6WQW
Thermobacillus composti GH10 xylanase
Summary for 6WQW
Entry DOI | 10.2210/pdb6wqw/pdb |
Descriptor | Beta-xylanase, beta-D-xylopyranose (3 entities in total) |
Functional Keywords | gh 10, glycoside hydrolase, thermobacillus composti, hydrolase |
Biological source | Thermobacillus composti |
Total number of polymer chains | 1 |
Total formula weight | 38744.54 |
Authors | Briganti, L.,Polikarpov, I. (deposition date: 2020-04-29, release date: 2021-04-28, Last modification date: 2023-10-18) |
Primary citation | Sepulchro, A.G.V.,Pellegrini, V.O.A.,Briganti, L.,de Araujo, E.A.,de Araujo, S.S.,Polikarpov, I. Transformation of xylan into value-added biocommodities using Thermobacillus composti GH10 xylanase. Carbohydr Polym, 247:116714-116714, 2020 Cited by PubMed Abstract: Enzymatic transformation of xylans into renewable fuels and value-added products is mediated by xylanases. Here we describe the biochemical and X-ray structural characterization of Thermobacillus composti GH10 xylanase (TcXyn10A) at 2.1 Å resolution aiming to unravel details of its recognition of glucurono- and arabinoxylan at a molecular level. TcXyn10A improves the efficiency of pretreated lignocellulosic biomass hydrolysis by a commercial enzyme cocktail causing a 15.35 % increase in xylose release and 4.38 % glucose release after 24 h of reaction. The enzyme releases predominantly xylobiose and xylotriose, as well as MeGlcA3 × 3 (from beechwood glucuronoxylan) and a range of decorated xylooligosaccharides (XOS) from rye arabinoxylan, with Ara2 × 2 being the major product. The enzyme liberates XOS with the yields of 29.09 % for beechwood glucuronoxylan and 16.98 % for rye arabinoxylan. Finally, TcXyn10A has a high thermal stability, halotolerance, and resistance to ethanol, biochemical properties that can be desirable for a number of industrial applications. PubMed: 32829841DOI: 10.1016/j.carbpol.2020.116714 PDB entries with the same primary citation |
Experimental method | X-RAY DIFFRACTION (2.102 Å) |
Structure validation
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