Jia Bao Zhang,Wei Chen,Yong Jun Yang,Zhen Zhen Liu
Genistein, a plant-derived isoflavone with pharmaceutical value, is conventionally obtained through ecologically detrimental extraction processes that rely on large-scale plant harvesting and hazardous solvents. Here, we report the discovery of native genistein biosynthesis in the Paenibacillus jilinensis, which inherently produces 5.7 mg L−1 genistein via the phenylalanine branch of the phenylpropanoid pathway. This pathway mirrors plant flavonoid synthesis but operates through seven bacterial enzymes (PjPAL, PjC4H, Pj4CL, PjCHS, PjCHI, PjIFS, and PjHID) with about 30% sequence homology to the corresponding protein sequences in plants, suggesting evolutionary convergence. To leverage this native capability for sustainable production, we constructed a genome-scale metabolic model (GSMM YPG26) with 1636 reactions and 717 genes to rationally optimize carbon flux. Metabolic engineering elevated genistein titers by 9.3-fold to 52.8 mg L−1 without introducing heterologous plant genes. Green-chemistry analysis further showed that P. jilinensis-ΔGLN achieves 92% less waste than soybean extraction and up to one order of magnitude better than state-of-the-art E. coli and yeast systems. It is crucial that this bacterial platform requires only a basic culture medium for sustained production, and eliminates dependence on medicinal plants. Our findings reveal P. jilinensis as a naturally gifted genistein producer and a green chassis for industrial isoflavone synthesis, aligning with green chemistry goals of waste prevention and bio-based process innovation.
Ke Ma,Wei Chen,Shi-Qing Yan,Zhen-Zhen Liu,Xiao-Qi Lin,Jia-Bao Zhang,Yu Gao,Tao Wang,Jian-Gang Zhang,Yong-Jun Yang
Antimicrobial compounds from the commensal gut microbiota have gained much attention due to their multifunctionality in maintaining good health in the host and killing multidrug-resistant bacteria. Our previous study showed that Paenibacillus jilinensis YPG26 isolated from chicken intestine can antagonize multiple pathogens. Herein, we characterized a bacteriocin-like inhibitory substance, jileicin, purified from P. jilinensis YPG26. Mass spectrometry analysis revealed that jileicin was a protein consisting of 211 amino acids, which showed 88.98% identity to the SIMPL domain-containing protein. The jileicin showed a relatively broad-spectrum antibacterial ability, especially against enterococci. Additionally, the jileicin exhibited good stability after various treatments, no detectable resistance, no significant cytotoxicity, and very low levels of hemolytic activity. The mode of action against Enterococcus faecium demonstrated that jileicin could destroy cell membrane integrity, increase cell membrane permeability, and eventually lead to cell death. Furthermore, jileicin was efficient in controlling the growth of E. faecium in milk. In conclusion, jileicin, as a newly identified antibacterial agent, is expected to be a promising candidate for application in the food, pharmaceutical, and biomedical industries.
危险品化学品经营许可证（带存储）