Induction and purification of endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae grown in ovalbumin

K. Takegawa, M. Nakoshi, S. Iwahara, K. Yamamoto, T. Tochikura

研究成果: ジャーナルへの寄稿記事

63 引用 (Scopus)

抄録

Arthrobacter protophormiae produced a high level of extracellular endo-β-N-acetylglucosaminidase when cells were grown in a medium containing ovalbumin. The enzyme was incuded by the glycopeptide fraction of ovalbumin prepared by pronase digestion. Production of the enzyme was also induced by glycoproteins such as yeast invertase and bovine ribonuclease B but not by monosaccharides such as mannose, N-acetylglucosamine, and galactose. The enzyme was purified to homogeneity as demonstrated by polyacrylamide gel electrophoresis and has an apparent molecular weight of about 80,000. The enzyme showed a broad optimum pH in the range of pH 5.0 to 11.0. The enzyme hydrolyzed all heterogeneous ovalbumin glycopeptides, although the hydrolysis rates for hybrid type glycopeptides were very low. The substrate specificity of A. protophormiae endo-β-N-acetylglucosaminidase was very similar to that of Endo-C(II) from Clostridium perfringens. Therefore, the enzyme induction by A. protophormiae seems to have a close relation to the substrate specificity of the enzyme.

元の言語英語
ページ(範囲)3107-3112
ページ数6
ジャーナルApplied and environmental microbiology
55
発行部数12
出版物ステータス出版済み - 12 21 1989
外部発表Yes

Fingerprint

Arthrobacter protophormiae
Arthrobacter
Acetylglucosaminidase
ovalbumin
Ovalbumin
purification
enzyme
glycopeptides
Glycopeptides
Enzymes
enzymes
substrate specificity
Substrate Specificity
beta-Fructofuranosidase
N-acetylglucosamine
Pronase
Clostridium perfringens
Enzyme Induction
Acetylglucosamine
ribonucleases

All Science Journal Classification (ASJC) codes

  • Biotechnology
  • Food Science
  • Applied Microbiology and Biotechnology
  • Ecology

これを引用

Induction and purification of endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae grown in ovalbumin. / Takegawa, K.; Nakoshi, M.; Iwahara, S.; Yamamoto, K.; Tochikura, T.

:: Applied and environmental microbiology, 巻 55, 番号 12, 21.12.1989, p. 3107-3112.

研究成果: ジャーナルへの寄稿記事

Takegawa, K. ; Nakoshi, M. ; Iwahara, S. ; Yamamoto, K. ; Tochikura, T. / Induction and purification of endo-β-N-acetylglucosaminidase from Arthrobacter protophormiae grown in ovalbumin. :: Applied and environmental microbiology. 1989 ; 巻 55, 番号 12. pp. 3107-3112.
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abstract = "Arthrobacter protophormiae produced a high level of extracellular endo-β-N-acetylglucosaminidase when cells were grown in a medium containing ovalbumin. The enzyme was incuded by the glycopeptide fraction of ovalbumin prepared by pronase digestion. Production of the enzyme was also induced by glycoproteins such as yeast invertase and bovine ribonuclease B but not by monosaccharides such as mannose, N-acetylglucosamine, and galactose. The enzyme was purified to homogeneity as demonstrated by polyacrylamide gel electrophoresis and has an apparent molecular weight of about 80,000. The enzyme showed a broad optimum pH in the range of pH 5.0 to 11.0. The enzyme hydrolyzed all heterogeneous ovalbumin glycopeptides, although the hydrolysis rates for hybrid type glycopeptides were very low. The substrate specificity of A. protophormiae endo-β-N-acetylglucosaminidase was very similar to that of Endo-C(II) from Clostridium perfringens. Therefore, the enzyme induction by A. protophormiae seems to have a close relation to the substrate specificity of the enzyme.",
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AU - Iwahara, S.

AU - Yamamoto, K.

AU - Tochikura, T.

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N2 - Arthrobacter protophormiae produced a high level of extracellular endo-β-N-acetylglucosaminidase when cells were grown in a medium containing ovalbumin. The enzyme was incuded by the glycopeptide fraction of ovalbumin prepared by pronase digestion. Production of the enzyme was also induced by glycoproteins such as yeast invertase and bovine ribonuclease B but not by monosaccharides such as mannose, N-acetylglucosamine, and galactose. The enzyme was purified to homogeneity as demonstrated by polyacrylamide gel electrophoresis and has an apparent molecular weight of about 80,000. The enzyme showed a broad optimum pH in the range of pH 5.0 to 11.0. The enzyme hydrolyzed all heterogeneous ovalbumin glycopeptides, although the hydrolysis rates for hybrid type glycopeptides were very low. The substrate specificity of A. protophormiae endo-β-N-acetylglucosaminidase was very similar to that of Endo-C(II) from Clostridium perfringens. Therefore, the enzyme induction by A. protophormiae seems to have a close relation to the substrate specificity of the enzyme.

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