Lily bulb polyphenol oxidase obtained via an optimized multi-stage separation strategy for structural analysis and browning mechanism elucidation
文献类型： 外文期刊
作者： Xu, Haishan 1 ; Wang, Xinyu 2 ; Li, Huan 2 ; Xie, Ying 2 ; Ding, Ke 2 ; Xu, Saiqing 2 ; Ding, Shenghua 2 ; Wang, Rongrong 1 ;
作者机构： 1.Hunan Agr Univ, Coll Food Sci & Technol, Changsha 410128, Peoples R China
2.Hunan Acad Agr Sci, Hunan Agr Prod Proc Inst, DongTing Lab, Changsha 410125, Peoples R China
3.Hunan Univ, Coll Biol, Longping Branch, Changsha 410125, Peoples R China
关键词： Lily bulb; Polyphenol oxidase; Purification optimization; Binding sites; Molecular docking
期刊名称：FOOD CHEMISTRY （ 影响因子：9.8； 五年影响因子：9.7 ）
ISSN： 0308-8146
年卷期： 2025 年 463 卷
页码：
收录情况： SCI
摘要： An optimized multi-stage separation strategy was developed to purify lily bulb polyphenol oxidase (PPO) for revealing its molecular structure. The PPO was purified 14.64-fold with high specific activity of 153,900 U/mg via optimized conditions of phosphate buffer pH (6.5), solid-liquid ratio (1:3), PVPP content (2 %), extraction time (4 h), followed by 30 %-50 % ammonium sulfate, diethylaminoethyl ion-exchange chromatography (0.1 M NaCl), and size exclusion chromatography. The PPO was identified as a dimeric protein with molecular weight of 135 kDa, containing 58.79 % random coil, 20.78 % alpha-helix, 17.41 % /3-folding, and 3.02 % /3-corner. The threedimensional structure via homology modeling suggested that active center CuA bound to His151, His172, and His181, CuB bound to His307, His311, and His341. Furthermore, molecular docking indicated that its Phe337 and Tyr312 residues were catalytic cavity gates of catechol and 4-methylcatechol, respectively. Therefore, this study successfully analyzed purified PPO structure and further provided a theoretical foundation for its browning mechanism.
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