Author

D. Cai

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Jul 2026

Development of a bifunctional dynamic control system for effective product synthesis in Bacillus licheniformis DW2.

Bacillus licheniformis DW2 has emerged as a promising microbial chassis for biosynthesis of industrial enzymes, lipopeptides and biochemicals. However, the lack of dynamic control tools to date has limited its expansion in basic research and industrial applications. Here, a well- performing bifunctional dynamic control system was developed for the dynamic up- and down- regulation of genes, as well as the effective biosynthesis of poly-γ-glutamic acid (γ-PGA). Firstly, a dynamic turn-on module was developed in B. licheniformis DW2, including an artificially designed broad-range regulated xylose-inducible expression system with a regulation range of 1.03 ∼ 352.37-fold, and an artificially designed highly sensitive IPTG-inducible expression system that can respond to 0.001 mM IPTG. Subsequently, a dynamic turn-off module based on the ClpXP protease was developed, which could regulate the degradation efficiency of target protein by selecting different ssrA tags. Then, a bifunctional dynamic control system based on the coupling of LacI and ClpXP was established in B. licheniformis for the first time, through combining the dynamic turn- on and off modules, which realized the dynamic up- and down- regulation of the expression of rfp and gfp genes simultaneously. Finally, it was successfully applied to dynamically optimize the metabolic flux of γ-PGA, increasing the yields of γ-PGA by 33.51 %. This work not only developed a well-performance bifunctional dynamic control tool for gene expression regulation, but also offered a strong support for the efficient production of diversified products by B. licheniformis.

Y. Rao, Jiaqi Wang, Junyan Liu et al. · Bioresource Technology · 0 citations

Open access Aug 2026

System reconstruction of Bacillus licheniformis for efficient expression of alkaline protease

Industrial enzymes are widely used in diverse applications, but low productivity limits their further widespread utilization. This research aimed to develop high-performance alkaline protease (AprE) expression strains of Bacillus licheniformis through element optimization and modular engineering. Firstly, the aprE gene expression cassette was systematically optimized through element engineering. To minimize host background interference, five large gene fragments were deleted from the genome of B. licheniformis DW2. This expression cassette and genome-reduced strain resulted in 5.77-, 4.84- and 1.31-fold increases in the activities of alkaline protease, nattokinase and chitinase, respectively. Crucially, metabolomics analysis then served as the pivotal discovery tool, revealing that high expression of AprE was constrained by insufficient precursor amino acids and excessive metabolic overflow. Subsequently, the amino acid biosynthesis, energy metabolism, overflow metabolism, and cell membrane/wall modules of the strain were successively modified. The final AprE expression host DM6E10 achieved a remarkable enzyme activity of 34,343 U/mL, with a maximum activity of 107,100 U/mL in a 5-L bioreactor. This study built an efficient cell factory for AprE production and provided insights for the optimization of other protein expression hosts.

Qing Zhang, Mengyuan Zhang, Zhihao Zhu et al. · Synthetic and Systems Biotec... · 0 citations