期刊
FOOD CHEMISTRY
卷 393, 期 -, 页码 -出版社
ELSEVIER SCI LTD
DOI: 10.1016/j.foodchem.2022.133415
关键词
Inhibition mechanism; Polyphenol oxidase (PPO); Epigallocatechin-3-gallate (EGCG); Multispectroscopic; Computational simulation
In this study, it was found that EGCG could inhibit PPO activity by competing for catalytic centers and inducing aggregation. The binding mode of EGCG with PPO and the conformational and secondary structure changes of PPO after binding were revealed through various experimental methods and computational simulations.
Polyphenol oxidase (PPO)-mediated enzymatic browning occurs in fruit, vegetables and aquatic products and causes huge economic losses every year. In this study, epigallocatechin-3-gallate (EGCG) displayed high affinity for and efficient inhibitory capacity against PPO. To explore the inhibition mechanism, multispectroscopic methods and computational simulations were implemented. Initially, EGCG inhibited PPO activity reversibly in a mixed-type manner. Then, the conformation and secondary structure changes of PPO after binding with EGCG were discovered by fluorescence emission spectra and circular dichroism. Molecular docking and dynamic simulation results revealed that EGCG could tightly bind with the binuclear copper domain of PPO through hydrophobic stacking and hydrogen bonds. Moreover, EGCG might act as a linker to interact with different PPO molecules at another binding site. Transmission electron microscopy observation suggested that EGCG induced the aggregation of PPO. Therefore, the inhibition mechanism of EGCG on PPO included competition for catalytic centers and induced aggregation.
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