摘要
茶树多酚氧化酶(polyphenol oxidase,PPO)对茶产品的品质形成具有重要作用,一直是人们研究的重点,但至今未见体外表达茶树PPO的报道。笔者在原核中表达纯化获得具有催化活性宜红早PPO的基础上,成功表达纯化获得切除转移肽的宜红早PPO成熟蛋白,该蛋白的比活力比全蛋白高约3倍,并发现转移肽对PPO活性具有抑制作用,这为茶树高活性PPO工程蛋白在体外大量制备及应用提供了基础。
Camellia sinensis polyphenol oxdiase （PPO） plays essential roles in the quality formation of tea processing. Despite that it always is a hotspot, there is no report on expressing C. sinensis PPO in vitro. Based on purifying the active Yihongzao PPO with transit-peptide expressed in Escherichia coli, the active mature form was also expressed in E. coli and purified from the inclusion bodies. The specific activity of the mature form was higher about three times than that of PPO with transit-peptide, which suggests that the transit-peptide should restrain the activity of PPO in vivo and in vitro. It is helpful to yield and apply for the C. sinensis engineering PPO with high activity in a large-scale.
出处
《茶叶科学》
CAS
CSCD
北大核心
2010年第2期136-140,共5页
Journal of Tea Science
基金
华中农业大学人才基金项目
关键词
茶
多酚氧化酶
成熟蛋白
原核表达
Camellia sinensis
polyphenol oxidase
mature protein
prokaryotic expression
