Abstract: Clostridium thermocellum has been studied as a model organism that is highly specialized in cellulose deconstruction, and in secretion of cellulolytic enzymes organized into an enzymic complex known as the cellulosome. Lignocellulose deconstruction requires a variety of enzymes, including cellulases, hemicellulases, and pectin-degrading enzymes. In addition to cellulase production, C. thermocellum is an efficient producer of xylanases, which can be found as cellulosome components. These enzymes work in synergy with cellulosomal cellulases to effect complete hydrolysis of holocellulose. Xylan-degrading enzymes are highly sought after for industrial applications, including production of biofuels and paper and pulp. In this context, industrial processes could take advantage of the properties of xylanases derived from C. thermocellum, such as thermal stability and specificity for different xylans. In this review, we describe the potential of C. thermocellum in degrading xylan-based polymers by reviewing the main findings regarding xylan-degrading enzymes synthesized by this organism, including the repertoire of substrates that can be synergically hydrolyzed through the action of distinct glycoside hydrolase (GH) families. Features of these enzymes, including their modular architecture, specificity for different xylan polymers, and biochem. properties, are discussed. Custom-tailored xylanosomes employing the xylan specificity of GH from families 30, 5, 10, and 11 are proposed as enzymic machinery for more efficient hemicellulose deconstruction.