Thermoascus aurantiacus is a thermophilic fungus in Eurotiales that has been examined extensively for its ability to secrete large amounts of thermostable enzymes for the depoymerization of cellulose and hemicellulose from plant biomass (Biotechnology for Biofuels, 2012, 5, 54). T. aurantiacus has been a key source of glycoside hydrolase family 61 proteins, which function as polysaccharide monooxygenases and complement the well-studied hydrolytic depolymerization enzymes. Detailed characterization of T. aurantiacus GH61 has demonstrated that it has a copper-containing active site with an unusual methylated histidine bound to the copper (PNAS, 2011, 108, 15079). Sequencing of T. aurantiacus will provide key insights into the expression of these important polysaccharide deconstructing enzymes and allow T. aurantiacus to be a used as platform for the production of thermophilic enzymes.
