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

Research output: Contribution to journalArticle

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 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.

Original languageEnglish (US)
Pages (from-to)5237-5241
Number of pages5
JournalLangmuir
Volume21
Issue number12
DOIs
StatePublished - Jun 7 2005

ASJC Scopus subject areas

  • Materials Science(all)
  • Condensed Matter Physics
  • Surfaces and Interfaces
  • Spectroscopy
  • Electrochemistry

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    Loos, K., Kennedy, S. B., Eidelman, N., Tai, Y., Zharnikov, M., Amis, E. J., Ulman, A., & Gross, R. A. (2005). Combinatorial approach to study enzyme/surface interactions. Langmuir, 21(12), 5237-5241. https://doi.org/10.1021/la0469304