β-Galactosidase from Ginkgo biloba seeds active against β-galactose-containing N-glycans: Purification and characterization

M. Ziaur Rahman, Megumi Maeda, Yoshinobu Kimura

Research output: Contribution to journalArticle

2 Citations (Scopus)

Abstract

In this study, we purified an acidic β-galactosidase to homogeneity from Ginkgo biloba seeds (β-Gal'ase Gb-1) with approximately 270-fold purification. A molecular mass of the purified β-Gal'ase Gb-1 was estimated about 35 kDa by gel filtration and 32 kDa by SDS-PAGE under non-reducing condition, respectively. On the other hand, β-Gal'ase Gb-1 produced a single band with a molecular mass of 16 kDa by SDS-PAGE under reducing condition. The N-terminal amino acid sequences of 32 kDa and 16 kDa molecules were the same and identified as H-K-A-N-X-V-T-V-A-F-V-M-T-Q-H-, suggesting that β-Gal'ase Gb-1 may function as a homodimeric structure in vivo. When complex-type N-glycans containing β-galactosyl residues were used as substrates, β-Gal'ase Gb-1 showed substantial activity for β1-4 galactosyl residue and modest activity for β1-3 galactosyl residue with an optimum pH near 5.0. Based on these results, the involvement of β-Gal'ase Gb-1 in the degradation of plant complextype N-glycans is discussed.

Original languageEnglish
Pages (from-to)1464-1472
Number of pages9
JournalBioscience, Biotechnology and Biochemistry
Volume79
Issue number9
DOIs
Publication statusPublished - Jan 1 2015

Keywords

  • Ginkgo biloba
  • Glycosidase
  • N-glycan degradation
  • Plant N-glycan
  • Β-galactosidase

ASJC Scopus subject areas

  • Biotechnology
  • Analytical Chemistry
  • Biochemistry
  • Applied Microbiology and Biotechnology
  • Molecular Biology
  • Organic Chemistry

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