The knowledge of enzyme kinetics is a crucial parameter for a better understanding of biological processes as well as for the sustainable valorization of biomass. A challenge at interfaces is the complex interplay between the substrate and the enzyme which is often described by Michaelis-Menten kinetics. However, this approach and its determination of the reaction constants is sometimes challenging, particularly if nanoconfined films are of interest. Here, we explore the efficiency of different xylanases on xylan decorated cellulose surfaces using surface plasmon resonance spectroscopy and fast-scan atomic force microscopy. The results show that the reaction cannot be described as Michaleis Menten kinetics and that, dependent on film thickness, different kinetic constants are obtained. The work presented here has implications for the screening of novel xylanses and may be used in the design of microarrays.

Xylanase surface kinetics on xylan decorated cellulose thin films

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