Combinatorial approach to study enzyme/surface interactions

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 immo...

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Bibliographic Details
Published in:Langmuir
Main Authors: Loos, Katja, Kennedy, Scott B., Eidelman, Naomi, Tai, Yian, Zharnikov, Michael, Amis, Eric J., Ulman, Abraham, Gross, Richard A.
Format: Article in Journal/Newspaper
Language:English
Published: 2005
Subjects:
SELF-ASSEMBLED MONOLAYERS
SOL-GEL-MATERIALS
PROTEIN ADSORPTION
X-RAY
HETEROGENEOUS BIOCATALYSTS
ALKANETHIOL MONOLAYERS
POLYMER SURFACE
LIPASE
PHOTOOXIDATION
GOLD
Antarc*
Antarctica
Online Access:https://hdl.handle.net/11370/704aa750-7e71-4458-921d-4458f0ec0feb
https://research.rug.nl/en/publications/704aa750-7e71-4458-921d-4458f0ec0feb
https://doi.org/10.1021/la0469304
Description
Summary: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.

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