dc.contributor.author | Nieto-MárquezCalvo, Jorge | |
dc.contributor.author | Elices, Manuel | |
dc.contributor.author | V.Guinea, Gustavo | |
dc.contributor.author | Pérez-Rigueiro, José | |
dc.contributor.author | Arroyo-Hernández, María | |
dc.date.accessioned | 2021-01-26T09:13:20Z | |
dc.date.available | 2021-01-26T09:13:20Z | |
dc.date.issued | 2017 | |
dc.identifier.issn | 0169-4332 | spa |
dc.identifier.uri | http://hdl.handle.net/10641/2192 | |
dc.description.abstract | The interaction between surfaces and biological elements, in particular, proteins is critical for
the performance of biomaterials and biosensors. This interaction can be controlled by
modifying the surface in a process known as biofunctionalization. In this work, the enzyme
lactate dehydrogenase (LDH) is used to study the stability of the interaction between a
functional protein and amine-functionalized surfaces. Two different functionalization
procedures were compared: Activated Vapour Silanization (AVS) and Immersion Silanization
(IS). Adsorption kinetics is shown to follow the Langmuir model for AVS-functionalized
samples, while IS-functionalized samples show a certain instability if immersed in an aqueous
medium for several hours. In turn, the enzymatic activity of LDH is preserved for longer times
by using glutaraldehyde as crosslinker between the AVS biofunctional surface and the enzyme. | spa |
dc.language.iso | eng | spa |
dc.publisher | Applied Surface Science | spa |
dc.rights | Atribución-NoComercial-SinDerivadas 3.0 España | * |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/3.0/es/ | * |
dc.subject | Surface modification | spa |
dc.subject | Activated vapor silanization | spa |
dc.subject | Infrared spectroscopy | spa |
dc.subject | Protein adsorption | spa |
dc.subject | Langmuir model | spa |
dc.title | Stability and activity of lactate dehydrogenase on biofunctional layers deposited by activated vapour silanization (AVS) and immersion silanization (IS). | spa |
dc.type | journal article | spa |
dc.type.hasVersion | SMUR | spa |
dc.rights.accessRights | open access | spa |
dc.description.extent | 966 KB | spa |
dc.identifier.doi | 10.1016/j.apsusc.2017.04.123 | spa |
dc.relation.publisherversion | https://www.sciencedirect.com/science/article/abs/pii/S0169433217311509 | spa |