Biochemical and biophysical characterization of novel GH10 xylanase prospected from a sugar cane bagasse compost-derived microbial consortia

• Published in: International journal of biological macromolecules 2018-04, Vol.109, p.560-568
• Main Authors: Evangelista, Danilo Elton, Kadowaki, Marco Antonio Seiki, Mello, Bruno Luan, Polikarpov, Igor
• Format: Article
• Language: English
• Subjects: Biochemical characterization; Compost-derived enzyme; GH10; SAXS; β-1,4-xylanase
• ISSN: 0141-8130; 1879-0003
• DOI: 10.1016/j.ijbiomac.2017.12.099

•Environmental awareness drives us to development innovative technologies aiming for production of renewable energy and green products.•Xylanases play an important role in hydrolyzing the glycosidic bonds of xylan, the major component of hemicellulose.•Here, we report a novel GH10-xylanase (Xyn10) identified in the metatranscriptome of sugar cane bagasse compost-derived microbial consortia.•Xyn10 was cloned, expressed, purified, biochemically and biophysically characterized. Environmental issues are promoting the development of innovative technologies for the production of renewable energy and “green products” from plant biomass residues. These technologies rely on the conversion of the plant cell wall (PCW) polysaccharides into simple sugars, which involve synergistic activities of different PCW degrading enzymes, including xylanases; these are widely applied in food and feed sectors, paper and textile industries, among others. We cloned, expressed and biochemically characterized a novel xylanase (Xyn10) from the GH10 identified in a metatranscriptome of compost-derived microbial consortia and determined its low-resolution SAXS molecular envelope in solution. Our results reveal that Xyn10 is a monomeric flexible globular enzyme, with high stability with a broad pH range from 4 to 10 and optimal activity conditions at pH 7 and 40 °C. Only 10% of activity loss was observed after the enzyme was incubated for 30 h at 40 °C with a pH ranging from 5 to 10. Moreover, Xyn10 maintained 100% of its initial activity after incubation for 120 h at 40 °C and 51% after incubation for 24 h at 50 °C (pH = 7.0). Xyn10 shows endocatalytic activity towards xylan and arabinoxylan, liberating xylose, xylobiose, 1,2-α-d-methylglucuronic acid decorated xylotriose, and 1,3-α-l-arabinofuranose decorated xylobiose and xylotriose oligosaccharides.