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Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers

[Image: see text] 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,...

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Autores principales: Yamaguchi, Atsushi, Nakayama, Haruna, Morita, Yuko, Sakamoto, Hiroaki, Kitamura, Takeo, Hashimoto, Masayuki, Suye, Shin-ichiro
Formato: Online Artículo Texto
Lenguaje:English
Publicado: American Chemical Society 2020
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7408217/
https://www.ncbi.nlm.nih.gov/pubmed/32775884
http://dx.doi.org/10.1021/acsomega.0c01948
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author Yamaguchi, Atsushi
Nakayama, Haruna
Morita, Yuko
Sakamoto, Hiroaki
Kitamura, Takeo
Hashimoto, Masayuki
Suye, Shin-ichiro
author_facet Yamaguchi, Atsushi
Nakayama, Haruna
Morita, Yuko
Sakamoto, Hiroaki
Kitamura, Takeo
Hashimoto, Masayuki
Suye, Shin-ichiro
author_sort Yamaguchi, Atsushi
collection PubMed
description [Image: see text] 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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spelling pubmed-74082172020-08-07 Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers Yamaguchi, Atsushi Nakayama, Haruna Morita, Yuko Sakamoto, Hiroaki Kitamura, Takeo Hashimoto, Masayuki Suye, Shin-ichiro ACS Omega [Image: see text] 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. American Chemical Society 2020-07-22 /pmc/articles/PMC7408217/ /pubmed/32775884 http://dx.doi.org/10.1021/acsomega.0c01948 Text en Copyright © 2020 American Chemical Society This is an open access article published under an ACS AuthorChoice License (http://pubs.acs.org/page/policy/authorchoice_termsofuse.html) , which permits copying and redistribution of the article or any adaptations for non-commercial purposes.
spellingShingle Yamaguchi, Atsushi
Nakayama, Haruna
Morita, Yuko
Sakamoto, Hiroaki
Kitamura, Takeo
Hashimoto, Masayuki
Suye, Shin-ichiro
Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers
title Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers
title_full Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers
title_fullStr Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers
title_full_unstemmed Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers
title_short Enhanced and Prolonged Activity of Enzymes Adsorbed on TEMPO-Oxidized Cellulose Nanofibers
title_sort enhanced and prolonged activity of enzymes adsorbed on tempo-oxidized cellulose nanofibers
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7408217/
https://www.ncbi.nlm.nih.gov/pubmed/32775884
http://dx.doi.org/10.1021/acsomega.0c01948
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