Whole-cell biocatalyst for cadaverine production using stable, constitutive and high expression of lysine decarboxylase in recombinant Escherichia coli W3110

Microbial production of industrial chemicals is a sustainable approach to reduce the dependence on petroleumbased chemicals such as acids, alcohols, and amines, in which the cadaverine is a natural diamide and serves as one of the key monomers for biopolymer production. In this study, the constitutive promoter J23100 driven lysine decarboxylase (CadA) for cadaverine production was established and compared in different Escherichia coli strains. The best chassis designed as JW, expressed the highest amount of CadA by using J23100 promoter, showing stable and high copy numbers (i.e., PCN > 100) when culture in the antibiotic-free medium. JW attained a CadA activity of 167 g-DAP/g-DCW-h and had the maximum biocatalyst of 45.6 g-DCW/L in fed-batch fermentation. In addition, JW was able to convert 2.5 M L-lysine to 221 g/L cadaverine, with 86 % yield and 55.3 g/L-h productivity. The whole-cell biocatalyst could be reused over four times at an average of 97 % conversion when supplied half of fresh cells in the reaction. This work developed a stable, constitutive expression, long-term preservation, high-level expression of CadA for DAP production, and paved an alternative opportunity of bio-nylon for industry in the future.

Automated summary

This study established a stable and high-level expression system for CadA production, achieving high productivity and yield of cadaverine in engineered E. coli strain JW. The whole-cell biocatalyst showed excellent reusability and potential for bio-nylon production in the future.