Metabolic Engineering of Vitamin C Production in Arabidops

Vitamin C (L-ascorbic acid, AsA) is a compound which provides major nutritional value, both for plants and humans. In this study, three distinct metabolic engineering strategies, including overexpression of biosynthesis enzyme, suppression of catabolism enzyme and switching the sub-cellular localiza...

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Bibliographic Details
Published inBiotechnology and bioprocess engineering pp. 677 - 684
Main Authors Ling Xiao, Ying Xiao, Zinan Wang, Hexin Tan, Kexuan Tang, Lei Zhang
Format Journal Article
LanguageEnglish
Published 한국생물공학회 01.08.2015
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Summary:Vitamin C (L-ascorbic acid, AsA) is a compound which provides major nutritional value, both for plants and humans. In this study, three distinct metabolic engineering strategies, including overexpression of biosynthesis enzyme, suppression of catabolism enzyme and switching the sub-cellular localization of compartment enzyme, were employed to enhance the production of AsA in Arabidopsis thaliana. The results showed that (1) overexpression of L-Galactose-1-P Phosphatase (GalPPase) enhanced AsA content to 3.96 μmol/g FW, which was 1.6-fold more than that in their wild-type (WT) counterparts; (2) RNAi suppression of ascorbate oxidase (AO) resulted in a significant increase of AsA accumulation (0.86 μmol/g FW) in apoplast; (3) both mitochondrion-target and none-target overexpression of L-Galactose dehydrogenase (GalDH) did not significantly promote AsA production compared with WT (1.96 μmol/g), however a dramatic enhancement was observed following infiltration with L-galactono-1, 4-lactone (L-GalL), both in transgenic and WT plants. The best line produced AsA with the content of 3.90 μmol/g FW, which was about 2-fold of that in the untreated control (1.99 μmol/g FW). This study provides new strategies including GalPPase overexpression, AO suppression as well as L-GalL feeding for modern breeding aimed at stimulating the AsA content in plants. KCI Citation Count: 2
Bibliography:G704-000785.2015.20.4.006
ISSN:1226-8372
1976-3816