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Interaction of epigallocatechin-3-gallate with β-lactoglobulin: molecular characterization and biological implication

Interaction of epigallocatechin-3-gallate with β-lactoglobulin: molecular characterization and... Epigallocatechin-3-gallate (EGCG), an antioxidant present in green tea, could play an important role in the prevention of cancer. However, its bioavailability is low due to its instability in gastrointestinal environment. β-Lactoglobulin (β-Lg), the major protein in whey, is known for its capacity to bind bioactive molecules and could protect them from oxidation. Interaction between β-Lg and EGCG was investigated at pH 7.0 and 4.0 using fluorescence and Fourier transform infrared spectroscopy, and its impact on EGCG antioxidant activity was determined using the ferric-reducing antioxidant power method. EGCG bound to native or heat-denatured β-Lg by hydrogen bonding and possibly hydrophobic interaction at pH 7.0 and 4.0. The affinity of EGCG for heat-denatured β-Lg at pH 7.0 was greater than for native β-Lg and greater than its affinity for the protein in either state at pH 4.0. Complexing with β-Lg decreased the antioxidant activity of EGCG under all conditions investigated. However, the protein provided limited protection of EGCG against degradation over time, the heat-denatured form being slightly more effective at pH 7.0. This study provides insight into the characteristics of β-Lg binding with a flavonoid and its impact on the antioxidant activity of flavonoids in food systems. http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Dairy Science & Technology Springer Journals

Interaction of epigallocatechin-3-gallate with β-lactoglobulin: molecular characterization and biological implication

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Publisher
Springer Journals
Copyright
Copyright © 2011 by INRA and Springer Science+Business Media B.V.
Subject
Chemistry; Microbiology; Agriculture; Food Science
ISSN
1958-5586
eISSN
1958-5594
DOI
10.1007/s13594-011-0036-3
Publisher site
See Article on Publisher Site

Abstract

Epigallocatechin-3-gallate (EGCG), an antioxidant present in green tea, could play an important role in the prevention of cancer. However, its bioavailability is low due to its instability in gastrointestinal environment. β-Lactoglobulin (β-Lg), the major protein in whey, is known for its capacity to bind bioactive molecules and could protect them from oxidation. Interaction between β-Lg and EGCG was investigated at pH 7.0 and 4.0 using fluorescence and Fourier transform infrared spectroscopy, and its impact on EGCG antioxidant activity was determined using the ferric-reducing antioxidant power method. EGCG bound to native or heat-denatured β-Lg by hydrogen bonding and possibly hydrophobic interaction at pH 7.0 and 4.0. The affinity of EGCG for heat-denatured β-Lg at pH 7.0 was greater than for native β-Lg and greater than its affinity for the protein in either state at pH 4.0. Complexing with β-Lg decreased the antioxidant activity of EGCG under all conditions investigated. However, the protein provided limited protection of EGCG against degradation over time, the heat-denatured form being slightly more effective at pH 7.0. This study provides insight into the characteristics of β-Lg binding with a flavonoid and its impact on the antioxidant activity of flavonoids in food systems.

Journal

Dairy Science & TechnologySpringer Journals

Published: Aug 2, 2011

References