Assembly of graphene oxide-formate dehydrogenase composites by nickel-coordination with enhanced stability and reusability.

ABSTRACT: Featuring unique planar structure, large surface area and biocompatibility, graphene oxide (GO) has been widely taken as an ideal scaffold for the immobilization of various enzymes. In this regard, nickel-coordinated graphene oxide composites (GO-Ni) were prepared as novel supporters for the immobilization of formate dehydrogenase. The catalytic activity, stability and morphology were studied. Compared with GO, the enzyme loading capacity of GO-Ni was enhanced by 5.2-fold, besides the immobilized enzyme GO-Ni-FDH exhibited better thermostability, storage stability and reuse stability than GO-FDH. GO-Ni-FDH retained 40.9% of its initial activity after 3 h at 60°C, and retained 31.4% of its initial relative activity after 20 days' storage at 4°C. After eight times usages, GO-Ni-FDH maintained 63.8% of its initial activity. Mechanism insights of the multiple interactions of enzyme with the GO-Ni were studied, considering coordination bonds, hydrogen bonds, electrostatic forces, coordination bonds, and etc. A practical and simple immobilization strategy by metal ions coordination for multimeric dehydrogenase was developed.

SUBMITTER: Lin P 

PROVIDER: S-EPMC6999310 | biostudies-literature | 2018 May

REPOSITORIES: biostudies-literature