Chinese Science Bulletin

, Volume 47, Issue 11, pp 915–917 | Cite as

Molecular cloning, in vitro expression and enzyme activity analysis of violaxanthin de-epoxidase from Oryza sauva L.



The violaxanthin de-epoxidase gene was cloned from rice (Oryza sauva subsp japonica). The full length of the cDNA is 1887 bp, encoding a 446-amino acids protein with the transit peptide of 98 amino acids. The bacterial expression vector pET-Rvde was constructed and the expression quantity of the exogenous protein increased with the induction time by 0.4 mmol/L IPTG. Its molecular weight was similar with that of the native VDE. Western blotting indicated that the expressed protein has immunological reaction with the VDE polyclonal antibody. The absorbance spectrum together with xanthophyll pigments quantification by HPLC demonstrated that the expressed VDE has its enzyme activity, which can de-epoxidate violaxanthin into antheraxanthin and zeaxanthin in vitro.


Oryza sativa L. violaxanthin de-epoxidase clone expression enzyme activity 


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Copyright information

© Science in China Press 2002

Authors and Affiliations

  1. 1.Photosynthesis Research Center, Institute of BotanyChinese Academy of SciencesBeijingChina

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