Cloning, expression and hydrolytic characterization of a novel xylanase Nsi Xyn11A from Neurospora sitophila BDJ1I.
The Nsi xyn11A gene, encoding the endo-1,4-β-xylanase Nsi Xyn11A was isolated from genomic DNA of Neurospora sitophila BDJ1I. The open reading frame of the Nsi xyn11A gene was 1131 base pairs long and encoded a polypeptide of 376 amino acids with a calculated molecular mass of 40.7 kDa. The Nsi xyn11A gene was expressed in Escherichia coli and the recombinant enzyme was characterized to evaluate its hydrolytic capacity on lignocellulosic biomass, showing preference on Agave tequilana bagasse. The enzyme Nsi Xyn11A showed an optimal activity at pH 5.5 and 55 °C. Nsi Xyn11A is thermostable as it showed half-lives of more than 2h at 70 and 80 °C and more than 4 h at 50 and 60 °C. This is the first report describing the cloning and expression of an endo-1,4-β-xylanase encoding gene from N. sitophila and the hydrolytic characterization of the new xylanase Nsi Xyn11A. Our study showed that the xylanase Nsi Xyn11A may be suitable for industrial applications in the food and feed industries, or in the pretreatment of lignocellulosic biomass required to improve the yields of fermentable sugars for bioethanol production.
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