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Carbon Nanotubes as Supports for Inulinase Immobilization

The commercial inulinase obtained from Aspergillus niger was non-covalently immobilized on multiwalled carbon nanotubes (MWNT-COOH). The immobilization conditions for the carbon nanotubes were defined by the central composite rotational design (CCRD). The effects of enzyme concentration (0.8%–1.7% v...

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Autores principales: Garlet, Tais B., Weber, Caroline T., Klaic, Rodrigo, Foletto, Edson L., Jahn, Sergio L., Mazutti, Marcio A., Kuhn, Raquel C.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2014
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270940/
https://www.ncbi.nlm.nih.gov/pubmed/25225722
http://dx.doi.org/10.3390/molecules190914615
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author Garlet, Tais B.
Weber, Caroline T.
Klaic, Rodrigo
Foletto, Edson L.
Jahn, Sergio L.
Mazutti, Marcio A.
Kuhn, Raquel C.
author_facet Garlet, Tais B.
Weber, Caroline T.
Klaic, Rodrigo
Foletto, Edson L.
Jahn, Sergio L.
Mazutti, Marcio A.
Kuhn, Raquel C.
author_sort Garlet, Tais B.
collection PubMed
description The commercial inulinase obtained from Aspergillus niger was non-covalently immobilized on multiwalled carbon nanotubes (MWNT-COOH). The immobilization conditions for the carbon nanotubes were defined by the central composite rotational design (CCRD). The effects of enzyme concentration (0.8%–1.7% v/v) and adsorbent:adsorbate ratio (1:460–1:175) on the enzyme immobilization were studied. The adsorbent:adsorbate ratio variable has positive effect and the enzyme concentration has a negative effect on the inulinase immobilization (U/g) response at the 90% significance level. These results show that the lower the enzyme concentration and the higher the adsorbent:adsorbate ratio, better is the immobilization. According to the results, it is possible to observe that the carbon nanotubes present an effective inulinase adsorption. Fast adsorption in about six minutes and a loading capacity of 51,047 U/g support using a 1.3% (v/v) inulinase concentration and a 1:460 adsorbent:adsorbate ratio was observed. The effects of temperature on the immobilized enzyme activity were evaluated, showing better activity at 50 °C. The immobilized enzyme maintained 100% of its activity during five weeks at room temperature. The immobilization strategy with MWNT-COOH was defined by the experimental design, showing that inulinase immobilization is a promising biotechnological application of carbon nanotubes.
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spelling pubmed-62709402018-12-27 Carbon Nanotubes as Supports for Inulinase Immobilization Garlet, Tais B. Weber, Caroline T. Klaic, Rodrigo Foletto, Edson L. Jahn, Sergio L. Mazutti, Marcio A. Kuhn, Raquel C. Molecules Article The commercial inulinase obtained from Aspergillus niger was non-covalently immobilized on multiwalled carbon nanotubes (MWNT-COOH). The immobilization conditions for the carbon nanotubes were defined by the central composite rotational design (CCRD). The effects of enzyme concentration (0.8%–1.7% v/v) and adsorbent:adsorbate ratio (1:460–1:175) on the enzyme immobilization were studied. The adsorbent:adsorbate ratio variable has positive effect and the enzyme concentration has a negative effect on the inulinase immobilization (U/g) response at the 90% significance level. These results show that the lower the enzyme concentration and the higher the adsorbent:adsorbate ratio, better is the immobilization. According to the results, it is possible to observe that the carbon nanotubes present an effective inulinase adsorption. Fast adsorption in about six minutes and a loading capacity of 51,047 U/g support using a 1.3% (v/v) inulinase concentration and a 1:460 adsorbent:adsorbate ratio was observed. The effects of temperature on the immobilized enzyme activity were evaluated, showing better activity at 50 °C. The immobilized enzyme maintained 100% of its activity during five weeks at room temperature. The immobilization strategy with MWNT-COOH was defined by the experimental design, showing that inulinase immobilization is a promising biotechnological application of carbon nanotubes. MDPI 2014-09-15 /pmc/articles/PMC6270940/ /pubmed/25225722 http://dx.doi.org/10.3390/molecules190914615 Text en © 2014 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution license (http://creativecommons.org/licenses/by/3.0/).
spellingShingle Article
Garlet, Tais B.
Weber, Caroline T.
Klaic, Rodrigo
Foletto, Edson L.
Jahn, Sergio L.
Mazutti, Marcio A.
Kuhn, Raquel C.
Carbon Nanotubes as Supports for Inulinase Immobilization
title Carbon Nanotubes as Supports for Inulinase Immobilization
title_full Carbon Nanotubes as Supports for Inulinase Immobilization
title_fullStr Carbon Nanotubes as Supports for Inulinase Immobilization
title_full_unstemmed Carbon Nanotubes as Supports for Inulinase Immobilization
title_short Carbon Nanotubes as Supports for Inulinase Immobilization
title_sort carbon nanotubes as supports for inulinase immobilization
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC6270940/
https://www.ncbi.nlm.nih.gov/pubmed/25225722
http://dx.doi.org/10.3390/molecules190914615
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