茶黄素
多酚氧化酶
山茶
儿茶酚
化学
愈创木酚
没食子酸表没食子酸酯
酪氨酸酶
酶
多酚
儿茶酚氧化酶
生物化学
表儿茶素没食子酸盐
食品科学
生物
植物
过氧化物酶
抗氧化剂
作者
Jie Teng,Zhihua Gong,Yanli Deng,Ling Chen,Li Qin,Yuanyuan Shao,Gang Li,Wenjun Xiao
标识
DOI:10.1016/j.lwt.2017.05.065
摘要
Polyphenol oxidase (PPO) plays a key role in tea processing, converting catechins into theaflavines. Two PPOs were isolated and purified from tea (Camellia sinensis) leaves. PPO1 and PPO2 exhibited molecular weights of 85 KDa and 42 KDa, respectively. PPO activities were evaluated at different temperatures and pH values to determine thermal stability as well as the optimal temperature and pH. Moreover, PPO1 and PPO2 were allowed to react with catechol, epigallocatechin (EGC), epigallocatechin gallate (EGCG), l-tyrosine, guaiacol, and pyrogallic acid as enzyme substrates. PPO isozymes were more active with the triphenolic substrate, and PPO2 demonstrated no activity toward guaiacol. PPO1 activity only resulted in the synthesis of simple theaflavin (TF), while PPO2 was able to synthesize four types of theaflavins, particularly theaflavin-3-3'-gallate (TFDG). These data provide insights into the optimum manufacturing conditions for the enzymatic synthesis of theaflavins.
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