%0 Journal Article
%T Characterization of novel endo-β-N-acetylglucosaminidase from Bacteroides nordii that hydrolyzes multi-branched complex type N-glycans.
%A Bienes KM
%A Tautau FAP
%A Mitani A
%A Kinoshita T
%A Nakakita SI
%A Higuchi Y
%A Takegawa K
%A Bienes KM
%A Tautau FAP
%A Mitani A
%A Kinoshita T
%A Nakakita SI
%A Higuchi Y
%A Takegawa K
%J J Biosci Bioeng
%V 134
%N 1
%D Jul 2022
%M 35484013
%F 3.185
%R 10.1016/j.jbiosc.2022.03.011
%X Endo-β-N-acetylglucosaminidases (ENGases) are enzymes that hydrolyze the N-linked oligosaccharides. Many ENGases have already been identified and characterized. However, there are still a few enzymes that have hydrolytic activity toward multibranched complex-type N-glycans on glycoproteins. In this study, one novel ENGase from Bacteroides nordii (Endo-BN) species was identified and characterized. The recombinant protein was prepared and expressed in Escherichia coli cells. This Endo-BN exhibited optimum hydrolytic activity at pH 4.0. High performance liquid chromatography (HPLC) analysis showed that Endo-BN preferred core-fucosylated complex-type N-glycans, with galactose or α2,6-linked sialic acid residues at their non-reducing ends. The hydrolytic activities of Endo-BN were also tested on different glycoproteins from high-mannose type to complex-type oligosaccharides. The reaction with human transferrin, fetuin, and α1-acid glycoprotein subsequently showed that Endo-BN is capable of releasing multi-branched complex-type N-glycans from these glycoproteins.