Elucidation of the role of sugar chains in glucoamylase using endo-β-N-acetylglucosaminidase from Flavobacterium sp.

Kaoru Takegawa, Masaki Inami, Kenji Yamamoto, Hidehiko Kumagai, Tatsurokuro Tochikura, Bunzo Mikami, Yuhei Morita

研究成果: Contribution to journalArticle査読

28 被引用数 (Scopus)

抄録

Endo-β-N-acetylglucosaminidase (glycopeptide-d-mannosyl-N4-(N-acetyl-d-glucosaminyl)2-asparagine1,4-N-acetyl-β-glucosaminohydrolase, EC 3.2.1.96), homogenized from the culture filtrate of Flavobacterium sp., could liberate about 50% of the sugar chains from the glucoamylase of Rhizopus niveus. The native and carbohydrate-depleted glucoamylases were compared in their various enzymatic properties. It was found that they were identical in their catalytic activities. However, the carbohydrate-depleted glucoamylase was less thermally stable than the native glucoamylase. Moreover, the carbohydrate-depleted glucoamylase was more sensitive to proteinases such as pronase, subtilisin and trypsin. These results suggest that the sugar chains of the glucoamylase contribute to the high stability of the enzyme. However, circular dichroism spectra of the native and carbohydrate-depleted glucoamylase were found to be identical.

本文言語英語
ページ(範囲)187-193
ページ数7
ジャーナルBiochimica et Biophysica Acta (BBA)/Protein Structure and Molecular
955
2
DOI
出版ステータス出版済み - 7 20 1988
外部発表はい

All Science Journal Classification (ASJC) codes

  • 生物理学
  • 構造生物学
  • 生化学
  • 分子生物学

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