ArticleACS omega2020
Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers.
Article in ACS omega, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
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Who cites it
6 citing papers in PubMed.
- Construction and utilization of FeComputational and structural biotechnology journal · 2025Article
- Cellulose Nanofibrils of High Immunoaffinity for Efficient Enrichment of Small Extracellular Vesicles.Small methods · 2024Article
- Stimuli-Responsive DNA-Based Hydrogels on Surfaces for Switchable Bioelectrocatalysis and Controlled Release of Loads.ACS applied materials & interfaces · 2023Article
- Nanocellulose: Recent Advances Toward Biomedical Applications.Small science · 2023Article
- Nanofiber Carriers of Therapeutic Load: Current Trends.International journal of molecular sciences · 2022Review
- Selective Oxidation of Cellulose-A Multitask Platform with Significant Environmental Impact.Materials (Basel, Switzerland) · 2022Review
Corrections and comments
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Authors and funding
7 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
2,2,6,6-Tetramethylpiperidine-1-oxyl (TEMPO)-oxidized cellulose nanofibers (TOCNs) have a width of about 4 nm and a very large specific surface area. TOCN is a negatively charged bionanomaterial having carboxy groups on the surface and promising physical properties. In particular, TOCN can be used as an adsorbent for biomolecules for biotechnological applications, but the adsorption behavior of biomolecules on the TOCN surface requires investigation. Thus, in this study, we investigated the adsorption behavior of pyrroloquinoline quinone-dependent glucose dehydrogenase (PQQ-GDH) on TOCN and evaluated the activity, structure, and long-term stability of the adsorbed enzyme. Transmission electron microscopy observation revealed that the enzyme was aligned and adsorbed on the TOCNs, and circular dichroism measurements were used to determine the structure of the enzyme adsorbed on TOCN. Interestingly, the adsorbed enzyme showed higher activity after adsorption, resulting in long-term retention of enzyme activity, probably because the stability of PQQ-GDH was improved by adsorption. These results suggest that TOCN is an excellent biomolecule immobilization material. Our results can be used for the development of biomaterials using TOCN as a scaffold for the adsorption of enzymes with increased stability and activity.
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Registered trials
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