Purification and substrate specificity of an endo-β-N-acetylglucosaminidase from pea (pisum sativum) seeds

Yoshinobu Kimura, Koushi Iwata, Yoshiko Sumi, Shigeaki Takagi

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19 Citations (Scopus)


An endo-β-N-acetyIglucosaminidase was purified to homogeneity from the seeds of pea (Pisum sativum). The molecular mass of the purified enzyme was estimated to be 41,669 Da by MALDI-TOF MS analysis and its isoelectric point to be 4.3 by isoelectric focusing. The enzyme was stable at pH 4–7 and at 25–50°C, and had the highest activity toward Man6GlcNAc2-PA at pH around 7.0. Oligomannose type sugar chains (Man9–6GlcNAc2-PA) and a hybrid type sugar chain (GlcNAc1Man5GlcNAc2-PA) were most favored substrates followed by Man5GlcNAc2-PA, Man3GlcNAc2-PA, and GlcNAc2Man3GlcNAc2-PA, but xylose-containing sugar chains (Man4–3Xyl1GlcNAc2-PA and Man3Fuc1Xyl1GlcNAc2-PA) or a biantennary complex type sugar chain (Gal2GlcNAc2Man3GlcNAc2-PA) could not be hydrolyzed by the enzyme. The Km values of the enzyme for Man5GlcNAc2-PA, Man6GlcNAc2-PA, and Man9GlcNAc2-PA were 0.40 mm, 0.25 mm and 0.32 mm, respectively.

Original languageEnglish
Pages (from-to)228-232
Number of pages5
JournalBioscience, Biotechnology and Biochemistry
Issue number2
Publication statusPublished - Jan 1 1996


  • Endo-β-N-acetylglucosaminidase
  • N-linked oligosaccharide
  • Pisum sativum
  • Plant glycoprotein

ASJC Scopus subject areas

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


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