title: Combinatorial approach to study enzyme/surface interactions.
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.
authors.forename: Katja
authors.initials: K
authors.lastname: Loos
authors.forename: Scott B
authors.initials: SB
authors.lastname: Kennedy
authors.forename: Naomi
authors.initials: N
authors.lastname: Eidelman
authors.forename: Yian
authors.initials: Y
authors.lastname: Tai
authors.forename: Michael
authors.initials: M
authors.lastname: Zharnikov
authors.forename: Eric J
authors.initials: EJ
authors.lastname: Amis
authors.forename: Abraham
authors.initials: A
authors.lastname: Ulman
authors.forename: Richard A
authors.initials: RA
authors.lastname: Gross
mesh_terms: D020650:Combinatorial Chemistry Techniques / Q000379:methods; D004800:Enzymes, Immobilized / Q000737:chemistry*; D005656:Fungal Proteins; D005782:Gels; D007700:Kinetics; D008049:Lipase / Q000737:chemistry* / Q000502:physiology; D012833:Siloxanes / Q000737:chemistry; D017550:Spectroscopy, Fourier Transform Infrared; D013499:Surface Properties
chemical_list: D004800:Enzymes, Immobilized; D005656:Fungal Proteins; D005782:Gels; D012833:Siloxanes; D008049:Lipase; C431349:lipase B, Candida antarctica