Combinatorial Approach To Study Enzyme/Surface Interactions
| Autor: | Eric J. Amis, Richard A. Gross, Katja Loos, Abraham Ulman, Michael Zharnikov, Naomi Eidelman, Yian Tai, S B. Kennedy |
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| Přispěvatelé: | Macromolecular Chemistry & New Polymeric Materials, Polymers at Surfaces and Interfaces, Zernike Institute for Advanced Materials |
| Rok vydání: | 2005 |
| Předmět: |
Siloxanes
PROTEIN ADSORPTION Immobilized enzyme Surface Properties Fungal Proteins SELF-ASSEMBLED MONOLAYERS Spectroscopy Fourier Transform Infrared Monolayer Electrochemistry Surface roughness Combinatorial Chemistry Techniques General Materials Science GOLD Lipase Spectroscopy Chromatography biology POLYMER SURFACE Chemistry Self-assembled monolayer Surfaces and Interfaces Enzymes Immobilized Condensed Matter Physics biology.organism_classification ALKANETHIOL MONOLAYERS Surface energy Kinetics X-RAY biology.protein LIPASE Candida antarctica SOL-GEL-MATERIALS PHOTOOXIDATION HETEROGENEOUS BIOCATALYSTS Gels Protein adsorption |
| Zdroj: | Langmuir, 21(12), 5237-5241. AMER CHEMICAL SOC |
| ISSN: | 1520-5827 0743-7463 |
| Popis: | A fast combinatorial approach to access information about the immobilization behavior and kinetics of enzymes on a variation of surfaces is presented. As a test system, Candida Antarctica Lipase B was immobilized on a self-assembled monolayer bearing a gradient of surface energy. The respective immobilization behavior was monitored by Fourier transform infrared microspectroscopy. In addition, the activity of the immobilized enzyme was monitored over the entire film in real time with a specially developed fluorescence activity assay embedded into a siloxane gel. It was found that the highest amount of active protein was immobilized on the hydrophilic end of the gradient surface. This effect is associated with a higher surface roughness of this area resulting in hydrophobic microenviroments in which the enzyme gets immobilized. |
| Databáze: | OpenAIRE |
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