Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger

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 w...

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Bibliographic Details
Published inBiochemistry and cell biology Vol. 67; no. 8; pp. 460 - 464
Main Authors Takegawa, K, Fujiwara, K, Iwahara, S, Yamamoto, K, Tochikura, T
Format Journal Article
LanguageEnglish
Published Canada 01.08.1989
Subjects
Acetylglucosaminidase - pharmacology
Aspergillus niger
Aspergillus niger - enzymology
Carbohydrate Metabolism
Enzyme Stability
glucose oxidase
Glucose Oxidase - metabolism
Glycosylation
Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
stability
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Summary: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.
ISSN:0829-8211
1208-6002
DOI:10.1139/o89-072