An artificial pathway for trans-4-hydroxy-L-pipecolic acid production from L-lysine in Escherichia coli

Author:

Cheng Jie1,Luo Zhou1,Wang Bangxu12,Yan Lixiu3,Zhang Suyi4,Zhang Jiamin1,Lu Yao2,Wang Wei1

Affiliation:

1. Meat Processing Key Laboratory of Sichuan Province, College of Food and Biological Engineering, Chengdu University , Chengdu , P. R. China

2. College of Biological and Chemical Engineering, Guangxi University of Science and Technology , Liuzhou , P. R. China

3. Chongqing Academy of Metrology and Quality Inspection , Chongqing , P. R. China

4. Luzhou Laojiao Co. , Ltd., Luzhou, Sichuan , P. R. China

Abstract

ABSTRACT Trans-4-hydroxy-L-pipecolic acid (trans-4-HyPip) is a hydroxylated product of L-pipecolic acid, which is widely used in the pharmaceutical and chemical industries. Here, a trans-4-HyPip biosynthesis module was designed and constructed in Escherichia coli by overexpressing lysine α-oxidase, Δ1-piperideine-2-carboxylase reductase, glucose dehydrogenase, lysine permease, catalase and L-pipecolic acid trans-4-hydroxylase for expanding the lysine catabolism pathway. A total of 4.89 g/L of trans-4-HyPip was generated in shake flasks from 8 g/L of L-pipecolic acid. By this approach, 14.86 g/L of trans-4-HyPip was produced from lysine after 48 h in a 5 L bioreactor. As far as we know, this is the first multi-enzyme cascade catalytic system for the production of trans-4-HyPip using E. coli from L-lysine. Therefore, it can be considered as a potential candidate for the industrial production of trans-4-HyPip in microorganisms.

Funder

National Natural Science Foundation of China

Open Funding Project of Meat Processing Key Laboratory of Sichuan Province

Publisher

Oxford University Press (OUP)

Subject

Organic Chemistry,Molecular Biology,Applied Microbiology and Biotechnology,General Medicine,Biochemistry,Analytical Chemistry,Biotechnology

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