抄録
Endo-beta-N-acetylglucosaminidase from Flavobacterium sp. released about 30% of the N-linked sugar chains from the glucose oxidase of Aspergillus niger. To elucidate the role of the carbohydrate moiety, the enzymatic properties of native and carbohydrate-depleted glucose oxidases were compared. It was found that their catalytic activities and thermal and pH stabilities were identical. However, the carbohydrate-depleted glucose oxidase was more rapidly precipitated by the addition of trichloroacetic acid and ammonium sulfate than the native enzyme. These results show that the N-linked sugar chains of the glucose oxidase contributed to the high solubility of the enzyme in water.
本文言語 | 英語 |
---|---|
ページ(範囲) | 460-464 |
ページ数 | 5 |
ジャーナル | Biochemistry and cell biology = Biochimie et biologie cellulaire |
巻 | 67 |
号 | 8 |
DOI | |
出版ステータス | 出版済み - 1月 1 1989 |
外部発表 | はい |
!!!All Science Journal Classification (ASJC) codes
- 生化学
- 分子生物学
- 細胞生物学