For the efficient conversion of L-tyrosine (L-Tyr) to tyrosol
which is an aromatic compound widely used in the pharmaceutical and chemical industries
a novel four-enzyme cascade pathway based on the Ehrlich pathway of
Saccharomyces cerevisiae
was designed and reconstructed in
Escherichia coli
. Then
the expression levels of the relevant enzymes were coordinated using a modular approach and gene duplication after the identification of the pyruvate decarboxylase from
Candida tropicalis
(
Ct
PDC) as the rate-limiting enzymatic step.
In situ
product removal (ISPR) strategy with XAD4 resins was explored to avoid product inhibition and further improve tyrosol yield. As a result
the titer and conversion rate of tyrosol obtained were 35.7 g·L
-1
and 93.6%
respectively
in a 3-L bioreactor. Results presented here provide a potential enzymatic process for industrial production of tyrosol from cheap amino acids.
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Reconstruction of tyrosol synthetic pathways in Escherichia coli
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Related Author
Cui Yang
Xianzhong Chen
Junzhuang Chang
Lihua Zhang
Wei Xu
Wei Shen
You Fan
Huanru Ding
Related Institution
2 School of Biotechnology, Jiangnan University
2 Department of Chemical and Biological Engineering, Zhejiang University
3 School of Biological and Chemical Engineering, Zhejiang University of Science and Technology
4 Department of Chemical Engineering, The University of Utah, Salt Lake City 84102, America