This article describes a new strategy for coupling the enzyme horseradish peroxidase to a two-component polyurethane (2C-PUR) coating. A stable polymer conjugate was achieved by combining the enzyme and the 2C-PUR coating which was modified with poly(dimethylsiloxane) (PDMS), located at the surface. An atmospheric pressure plasma jet system was used to convert alkyl groups from the PDMS into polar silanol functionalities. This conversion was proven by X-ray photoelectron spectroscopy and dynamic contact angle measurements. In addition, the stability of the activated 2C-PUR surface containing silanol groups was determined by measuring the contact angle as a function of time. Compared to the non-modified 2C-PUR systems the one with PDMS displayed a higher stability over a time period over 28 h. In a silanization process the coating was treated with (3-aminopropyl) trimethoxysilane and the enzyme was subsequently immobilized to the coating via the cross linker glutaraldehyde to receive new biomimetic catalytic/enzymatic functions. The chemical immobilization (chemisorption) of the enzyme to the surface showed statistically significant higher biological activity as compared to references samples without using a cross linker (physisorption). The presented technique offers the opportunity to design new and smart multifunctional surface coatings which employ biomimetic capabilities. (C) 2013 Elsevier B.V. All rights reserved.