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 |
|---|---|
| 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 |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
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Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger. / Takegawa, Kaoru; Fujiwara, K.; Iwahara, S.; Yamamoto, K.; Tochikura, T.
In: Biochemistry and cell biology = Biochimie et biologie cellulaire, Vol. 67, No. 8, 01.01.1989, p. 460-464.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger.
AU - Takegawa, Kaoru
AU - Fujiwara, K.
AU - Iwahara, S.
AU - Yamamoto, K.
AU - Tochikura, T.
PY - 1989/1/1
Y1 - 1989/1/1
N2 - 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.
AB - 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.
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UR - http://www.scopus.com/inward/citedby.url?scp=0024707969&partnerID=8YFLogxK
U2 - 10.1139/o89-072
DO - 10.1139/o89-072
M3 - Article
VL - 67
SP - 460
EP - 464
JO - Biochemistry and Cell Biology
JF - Biochemistry and Cell Biology
SN - 0829-8211
IS - 8
ER -