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Combinatorial Approach To Study Enzyme/Surface Interactions

2005; American Chemical Society; Volume: 21; Issue: 12 Linguagem: Inglês

10.1021/la0469304

1520-5827

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

Biotin and Related Studies

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.