Loos, K.
, Kennedy, S.
, Eidelman, N.
, Tai, Y.
, Zharnikov, M.
, Amis, E.
, Ulman, A.
and Gross, R.
(2005),
Combinatorial Approach to Study Enzyme/Surface Interactions, Langmuir (Accessed May 11, 2026)
Official websites use .gov
A .gov website belongs to an official government organization in the United States.
Secure .gov websites use HTTPS
A lock (
) or https:// means you’ve safely connected to the .gov website. Share sensitive information only on official, secure websites.
Combinatorial Approach to Study Enzyme/Surface Interactions
Published
Author(s)
K Loos, , , Y Tai, M Zharnikov, , A Ulman, R A. Gross
Abstract
A fast combinatorial approach to access information on the immobilization behavior and kinetics of enzymes on a variation of surfaces is presented. As a test system, Candida Antarctica Lipase B (CAL-B) was immobilized on a self-assembled monolayer (SAM) bearing a gradient of surface energy. The respective immobilization behavior was monitored by FTIR 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 presumably associated with a higher surface roughness of this area resulting in hydrophobic microenviroments in which the enzyme gets immobilized.Citation
Langmuir
Volume
21
Pub Type
Journals
Keywords
Candida Antartica Lipase B, enzyme catalyst, fluorescence activity assay, FTIR-Microspectroscopy, gradient surfaces, immobilization
Citation
Issues
If you have any questions about this publication or are having problems accessing it, please contact [email protected].
Created February 28, 2005, Updated October 12, 2021