Xylanases are glycoside hydrolases (GHs) that can cleave the β-1,4-glycoside linkages in the xylan backbone. They are synthesized by various organisms and exhibit diverse substrate specificities, catalytic mechanisms, and physicochemical properties. Based on the Carbohydrate-Active enZYme (CAZy) database, GH families 5, 7, 8, 10, 11, and 43 are classified as xylanases, of which the endo-type GH11 family is considered a “true xylanase” that specifically recognizes xylan substrates but not cellulose. Xylanases have attracted increasing attention due to their potential for use in various applications. Consequently, the characteristics and structures of xylanase derived from various organisms have been continuously analyzed, with efforts being made to discover new xylanases with novel and superior characteristics.
Thermophilic lignocellulose-degrading bacteria have the natural ability to digest and ferment polysaccharides (i.e., cellulose and hemicellulose) at elevated temperatures and are considered an important source of robust CAZymes. Thermoanaerobacterium saccharolyticum is a thermophilic anaerobic bacterium that grows in a temperature range of 45–70 °C and can ferment various carbohydrates such as starch, xylan, glucose, cellobiose, xylose, arabinose, mannose, and galactose; whereas it cannot degrade crystalline cellulose. In the genome of T. saccharolyticum, three genes (Tsac_0897, Tsac_1459, and Tsac_1460) are annotated as putative endo-xylanases in the UniProt protein database of which Tsac_1459 and Tsac_1460 belong to GH10, while Tsac_0897 belongs to GH11. Here you can see the structure of TsaGH11 endo-1,4-beta-xylanase (PDB code: 8YYO)

Structure rendered with @proteinimaging, post-processed with @stylar.ai_official and depicted with @corelphotopaint

#molecularart ... #xylanase ... #thermophilic ... #xray

Xylanase
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Xylanase

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