Interaction of β -lactoglobulin with (−)-epigallocatechin-3-gallate under different processing conditions of pH and temperature by the fluorescence quenching method

摘要: The binding interactions between (−)-epigallocatechin-3-gallate (EGCG) and bovine β-lactoglobulin (β-LG) during food processing under different temperatures (25–100 °C) pH levels (3.2–7.4) were investigated using the fluorescence quenching method. results indicated that temperature had effects on structure EGCG-binding ability of β-LG. At a higher (≥6.4) (≥80 °C), conformation β-LG more open than those its native state due to heat-induced denaturation unfolding protein, which increased affinity with EGCG through hydrophobic hydrogen bonds, in turn promoted further unfolding. highest constant (K A ) site numbers (n) 12.50 (±0.60) × 105 M−1 (pH 6.4, 80 °C), 0.62 (±0.02)~0.97 (±0.16), respectively. However, at 100 °C neutral pH, oxidative loss thermal probably led decrease β-LG–EGCG interactions. These would be helpful better understand relevance interaction bioactivity bioavailability processing, maintain health benefits this type functional products industry.