ArticleEngineering in life sciences2018
Assembly of graphene oxide-formate dehydrogenase composites by nickel-coordination with enhanced stability and reusability.
Article in Engineering in life sciences, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 3 papers.
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Who cites it
3 citing papers in PubMed.
- Enzyme Immobilization on Nanomaterials and Their Applications.Materials (Basel, Switzerland) · 2025Review
- Mechanistic Aspects for the Modulation of Enzyme Reactions on the DNA Scaffold.Molecules (Basel, Switzerland) · 2022Review
- Immobilization of formate dehydrogenase on polyethylenimine-grafted graphene oxide with kinetics and stability study.Engineering in life sciences · 2020Article
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6 authors.
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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.
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