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Surface immobilization strategies for tyrosinase as biocatalyst applicable to polymer network synthesis

Published online by Cambridge University Press:  11 December 2018

Christian Wischke ,
Elen Bähr ,
Miroslava Racheva ,
Matthias Heuchel ,
Thomas Weigel  and
Andreas Lendlein
Christian Wischke
Affiliation:
Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Elen Bähr
Affiliation:
Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Miroslava Racheva
Affiliation:
Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Matthias Heuchel
Affiliation:
Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Thomas Weigel
Affiliation:
Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany
Andreas Lendlein*
Affiliation:
Institute of Biomaterial Science and Berlin-Brandenburg Center for Regenerative Therapies, Helmholtz-Zentrum Geesthacht, Kantstr. 55, 14513Teltow, Germany Institute of Chemistry, University of Potsdam, Germany
*
*Correspondence: [email protected]
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Abstract

Enzymes have recently attracted increasing attention in material research based on their capacity to catalyze the conversion of polymer-bound moieties for synthesizing polymer networks, particularly bulk hydrogels. In this study, the surface immobilization of a relevant enzyme, mushroom tyrosinase, should be explored using glass as model surface. In a first step, the glass support was functionalized with silanes to introduce either amine or carboxyl groups, as confirmed e.g. by X-ray photoelectron spectroscopy. By applying glutaraldehyde and EDC/NHS chemistry, respectively, surfaces have been activated for subsequent successful coupling of tyrosinase. Via protein hydrolysis and amino acid characterization by HPLC, the quantity of bound tyrosinase was shown to correspond to a full surface coverage. Based on the visualized enzymatic conversion of a test substrate at the glass support, the functionalized surfaces may be explored for surface-associated material synthesis in the future.

Keywords

Raman spectroscopysurface chemistryx-ray photoelectron spectroscopy (XPS)chemical synthesis
Type
Articles
Information
MRS Advances , Volume 3 , Issue 63: International Materials Research Congress XXVII , 2018 , pp. 3875 - 3881
Copyright
Copyright © Materials Research Society 2018 

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