In-situ-investigation of enzyme immobilization on polymer brushes

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Date
2019
Volume
7
Issue
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Title
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Publisher
Lausanne : Frontiers Media
Abstract

Herein, we report on the use of a combined setup of quartz-crystal microbalance, with dissipation monitoring and spectroscopic ellipsometry, to comprehensively investigate the covalent immobilization of an enzyme to a polymer layer. All steps of the covalent reaction of the model enzyme glucose oxidase with the poly(acrylic acid) brush by carbodiimide chemistry, were monitored in-situ. Data were analyzed using optical and viscoelastic modeling. A nearly complete collapse of the polymer chains was found upon activation of the carboxylic acid groups with N-(3-Dimethylaminopropyl)-N'-ethylcarbodiimide and N-Hydroxysuccinimide. The reaction with the amine groups of the enzyme occurs simultaneously with re-hydration of the polymer layer. Significantly more enzyme was immobilized on the surface compared to physical adsorption at similar conditions, at the same pH. It was found that the pH responsive swelling behavior was almost not affected by the presence of the enzyme. © 2019 Koenig, König, Eichhorn, Müller, Stamm and Uhlmann.

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Keywords
Ellipsometry, Enzyme immobilization, Enzymes, Polymer brushes, Quartz-crystal microbalance, Responsive coatings
Citation
Koenig, M., König, U., Eichhorn, K.-J., Müller, M., Stamm, M., & Uhlmann, P. (2019). In-situ-investigation of enzyme immobilization on polymer brushes. 7. https://doi.org//10.3389/fchem.2019.00101
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License
CC BY 4.0 Unported