Enzymes from extremophilic microorganisms have unique potential for industrial applications due their inherent stability to temperature, pH and other physical factors that might denature non-extremophilic enzymes.  We have been actively examining novel extremophilic enzymes for a variety of industrial applications. One such application is the bioprocessing of lignocellulosic materials.  Considerable work has been done in recent years on this topic, much of which has concentrated on cellulose hydrolysis.  Less attention has been paid to hemicellulose hydrolysis.  As such, our group has been actively studying hemicellulose degradation by extremophilic bacteria.  The work reported here details initial studies characterizing one hemicellulose degrading enzyme we isolated from a thermophilic bacterium, Alicyclobacillus acidocaldarius, originally cultivated from Nymph Creek in Yellowstone National Park (YNP).  This enzyme, an endo-xylanase, exhibits significant thermal and acid stability with an optimum temperature of 80°C and an optimum pH of 2.  Based on these characteristics, this enzyme promises to play a useful role in acid hydrolysis-based feedstock pretreatment.  We have also characterized a second enzyme, a catalase, from the thermophilic bacterium, Thermus brockianus, that we enriched from a hot pool in YNP.  This enzyme has a temperature optimum of 90°C and an optimum pH range of 8-10.  When immobilized on Eupergit C beads, the catalase remained stable for >35 days as compared to 7 hrs for commercially available catalase from Aspergillus niger.  As such, T. brockianus catalase may be well suited for a variety of industrial uses including both food and pulp processing.