The interaction between POZ-M NRs and CODH was further probed by electrophoretic mobility shift assay as shown in Fig. . Negatively charged POZ-M(-) NRs in isolation propagated slower than those NRs with the incubated CODH enzyme. After staining the gel with Coomassie brilliant blue and successive destaining, it reveals that the POZ-M(-) NRs with CODH has a delayed band that arose from the interaction between the two macromolecules. Notably, we have found out that a significant fraction of the sample propagated similar to the bare enzyme which could be attributed to enzyme that was not adsorbed on staining procedure we observed a far fainter band corresponding to free enzyme. This suggests that enzyme adsorbed on the surface of positively charged POZ-M(+) NRs remained in the well due to strong electrostatic interaction with POZ-M(+) NRs. We hypothesize that POZ-M NRs are most likely attracted to the surface of CODH enzyme via a combination of electrostatic interaction, van der Waals and hydrophobic effects.