Please use this identifier to cite or link to this item: doi:10.22028/D291-28875
Volltext verfügbar? / Dokumentlieferung
Title: Binding Forces of Cellulose Binding Modules on Cellulosic Nanomaterials
Author(s): Griffo, Alessandra
Rooijakkers, Bart J. M.
Hähl, Hendrik
Jacobs, Karin
Linder, Markus B.
Laaksonen, Päivi
Language: English
Title: Biomacromolecules
Volume: 20
Issue: 2
Startpage: 769
Endpage: 777
Publisher/Platform: American Chemical Society (ACS)
Year of Publication: 2019
Publikation type: Journal Article
Abstract: In this study, the interaction forces between different cellulosic nanomaterials and a protein domain belonging to cellulose binding modules family 1 (CBM1) were investigated at the molecular scale. Cellulose binding modules are protein domains found in carbohydrate active enzymes having an affinity toward cellulosic materials. Here, the binding force of a fusion protein containing a cellulose binding module (CBM1) produced recombinantly in E. coli was quantified on different cellulose nanocrystals immobilized on surfaces. Adhesion of the CBM on cellulose with different degrees of crystallinity as well as on chitin nanocrystals was examined. This study was carried out by single molecule force spectroscopy using an atomic force microscope, which enables the detection of binding force of individual molecules. The study contains a preliminary quantification of the interactions at the molecular level that sheds light on the development of new nanocellulose-based nanocomposites with improved strength and elasticity.
DOI of the first publication: 10.1021/acs.biomac.8b01346
Link to this record: hdl:20.500.11880/27756
http://dx.doi.org/10.22028/D291-28875
ISSN: 1525-7797
1526-4602
Date of registration: 12-Sep-2019
Faculty: NT - Naturwissenschaftlich- Technische Fakultät
Department: NT - Physik
Collections:UniBib – Die Universitätsbibliographie

Files for this record:
There are no files associated with this item.


Items in SciDok are protected by copyright, with all rights reserved, unless otherwise indicated.