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https://olympias.lib.uoi.gr/jspui/handle/123456789/13833Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Pavlidis, I. V. | en |
| dc.contributor.author | Vorhaben, T. | en |
| dc.contributor.author | Tsoufis, T. | en |
| dc.contributor.author | Rudolf, P. | en |
| dc.contributor.author | Bornscheuer, U. T. | en |
| dc.contributor.author | Gournis, D. | en |
| dc.contributor.author | Stamatis, H. | en |
| dc.date.accessioned | 2015-11-24T17:33:13Z | - |
| dc.date.available | 2015-11-24T17:33:13Z | - |
| dc.identifier.issn | 0960-8524 | - |
| dc.identifier.uri | https://olympias.lib.uoi.gr/jspui/handle/123456789/13833 | - |
| dc.rights | Default Licence | - |
| dc.subject | lipase | en |
| dc.subject | esterase | en |
| dc.subject | immobilization | en |
| dc.subject | carbon nanotubes | en |
| dc.subject | graphene oxide | en |
| dc.subject | lipase immobilization | en |
| dc.subject | enzyme immobilization | en |
| dc.subject | surface-chemistry | en |
| dc.subject | nanotubes | en |
| dc.subject | stability | en |
| dc.subject | esterases | en |
| dc.subject | proteins | en |
| dc.subject | graphene | en |
| dc.subject | oxide | en |
| dc.title | Development of effective nanobiocatalytic systems through the immobilization of hydrolases on functionalized carbon-based nanomaterials | en |
| heal.type | journalArticle | - |
| heal.type.en | Journal article | en |
| heal.type.el | Άρθρο Περιοδικού | el |
| heal.identifier.primary | DOI 10.1016/j.biortech.2011.11.007 | - |
| heal.identifier.secondary | <Go to ISI>://000305379000027 | - |
| heal.language | en | - |
| heal.access | campus | - |
| heal.recordProvider | Πανεπιστήμιο Ιωαννίνων. Σχολή Θετικών Επιστημών. Τμήμα Μηχανικών Επιστήμης Υλικών | el |
| heal.publicationDate | 2012 | - |
| heal.abstract | In this study we report the use of functionalized carbon-based nanomaterials, such as amine-functionalized graphene oxide (GO) and multi-walled carbon nanotubes (CNTs), as effective immobilization supports for various lipases and esterases of industrial interest. Structural and biochemical characterization have revealed that the curvature of the nanomaterial affect the immobilization yield, the catalytic behavior and the secondary structure of enzymes. Infrared spectroscopy study indicates that the catalytic behavior of the immobilized enzymes is correlated with their alpha-helical content. Hydrolases exhibit higher esterification activity (up to 20-fold) when immobilized on CNTs compared to GO. The covalently immobilized enzymes exhibited comparable or even higher activity compared to the physically adsorbed ones, while they presented higher operational stability. The enhanced catalytic behavior observed for most of the hydrolases covalently immobilized on amine-functionalized CNTs indicate that these functionalized nanomaterials are suitable for the development of efficient nanobiocatalytic systems. (C) 2011 Elsevier Ltd. All rights reserved. | en |
| heal.publisher | Elsevier | en |
| heal.journalName | Bioresour Technol | en |
| heal.journalType | peer reviewed | - |
| heal.fullTextAvailability | TRUE | - |
| Appears in Collections: | Άρθρα σε επιστημονικά περιοδικά ( Ανοικτά) | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| Gournis-2012-Development of effective.pdf | 499.25 kB | Adobe PDF | View/Open Request a copy |
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