Enhancing 10-HDA production of Escherichia coli by heterologous expression of MexHID transporter proteins

TL;DR

Scientists improved the production of 10-HDA, a valuable compound in royal jelly, by engineering bacteria to better export the compound and reduce cell damage.

Contribution

A novel transporter protein from Pseudomonas aeruginosa was used to enhance 10-HDA production in Escherichia coli.

Findings

Using a transporter protein from Pseudomonas aeruginosa improved 10-HDA efflux in E. coli.

The conversion rate of substrate to 10-HDA reached 88.6% with the new method.

10-HDA production reached 0.94 g/L using a replenishment flow-addition technique.

Abstract

10-Hydroxy-2-decenoic acid (10-HDA) is a medium-chain α,β-unsaturated carboxylic acid that exists in royal jelly with terminal hydroxylation. It has a broad market value because of its antibacterial, anti-inflammatory, anti-tumor, anti-radiation, and other active functions. The one-step whole-cell catalytic synthesis of 10-HDA by constructing engineered strains has improved the reaction rate to a certain extent compared with the previous two-step method. However, the accumulation of 10-HDA to a certain concentration in engineered Escherichia coli strains will damage the structure and function of cells and even lead to death; this unique antibacterial and antimicrobial activity seriously constrains the production of 10-HDA. In this study, we mined a transporter protein from Pseudomonas aeruginosa, which possesses the ability to efficiently efflux 10-HDA, and constructed a transporter protein overexpression strain by using the multicopy chromosome integration technique, which further improved the efficiency of product efflux, weakened the feedback inhibition of 10-HDA to a certain degree, and increased the substrate conversion rate to 88.6%. 10-HDA was synthesized up to 0.94 g/L by the replenishment flow-addition technique, providing a simple and efficient pathway for the yield breakthrough of 10-HDA biosynthesis.

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