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Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin

Journal of Food Science and Technology volume 54, pages 3421–3432 (2017)Cite this article

Abstract

In this study, theaflavins (TF1, TF2A, TF2B and TF3) were prepared from black tea and their interaction with bovine serum albumin (BSA) was explored by fluorescence and CD spectroscopy. The results showed that the structures of theaflavins exhibited significant effects on the binding/quenching process, and the binding affinity increased with the increase of molecular weight of theaflavins and the presence of galloyl moiety. The quenching effects showed a sequence as TF3 > TF2A > TF2B > TF1, demonstrating the important role of the galloyl moiety on the C-3 position of theaflavins. CD spectra indicated that TF3 in high concentration could change the skeleton structure of BSA and induce the unfolding of BSA secondary structure. The present results provide a new perspective for better understanding of the likely physiological fate of theaflavins and help to control the functional characteristics of food.

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Acknowledgements

This work was supported by a grant-in-aid from the National Key R&D Program of China (2017YFD0400800), a grant-in-aid from Key Technology R&D Program of Jiangsu Province (BE2013313) and a project funded by the Priority Academic Program Development of Jiangsu Higher Education Institutions (PAPD).

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Affiliations

  1. College of Food Science and Technology, Nanjing Agricultural University, Nanjing, 210095, China

    Shicheng Lei, Donglan Xu, Muhammad Saeeduddin, Asad Riaz & Xiaoxiong Zeng

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  1. Shicheng Lei
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  2. Donglan Xu
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  3. Muhammad Saeeduddin
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  4. Asad Riaz
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  5. Xiaoxiong Zeng
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Correspondence to Xiaoxiong Zeng.

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Lei, S., Xu, D., Saeeduddin, M. et al. Characterization of molecular structures of theaflavins and the interactions with bovine serum albumin. J Food Sci Technol 54, 3421–3432 (2017). https://doi.org/10.1007/s13197-017-2791-5

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  • DOI: https://doi.org/10.1007/s13197-017-2791-5

Keywords

  • Theaflavins
  • EGCG
  • Bovine serum albumin
  • Interaction
  • Fluorescence quenching