ArticleBioresources and bioprocessing2025
Bioactive expression of eukaryotic cytochrome P450 ferulate-5-hydroxylase in Escherichia coli for sustainable synthesis of antioxidant 5-hydroxyferulic acid.
Article in Bioresources and bioprocessing, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.
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2 citing papers in PubMed.
- Systems metabolic engineering of a plasmid-freeSynthetic and systems biotechnology · 2027Article
- Agricultural By-Products as Secondary Risk Matrices: Hazard Occurrence, Contaminant Fate, Mitigation Strategies, and Regulatory Considerations in Food Systems.Comprehensive reviews in food science and food safety · 2026Review
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6 authors.
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Abstract
The eukaryotic cytochrome P450 ferulate-5-hydroxylase (F5H), a membrane-bound protein, plays a critical role in lignin synthesis involved in the biosynthesis of 5-Hydroxyferulic acid (5-HFA) from ferulic acid, with 5-HFA offering enhanced antioxidant properties. However, there is challenging to engineer recombinants for 5-HFA synthesis by expressing F5H in Escherichia coli. In this work, we co-expressed F5H derived from Arabidopsis thaliana (AtF5H) and NADPH-dependent cytochrome P450 reductase (CPR) in E. coli, and successfully synthesized ortho-hydroxylated ferulic acid. Simultaneously, by modifying the N-terminal regions of membrane proteins, we increased the concentration of product 5-HFA to 63.6 mg/L. Ferulic acid, utilized as the substrate, was extracted from discarded agricultural by-products, demonstrating a sustainable approach to valorizing agricultural waste. This work also advances the application of plant-derived membrane-bound proteins for the production of plant secondary metabolites in E. coli.
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