BACKGROUND The immobilization of multiple oxidoreductases has attracted a lot of research interest for its industrial application in eco-friendly production. Here, a novel immobilization strategy was developed using manganese ion chelated linear polyethyleneimine as artificial hybrid scaffold that allowed self-assembly of bifunctional oxidoreductase (glycerol dehydrogenase-NADH oxidase) via multipoint coordination interaction. RESULT The immobilization formed a highly ordered polymer-metal-enzyme complex structure shaped like a leaf vein with 200-nm-wide nanowires. Preliminary results showed that the immobilization could not only retain but substantially increased the biological activity of the immobilized enzyme by 8.2-fold. The equilibrium concentration of the reaction product DHA also was increased by 4.5-fold compared with that of the free enzyme, exhibiting higher elimination efficiency of product inhibition compared with other enzyme immobilization strategy using nanoparticles or activated agarose beads. At the same time, linear polyethyleneimine (LPEI)-manganese scaffolds could prevent enzyme subunit disassociation and stabilize the active multimeric form, which improved catalytic condition adaption and thermal stability of target enzyme. CONCLUSION These results indicated a great potential of polymer-metal-enzyme hybrid in the enzyme immobilization and have provided a simple and efficient strategy for the immobilization of multiple oxidoreductases. (c) 2018 Society of Chemical Industry