Structural highlights
FunctionPublication Abstract from PubMedEnzymatic 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 A 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 x 3 (from beechwood glucuronoxylan) and a range of decorated xylooligosaccharides (XOS) from rye arabinoxylan, with Ara2 x 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. Transformation of xylan into value-added biocommodities using Thermobacillus composti GH10 xylanase.,Sepulchro AGV, Pellegrini VOA, Briganti L, de Araujo EA, de Araujo SS, Polikarpov I Carbohydr Polym. 2020 Nov 1;247:116714. doi: 10.1016/j.carbpol.2020.116714. Epub , 2020 Jul 3. PMID:32829841[1] From MEDLINE®/PubMed®, a database of the U.S. National Library of Medicine. References
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