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Combinatorial approach to study enzyme/surface interactions.

Katja Loos·Scott B Kennedy·Naomi Eidelman·Yian Tai·Michael Zharnikov·Eric J Amis·Abraham Ulman·Richard A Gross
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Abstract

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 micro-spectroscopy. 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 micro-environments in which the enzyme gets immobilized.

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Combinatorial Chemistry TechniquesEnzymes, ImmobilizedFungal ProteinsGelsKineticsLipaseSiloxanesSpectroscopy, Fourier Transform InfraredSurface PropertiesLetterResearch Support, Non-U.S. Gov't

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Katja Loos, Scott B Kennedy, Naomi Eidelman, Yian Tai, Michael Zharnikov, Eric J Amis, Abraham Ulman, Richard A Gross. 2005-06-07. Combinatorial approach to study enzyme/surface interactions.. https://doi.org/10.1021/la0469304

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