Format

Send to

Choose Destination
J Agric Food Chem. 2016 May 4;64(17):3380-5. doi: 10.1021/acs.jafc.6b00650. Epub 2016 Apr 21.

Enhancing Biosynthesis of a Ginsenoside Precursor by Self-Assembly of Two Key Enzymes in Pichia pastoris.

Author information

1
State Key Laboratory of Bioreactor Engineering, New World Institute of Biotechnology, East China University of Science and Technology , Shanghai 200237, China.
2
Key Laboratory of Synthetic Biology, Institute of Plant Physiology and Ecology, Shanghai Institutes for Biological Sciences, Chinese Academy of Sciences , Shanghai 200032, China.

Abstract

Ginsenosides from the edible and medicinal plant ginseng have demonstrated various pharmacological activities. However, producing ginsenoside efficiently remains a challenge. Engineering metabolic pathways through protein assembly in yeast is a promising way for ginsenoside production. In the biosynthetic pathway of ginsenosides, dammarenediol-II synthase and squalene epoxidase are two key enzymes that determine the production rate of the dammarane-type ginsenoside precursor dammarenediol-II. In this work, a strategy to enhance the biosynthesis of dammarenediol-II in Pichia pastoris was developed by the self-assembly of the two key enzymes via protein-protein interaction. After being modified by interacting proteins, the two enzymes were successfully co-localized, resulting in a 2.1-fold enhancement in dammarenediol-II yields.

KEYWORDS:

Pichia pastoris; dammarenediol-II; ginsenosides; self-assembly

PMID:
27074597
DOI:
10.1021/acs.jafc.6b00650
[Indexed for MEDLINE]

Supplemental Content

Full text links

Icon for American Chemical Society
Loading ...
Support Center