Cloning, characterization and expression of a gene encoding endo-1, 4- β-xylanase from the fungus Termitomyces clypeatus.

Enzymatic degradation of hemi-cellulosic substrates has gained plenty of industrial attentions recently. Complete enzymatic degradation of complex and recalcitrant hemicellulose requires an enzymatic cocktail consisting primarily of endo-1,4-β-xylanase (xyl), β-xylosidase, arabinofuranosidase etc. This article reports, for the first time, the identification, cloning, expression and partial characterization of a potent endo-1,4- β-xylanase gene (pxyl) from the mushroom Termitomyces clypeatus (TC) in E. coli and S. cerevisiae. The cDNA for pxyl was found to be 678 bp that in turn gives rise to a precursor protein (Pxyl) of 225 amino acids long when cloned in prokaryotic expression vector. To characterize additionally, the cDNA was also expressed in S. cerevisiae. Bioinformatics study predicted that the Pxyl contains a 19 amino acid long leader peptide that enables post translational modifications including glycosylation as well as its efficient secretion in the medium. The recombinant protein has been found to be a member of GH11 family containing two distant glutamic acids as catalytic residues. This report describes yet another new and potent source of xylanase for commercial exploitation by industry in future.