AGFD 169 |
| β-Lactoglobulin (β-LG), the major whey protein in the milk of ruminant, has a high affinity for a wide range of compounds. Resveratrol (3,5,4'-trihydroxystilbene), a natural polyphenolic compound found in grapes and red wine, exhibits many physiological effects, including anti-oxidant, anti-flammatory and anti-platelet aggregating actions. In this study, the interaction of resveratrol with β-LG is investigated using circular dichroism and fluorescence. Resveratrol can interact with β-LG to form 1:1 complexes, which has no apparent influence on the secondary structure of β-LG but partly destroys the tertiary structure of β-LG. The binding constants are between 104 and 106 M-1, indicating that the interaction of resveratrol with β-LG is a non-specific binding. After interacting with β-LG, resveratrol transfers from a hydrophilic environment in the aqueous solution to a more hydrophobic environment, which hydrophobicity is much weaker than 75% ethanol. These results suggest that resveratrol molecules are bound in the surface of β-LG. |
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General Posters
1:00 PM-3:00 PM, Tuesday, August 21, 2007 BCEC -- Exhibit Hall - B2, Poster
Division of Agricultural & Food Chemistry |