title: Studies on the cellulose-binding domains adsorption to cellulose.
abstract: Cellulose-binding domains (CBD) are modular peptides, present in many glycanases, which anchor these enzymes to the substrate. In this work, the effect of CBD adsorption on the surface properties of a model cellulose, Whatman CF11, was studied. The methods applied include inverse gas chromatography (IGC), ESCA, X-ray diffraction, and scanning electron microscopy (SEM). The CBD partition affinity (0.85 L/g) was calculated from adsorption isotherms. However, true adsorption equilibrium does not exist, since CBDs are apparently irreversibly adsorbed to the fibers. Both IGC and ESCA showed that fibers with adsorbed CBD have a lower acidic character and also a slightly higher affinity toward aliphatic molecules. This may however be a consequence of an increased surface area, a hypothesis that is supported by microscopic observations. The crystallinity index was not affected by CBD treatment.
authors.affiliation: Centro de Engenharia Biológica - CEB, Largo do Paço, Universidade do Minho, 4710-057 Braga, Portugal.
authors.forename: Ricardo
authors.initials: R
authors.lastname: Pinto
authors.forename: Susana
authors.initials: S
authors.lastname: Moreira
authors.forename: Manuel
authors.initials: M
authors.lastname: Mota
authors.forename: Miguel
authors.initials: M
authors.lastname: Gama
mesh_terms: D000327:Adsorption; D001665:Binding Sites; D002482:Cellulose / Q000737:chemistry*; D002845:Chromatography; D002849:Chromatography, Gas; D003460:Crystallization; D004058:Diffusion; D006026:Glycoside Hydrolases / Q000737:chemistry; D008855:Microscopy, Electron, Scanning; D011485:Protein Binding; D017434:Protein Structure, Tertiary; D013499:Surface Properties; D013816:Thermodynamics; D014961:X-Ray Diffraction
chemical_list: D002482:Cellulose; D006026:Glycoside Hydrolases; C020668:glycanase