Researchers have recently isolated the same cellulase enzyme from a number of strains of archaeabacteria found in a hot spring in Nevada. The enzyme is able to catalyze the breakdown of cellulose to glucose at high temperatures (above 100 degrees C), and function under a wide range of harsh conditions including the presence of detergents, high salinity, and high ionic content.
"The tight structure of lignocellulose is primarily responsible for its inherent stability and strength but presents a barrier to efficient hydrolysis, a significant problem when considering lignocellulose for biofuel production. Consequently, cellulosic biomass must first be subjected to pretreatment to increase the accessible surface area, and undergo either chemical or enzymatic deconstruction to release sugars that can be subsequently fermented to biofuels. Generally, enzymatic deconstruction and hydrolysis occurs slowly under conditions typically around 50 °C and pH 5.0. The conditions of many pretreatment processes are much more extreme, employing high temperatures combined with low or high pH, or steam explosion, for chemical pretreatment of feedstocks...Therefore, thermophilic cellulases have been targets of research to engineer durable enzymes that can withstand harsher conditions." (Graham et al. 2011:2)
"[T]he protein retained activity after boiling...The enzyme was active on a range of high molecular weight carbohydrate substrates containing β-1,4-linked glucose, including CMC, Avicel, and filter paper." (Graham et al. 2011:13)