Scientists from the University of Florida (UF, United States) report that enzymes found in termite salivary tissues may be able to accomplish the degradation of lignin in lignocellulosic biomass at room temperature. Lignin is the tough molecular wrapping around the cellulose and hemicellulosic  fibers in plant biomass. In the production of "cellulose-ethanol" from "second-generation" lignocellulosic feedstocks, lignin is usually removed by extreme thermochemical methods (high temperature, strong chemicals), so that cellulose in the biomass can be made readily accessible for further processing into ethanol. The finding by the UF researcher is significant, because the mild enzymatic conditions for lignin degradation may lower the (delignification) pretreatment cost of cellulose ethanol production. The paper (published in the Insect Biochemistry and Molecular Biology Journal, URL above) says that the enzymes "are evolutionarily distinct, host-derived, produced in the salivary gland, secreted into the foregut, bind copper, and play a role in lignocellulose digestion". The results may "contribute to a better understanding of termite digestion and gut physiology, and will assist future translational studies that examine the contributions of individual termite enzymes in lignocellulose digestion".