Cadaverine (1,5-pentanediamine) is essential for producing polyamides with excellent thermal stability and mechanical strength, finding applications in engineering plastics and high-performance fibers. While chemical synthesis routes exist, they require harsh reaction conditions and generate significant environmental pollution. Biocatalytic production using lysine decarboxylase offers a greener alternative but has been limited by poor enzyme stability and operational challenges.
Researchers at Jiangnan University employed a sophisticated immobilization strategy to enhance stability and operational longevity. The enzyme-overexpressing E. coli cells were first entrapped in κ-carrageenan gel, which forms strong, rigid structures in the presence of potassium ions. To prevent cell leakage, the gel was crosslinked with polyethylenimine (PEI). The positively charged PEI binds electrostatically to the negatively charged sulfate groups on carrageenan chains, reinforcing the gel network. In a 100-mL packed-bed reactor, the immobilized catalyst operated continuously for 8 days, achieving a cadaverine titer of 112 g/L, and a productivity of 44.8 g cadaverine/g_DCW/h, which is 2.3-fold higher than that of the free-cell batch process within this study.
The study addresses a critical bottleneck in the two-step biocatalytic route to cadaverine, where lysine is first produced by fermentation and then converted to cadaverine by enzymatic decarboxylation. While this route achieves higher overall yields than direct fermentation, the efficiency of the decarboxylation step has been limited by catalyst stability and recovery.
The work entitled “Continuous cadaverine production using κ-carrageenan/polyethylenimine-immobilized cells with exceptional catalytic performance” was published on Systems Microbiology and Biomanufacturing (published on Mar. 17, 2026).
DOI：10.1007/s43393-026-00442-y