Purification and Characterization of β-N-Acetylglucosaminidase from Alteromonas sp.Strain O-7

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概要

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• β-N-Acetylglucosaminidase (EC 3.2.1.30) was purified from the outer membrane of a marine bacterium, Alteromonas sp. strain O-7. The enzyme (GlcNAcase A) was purified by successive column chromatographies. The purified enzyme was found to be homogeneous on sodium dodecyl sulfate polyacrylamide gel electrophoresis. The molecular mass and pI of GlcNAcase A were 92 kDa and 4.9, respectively. The optimum pH and temperature were 6.0-7.0and 45℃, respectively. GlcNAcase A was stable up to 40℃ at pH 7.0, and hydrolyzed N-acetylchitooligosaccharides from dimer to hexamer. The amino-terminal 16 amino acid residues of GlcNAcase A were sequenced.

• 社団法人日本農芸化学会の論文
• 1995-06-23

著者

• Inamori Yoshihiko

  Department Of Microbiology Osaka University Of Pharmaceutical Sciences

• TSUJIBO Hiroshi

  Osaka University of Pharmaceutical Sciences

• MIYAMOTO Katsushiro

  Osaka University of Pharmaceutical Sciences

• INAMORI Yoshihiko

  Osaka University of Pharmaceutical Sciences

• IMADA Chiaki

  Institute of Microbial Chemistry

• OKAMI Yoshiro

  Institute of Microbial Chemistry

• Fujimoto Kazuhiro

  Osaka University Of Pharmaceutical Sciences

• Okami Y

  Institute Of Microbial Chemistry

• Imada C

  Graduate School Of Marine Science And Technology Tokyo University Of Marine Science And Technology

• Kimura Yoshihisa

  Osaka University of Pharmaceutical Sciences

• Miyamoto K

  Central Research Laboratories Osaka University Of Pharmaceutical Sciences

• Inamori Yoshihiko

  Osaka College Of Pharmacy

• Miyamoto Katsushiro

  Osaka Univ. Of Pharmaceutical Sciences

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