title: Effect of deglycosylation of N-linked sugar chains on glucose oxidase from Aspergillus niger.
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.
authors.affiliation: Department of Bioresource Science, Faculty of Agriculture, Kagawa University, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Takegawa
authors.forename: K
authors.initials: K
authors.lastname: Fujiwara
authors.forename: S
authors.initials: S
authors.lastname: Iwahara
authors.forename: K
authors.initials: K
authors.lastname: Yamamoto
authors.forename: T
authors.initials: T
authors.lastname: Tochikura
mesh_terms: D000118:Acetylglucosaminidase / Q000494:pharmacology; D001234:Aspergillus niger / Q000201:enzymology*; D050260:Carbohydrate Metabolism; D004795:Enzyme Stability; D005949:Glucose Oxidase / Q000378:metabolism*; D006031:Glycosylation; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase
chemical_list: D005949:Glucose Oxidase; D000118:Acetylglucosaminidase; D017038:Mannosyl-Glycoprotein Endo-beta-N-Acetylglucosaminidase