TY  - JOUR
AU  - Ohashi, Takao
AU  - Fujisawa, Yu
AU  - Hayes, Marc
AU  - Misaki, Ryo
AU  - Pietruszka, Jörg
AU  - Fujiyama, Kazuhito
TI  - Transglycosylation toward naringenin-7-O-glucoside using an N180H mutant of Coprinopsis cinerea endo-β-N-acetylglucosaminidase
JO  - Biochemical and biophysical research communications
VL  - 530
IS  - 1
SN  - 0006-291X
CY  - Orlando, Fla.
PB  - Academic Press
M1  - FZJ-2020-03840
SP  - 155 - 159
PY  - 2020
AB  - 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.
LB  - PUB:(DE-HGF)16
C6  - 32828279
UR  - <Go to ISI:>//WOS:000565184300025
DO  - DOI:10.1016/j.bbrc.2020.06.128
UR  - https://juser.fz-juelich.de/record/885457
ER  -