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

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Abstract

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

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Acknowledgments

The authors thank Prof. Mario G. Ferruzzi and Prof. Owen Griffith Jones in Purdue University for kindly providing valuable advice and instruments throughout this study. This work was supported financially in part by the Innovation and Exploration Fund of State Key Laboratory of Food Science and Technology, Jiangnan University (No. SKLF-ZZA-201504), the Fundamental Research Funds for the Central Universities (No. JUSRP21108), the ‘12th-Five’ National Science and Technology Support Program of China (No. 2012BAD37B01) and Scholarship Fund of China Scholarship Council Program (No. 2011832481).

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This article does not contain any studies with human or animal subjects.

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Authors and Affiliations

  1. State Key Laboratory of Food Science and Technology, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu, People’s Republic of China

    Zhiyong He & Jie Chen

  2. Synergetic Innovation Center of Food Safety and Nutrition, Jiangnan University, 1800 Lihu Avenue, Wuxi, 214122, Jiangsu, People’s Republic of China

    Jie Chen

  3. Department of Food Science, Purdue University, 745 Agriculture Mall Dr., West Lafayette, IN, 47906, USA

    Sydney Elizabeth Moser

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  1. Zhiyong He
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Correspondence to Zhiyong He.

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He, Z., Chen, J. & Moser, S.E. Interaction of β-lactoglobulin with (−)-epigallocatechin-3-gallate under different processing conditions of pH and temperature by the fluorescence quenching method. Eur Food Res Technol 241, 357–366 (2015). https://doi.org/10.1007/s00217-015-2466-2

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