Abstract
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.
Original language | English |
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Pages (from-to) | 460-464 |
Number of pages | 5 |
Journal | Biochemistry and cell biology = Biochimie et biologie cellulaire |
Volume | 67 |
Issue number | 8 |
DOIs | |
Publication status | Published - Jan 1 1989 |
Externally published | Yes |
All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology