Characterization of binding interactions of (-)-epigallocatechin-3-gallate from green tea and lipase.

@article{Wu2013CharacterizationOB,
  title={Characterization of binding interactions of (-)-epigallocatechin-3-gallate from green tea and lipase.},
  author={Xuli Wu and Weiyi He and Li Yao and H. P. Zhang and Zhigang Liu and Wenpu Wang and Ye Ye and Jijuan Cao},
  journal={Journal of agricultural and food chemistry},
  year={2013},
  volume={61 37},
  pages={
          8829-35
        }
}
Understanding the interaction of (-)-epigallocatechin-3-gallate (EGCG) and lipase is important for understanding EGCG's inhibition of lipase. In this paper, the interaction of EGCG and porcine lipase was characterized by fluorescence spectroscopy, circular dichroism (CD), isothermal titration calorimetry, and molecular docking. EGCG might act as a noncompetitive pancreatic lipase inhibiter. EGCG bound to lipase with affinity of K(a) = 2.70 × 10⁴ L mol⁻¹. Thermodynamic features suggested that… CONTINUE READING
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