A novel GH10 xylanase Xyn13-3 from alkaline soil: Gene cloning and heterogenous expression

Abstract

Xylanase, as critical hemicellulose degrading enzyme, it could degrade xylan into oligosaccharides and has been widely used in medicine, paper-making, animal forage, marine functional foods and textile industry. So exploring new xylanase with excellent enzymatic characteristic will be benefit for improving production efficiency and reducing cost. In this study, a novel xylanase of family 10 (Xyn13-3) was obtained from the genomic DNA of alkaline soil by touchdown-PCR and thermal asymmetric interlaced (TAIL) PCR methods, which shares the highest identity (61%) with the reported GH10 xylanase (XP_018659952.1) in GenBank database. Xyn13-3 contained a catalytic motif of GH10 (339 residues). The recombinant plasmid pPIC9-Xyn13-3 was constructed and the recombinant protein was successfully expressed in Pichia pastoris GS115. The special activity of recombinant xylanase was 135.24 U/mg. Exploring the use of novel enzymes from different organisms, with distinct characteristics, could contribute to the development of a highly efficient system for lignocellulose conversion.