Prokaryotic expression and purification of  Camellia sinensis  polyphenol oxidase | Zendy

Liu Jingwei | Zendy; Huang Youyi | Zendy; Ding Jian | Zendy; Liu Cong | Zendy; Xiao Xiudan | Zendy; Ni Dejiang | Zendy

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Prokaryotic expression and purification of Camellia sinensis polyphenol oxidase

Author(s) -

Liu Jingwei,

Huang Youyi,

Ding Jian,

Liu Cong,

Xiao Xiudan,

Ni Dejiang

Publication year - 2010

Publication title -

journal of the science of food and agriculture

Language(s) - English

Resource type - Journals

SCImago Journal Rank - 0.782

H-Index - 142

eISSN - 1097-0010

pISSN - 0022-5142

DOI - 10.1002/jsfa.4111

Subject(s) - polyphenol oxidase , camellia sinensis , catechol , escherichia coli , chemistry , catechol oxidase , polyphenol , biochemistry , enzyme , oxidase test , food science , biology , botany , gene , antioxidant , peroxidase

BACKGROUND: Polyphenol oxidase (PPO) causes the postharvest loss of fruits and vegetables but is also a key factor in the quality development of tea. However, there are no reports on engineered active plant PPO purified from prokaryotic cells. RESULTS: In this study the ppo gene of about 1800 bp from Camellia sinensis cv. Yihongzao was successfully cloned and expressed in Escherichia coli . The PPOs purified from both the soluble fraction and the inclusion bodies showed activity. In addition, 1.0 × 10 −7 mol L −1 Cu 2+ and acidic conditions were found to be favourable for the engineered PPO catalysis of catechol oxidation. CONCLUSION: This paper represents the first report on C. sinensis ppo expression in E. coli and engineered active PPO purification. The results of the study provide a basis for the large‐scale preparation and application of PPO. Copyright © 2010 Society of Chemical Industry

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