Integrating microbial cell factory with new-to-nature photobiocatalysis for de novo biosynthesis of d-homotryptophan

Read full text
Authors: Zhiqi Guo, Gengrong Gao, Guangming Xiang, Xiaoxi Yuan, Jinhai Yu, Bin Chen, Xiaoqiang Huang, Hongzhong Lu
Cited by: 1
References: 57

Abstract

Microbial cell factory is a powerful biological tool for synthesizing value-added molecules due to its unmatched sustainability and selectivity. However, the inherent catalytic specificity of natural enzymes limits product diversity. Although photobiocatalysis has expanded enzyme catalytic capabilities, challenges such as laborious enzyme purification, incompatibility with in vivo conditions, and complex unnatural substrate synthesis hinder photobiomanufacturing efforts. Herein, we combine a microbial cell factory with a new-to-nature photobiocatalytic transformation via a modular design that combines aerobic fermentation (Module I) and anaerobic photocatalysis (Module II) to achieve de novo biosynthesis of d-homotryptophan. In Module I, we engineer Escherichia coli equipped with a biosynthetic gene cluster to produce indole-3-acetic acid (IAA) via modifying metabolic flux and multi-copy genetic amplification strategies. In Module II, we develop an efficient synergistic photoredox/enzymatic synthesis of d-homotryptophan from l-serine and IAA by a pyridoxal phosphate (PLP)-dependent tryptophan synthase beta-subunit (TrpB) variant. This work synergistically merges emerging photobiocatalytic reactivity with natural biosynthesis, demonstrating a platform with potential for future biomanufacturing of non-natural products. Microbial cell factories are a powerful tool for synthesizing value-added molecules, but the inherent catalytic specificity of natural enzymes limits product diversity. Here, the authors combine a microbial cell factory with a new-to-nature photobiocatalytic transformation via a modular design that combines aerobic fermentation and anaerobic photocatalysis to achieve de novo biosynthesis of d-homotryptophan.

Fields of Study & Subjects

Enzyme Catalysis and Immobilization Enzyme-mediated dye degradation Steroid Chemistry and Biochemistry

Publication details

Journal / source
Nature Communications
Publisher
Springer Science and Business Media LLC
Volume
17
Issue
1
Publication date
11 June 2026
Language
EN