Purification and substrate specificity of a Ginkgo biloba glycosidase active in β-1,2-xylosidic linkage in plant complex type N-glycans

Biosci Biotechnol Biochem. 2013;77(9):1973-6. doi: 10.1271/bbb.130303. Epub 2013 Sep 7.


The β-xylosidase, which is active against plant complex type N-glycans, was purified to homogeneity from Ginkgo biloba seeds. The N-terminal amino acid sequence, G-S-A-A-G-N-R-, of the Ginkgo β-xylosidase (β-Xyl'ase Gb) was consistent with the deduced internal amino acid sequence of an Arabidopsis β-xylosidase (AtBXL1). β-Xyl'ase Gb hydrolyzed the β1-2 xylosyl residue from Xylβ1-2Manβ1-4GlcNAcβ1-4GlcNAc-PA and Xylβ1-2Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc-PA, but not that from Manα1-6(Manα1-3)(Xylβ1-2)Manβ1-4GlcNAcβ1-4(Fucα1-3)GlcNAc-PA.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Amino Acid Sequence
  • Carbohydrate Sequence
  • Ginkgo biloba / enzymology*
  • Molecular Sequence Data
  • Polysaccharides / chemistry*
  • Polysaccharides / metabolism*
  • Protein Binding
  • Substrate Specificity
  • Xylose / metabolism*
  • Xylosidases / chemistry
  • Xylosidases / isolation & purification*
  • Xylosidases / metabolism*


  • Polysaccharides
  • Xylose
  • Xylosidases