% IMPORTANT: The following is UTF-8 encoded.  This means that in the presence
% of non-ASCII characters, it will not work with BibTeX 0.99 or older.
% Instead, you should use an up-to-date BibTeX implementation like “bibtex8” or
% “biber”.

@ARTICLE{Ohashi:885457,
      author       = {Ohashi, Takao and Fujisawa, Yu and Hayes, Marc and Misaki,
                      Ryo and Pietruszka, Jörg and Fujiyama, Kazuhito},
      title        = {{T}ransglycosylation toward naringenin-7-{O}-glucoside
                      using an {N}180{H} mutant of {C}oprinopsis cinerea
                      endo-β-{N}-acetylglucosaminidase},
      journal      = {Biochemical and biophysical research communications},
      volume       = {530},
      number       = {1},
      issn         = {0006-291X},
      address      = {Orlando, Fla.},
      publisher    = {Academic Press},
      reportid     = {FZJ-2020-03840},
      pages        = {155 - 159},
      year         = {2020},
      abstract     = {Flavonoids are generally glycosylated, and the glycan
                      moieties of flavonoid glycosides are known to greatly affect
                      their physicochemical and biological properties. Thus, the
                      development of a variety of tools for glycan remodeling of
                      flavonoid glycosides is highly desired. An
                      endo-β-N-acetylglucosaminidase mutant Endo-CC N180H, which
                      is developed as an excellent chemoenzymatic tool for
                      creating sialylglycoproteins, was employed for the
                      glycosylation of flavonoids. Endo-CC N180H transferred the
                      sialyl biantennary glycans from the sialylglyco peptide to
                      pNP-GlcNAc and narigenin-7-O-glucoside. The kinetic
                      parameters of Endo-CC N180H towards SGP and pNP-GlcNAc were
                      determined. Flavonoid glucosides harboring a 1,3-diol
                      structure in the glucose moieties acted as substrates of
                      Endo-CC N180H. We proposed that the sialyl biantennary
                      glycan transfer to the flavonoid by Endo-CC N180H could pave
                      the way for the improvement of the inherent biological
                      functions of the flavonoids and creation of novel flavonoid
                      glycoside derivatives for future human health benefits
                      including foods and drugs.},
      cin          = {IBOC / IBG-1},
      ddc          = {570},
      cid          = {I:(DE-Juel1)IBOC-20090406 / I:(DE-Juel1)IBG-1-20101118},
      pnm          = {581 - Biotechnology (POF3-581)},
      pid          = {G:(DE-HGF)POF3-581},
      typ          = {PUB:(DE-HGF)16},
      pubmed       = {32828279},
      UT           = {WOS:000565184300025},
      doi          = {10.1016/j.bbrc.2020.06.128},
      url          = {https://juser.fz-juelich.de/record/885457},
}