Yoav D. Livney · Current Opinion in Colloid & Interface Science · 2009 · 930 citations
Structural Basis of the Tanford Transition of Bovine β-Lactoglobulin<sup>,</sup>
Bin Qin, Maria C. Bewley, Lawrence K. Creamer et al. · Biochemistry · 1998 · 475 citations