A Toxin-Antitoxin-Driven Biosensor Platform for the Directed Evolution of d -Allulose 3-Epimerase
Abstract
Biosensor-assisted growth-coupled screening facilitates the directed evolution of enzymes. However, antibiotic resistance-dependent screening tools generally suffer from declining selection pressure. To overcome this limitation, we developed a toxin-antitoxin-based high-throughput screening platform (TASP) for engineering d-allulose 3-epimerase (DAE), driven by a redesigned d-allulose-responsive biosensor (DB). Engineering the pPsiA promoter expanded its dynamic range to 150 mM d-allulose and enhanced signal-to-noise ratio by 14.2-fold. The TASP incorporates the toxin-antitoxin (AtaT-AtaR) as a sustainable and cell-autonomous selection pressure, where mCherry is used as a reporter gene. This design precisely links DAE catalytic activity to cell growth phenotypes, enabling both visual monitoring and quantitative analysis to rapidly identify variants. Using TASP, we identified the mutant M4-2 (W14C/G67A/L151Y/F245 K), which exhibits a 5.2-fold increase in catalytic activity and a 3.5-fold increase in half-life at 60 °C. This work establishes a reliable platform for high-throughput screening of DAE variants and advances the development of growth-coupled selection strategies.
Fields of Study & Subjects
Enzyme Catalysis and Immobilization
Microbial Metabolic Engineering and Bioproduction
Enzyme Production and Characterization
Publication details
- Journal / source
- Journal of Agricultural and Food Chemistry
- Volume
- 74
- Issue
- 9
- Pages
- 7692–7703
- Publication date
- 25 February 2026
- Language
- EN