Transcriptomic analysis identifies a furfural reductase in Lactiplantibacillus plantarum

• Published in: Biocatalysis and agricultural biotechnology 2024-12, Vol.62, Article 103449
• Main Authors: Surve, Sarvesh V., Rajkhowa, Riyakshi, Vyas, Parin, Vijayvargiya, Monty, Khare, Satyajeet, Kulkarni, Ram
• Format: Article
• Language: English
• Subjects: Dehydrogenases; Furan aldehydes; Lactobacillus; Lignocellulose; Transcriptome
• ISSN: 1878-8181; 1878-8181
• DOI: 10.1016/j.bcab.2024.103449

Lignocellulosic biomass (LCB) is a promising feedstock for producing value-added chemicals, with Lactiplantibacillus plantarum emerging as a potential cell factory due to its ability to metabolize lignocellulosic sugars. However, LCB preprocessing generates toxic compounds, such as furfural and 5-hydroxymethylfurfural (HMF), which inhibit microbial growth. In this study, we explored the transcriptional responses of L. plantarum JGR2 to furfural, HMF, and their combination using RNA-seq analysis. Notably, the pyr operon, involved in pyrimidine metabolism, was downregulated across all treatments, while 1,3-propanediol dehydrogenase (dhaT) was upregulated under furfural exposure. Recombinant E. coli overexpressing DhaT successfully converted furfural into the less toxic furfuryl alcohol. The identification of DhaT as a furfural reductase, along with the transcriptomic data on L. plantarum's response to furan aldehydes, can guide the development of LCB-driven L. plantarum as a novel microbial cell factory. [Display omitted] •Transcriptional profiling of furfural and HMF-exposed L. plantarum was performed.•Data suggests downregulation of nucleotide metabolism related pyr operon.•Upregulation of dhaT was observed upon furfural exposure.•Recombinant E. coli expressing DhaT shows about 7 folds higher furfural conversion.•First report of furfural dehydrogenase activity in lactobacilli.