The realization that microorganisms could live and thrive at temperatures ranging from the freezing point to above the boiling point of water have greatly expanded the range of possible conditions for enzyme catalysis and the identification of modules capable of binding under a variety of extreme conditions. Enzymes from thermophiles have the interesting property that they function optimally at high temperatures. The overall aim of the project is to evolve modules of thermostable glycosyl hydrolases (in particular xylanases) in order to understand and perfect their target specificity and thermostability properties and to employ these modules in biotechnology and bioanalysis. Our studies have focused on a carbohydrate binding module of the xylanase 10A derived from Rhodothermus marinus.
We target genes encoding protein domains with genetic variability, clone the genetic libraries in vectors suitable for subsequent selection of domain variants with superior properties using phage display or array technology. This has allowed us to understand the basic properties of the modules and to eventually evolve reagents with improved properties. Such modules have a great potential for applications concerning the use of plant material as food and feed as well as for the utilization and basic analysis of fibres out of these materials.