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Peptide-N4-( N -acetyl-β-glucosaminyl) asparagine amidases [PNGases (peptide  N -glycosidases),  N -glycanases, EC 3.5.1.52] are essential tools in the release of  N -glycans from glycoproteins. We hereby report the discovery and characterization of a novel bacterial  N -glycanase from  Terriglobus roseus  with an extremely low pH optimum of 2.6, and annotated it therefore as PNGase H + . The gene of PNGase H +  was cloned and the recombinant protein was successfully expressed in  Escherichia coli.  The recombinant PNGase H +  could liberate high mannose-, hybrid- and complex-type  N -glycans including core α1,3-fucosylated oligosaccharides from both glycoproteins and glycopeptides. In addition, PNGase H +  exhibited better release efficiency over  N -glycans without core α1,3-fucose compared with PNGase A. The facile expression, non-glycosylated nature, unusual pH optimum and broad substrate specificity of this novel type of  N -glycanase makes recombinant PNGase H +  a versatile tool in  N -glycan analysis.

Discovery and characterization of a novel extremely acidic bacterial N-glycanase with combined advantages of PNGase F and A