Fig. 2: CAHB mechanism of laccase immobilization on Cellulose-DNA hydrogels.

a Correlation between the amount of laccase immobilized on Cellulose-DNA hydrogels and solution pH changes before and after laccase immobilization. b Illustration of the suggested CAHB interaction between laccase and Cellulose-DNA hydrogels. FTIR (c) and ¹H NMR (d) spectra of laccase, Cellulose-DNA hydrogels, and laccase-immobilized Cellulose-DNA hydrogels (including deuteration). e Contribution from different amino acids to H-bond formation between laccase and Cellulose-DNA hydrogels in 100 ns MD simulations. Initial state (f, 0 ns), 17 ns (g), 23 ns (h), 35 ns (i), 41 ns (j), 77 ns (k), and the final equilibrium state (l, 100 ns) of the H-bond interaction between Cellulose-DNA hydrogels and laccase by MD simulations. The gray wireframe molecular structure is the water molecule. Application of the CAHB strategy for enzyme immobilization is conditional (i.e., |∆pK_a| or |∆PZC | <~5.0). Both purified and impure enzymes can theoretically be used, as long as the enzyme surface exposes functional groups that can meet the requirements for CAHB formation. In practical applications, it may be necessary to balance the cost and contaminant treatment efficiency of the final product, depending on the specific context and requirements. In (a), data are presented as mean from three replicates (n = 3).