Aspergillus niger glucose oxidase from

In redox reactions, isolated oxidative enzymes such as laccase C from Trametes and horseradish/soybean peroxidases (with mediators) have been shown to possess good catalytic activity in common ILs on syringaldizine and veratryl alcohol, respectively [35]. Recently, oxidase-peroxidase-catalyzed chemo- and stereoselective sulfoxidations of thioanisole and methyl-2-naphthyl sulfide have been successfully carried out with a system of Coprinus cinereus (CiP) peroxidase and Aspergillus niger glucose oxidase (GOD) in 10% water in [BMIM][PF6] (Scheme 2). An enantiomeric... 

Glucose oxidase (from Aspergillus niger) [9001-37-0] Mf 186,000, [EC 1.1.3.4]. Purified by dialysis against deionized water at 6° for 48hours, and by molecular exclusion chromatography with Sephadex G-25 at room temperature. [Holt and Cotton J Am Chem Soc 109 1841 1987.]... 

O Malley, J.J., and Weaver J.L. (1972) Subunit structure of glucose oxidase from Aspergillus niger. Biochemistry 11, 3527. 

Yoshitake, S., Yamada, Y., Ishikawa, E., and Masseyeff, R. (1979) Conjugation of glucose oxidase from Aspergillus niger and rabbit antibodies using N-hydroxysuccinimide ester of N-(4-carboxycyclohexyl methyljmaleimide. Eur.J. Biochem. 101, 395-399. 

Enzyme labels are usually coupled to secondary antibodies or to (strept)avidin. The latter is used for detection of biotinylated primary or secondary antibodies in ABC methods (see Sect. 6.2.1). Enzyme labels routinely used in immunohisto-chemistry are horseradish peroxidase (HRP) and calf intestinal alkaline phosphatase (AP). Glucose oxidase from Aspergillus niger and E. coli (3-galactosidase are only rarely applied. 

Enzymatic markers used in immunohistochemistry Horseradish peroxidase (HRP) and calf intestinal or E.coli alkaline phosphatase (AP). Glucose oxidase from Aspergillus niger and E.coli /3-galactosidase are only rarely applied. 

D Auria S, Herman P, Rossi M, Lakowicz JR. The fluorescence emission of the apo-glucose oxidase from Aspergillus niger as probe to estimate glucose concentrations. Biochemical and Biophysical Research Communications 1999, 263, 550-553. 

Reagents. Anhydrous d-glucose and glucose oxidase Type VII Aspergillus Niger were purchased from Sigma. Acrylamide 97%, potassium persulfate 99%, 2-(dimethylamino)ethylmethacrylate 98% (DMAEM), N,N-methylenebisacrylamide 99% and NaOH were from Aldrich. NaCl was from Mallinckrodt. HC1 was purchased from Fisher. 

Glucose oxidase (from Aspergillus niger, specific activity 20 unit/mg), was purchased from Boehringer Mannheim Canada Ltd. 

Kabsz HM, Hecht H-J, Schomburg D, Schmid RD. Crystallization and preliminary X-ray diffraction studies of a deglycosylated glucose oxidase from Aspergillus niger.] Mol Biol 1990 213 207-9. 

D-Glucose Oxidases.—Oxidation of the D-glucose oxidase from Aspergillus niger with periodate decreased its carbohydrate content, but the catalytic activity, immunological reactivity, and gross secondary and quaternary structures were not aff ected. The periodate-oxidized derivative was stable to heat treatment, although its stability was reduced in the presence of denaturants. 

In a study of the periodate oxidation of r>-glucose oxidase from Aspergillus niger, 50% of the carbohydrate was removed with little effect on enzymic activity. Gel permeation chromatography results suggested that the oxidized enzyme exists as a complex oligomerizing system. 

D-Glucose Oxidase.— The carbohydrate moieties of D-glucose oxidase from Aspergillus niger have been modified by oxidation with periodate ion. Although ca. 60% of the carbohydrate residues were oxidized at pH 5.6, none of the amino-acid residues was oxidized. The oxidized enzyme retained its full activity and was converted into an immobilized form. 

To avoid interference with the active site of the enzyme, D-glucose oxidase from Aspergillus niger has been immobilized by way of its carbohydrate moieties. Thus, treatment of the periodate-oxidized enzyme with a styrene derivative afforded a water-insoluble material retaining full enzymic activity and exhibiting enhanced thermal stability at 60 °C. 

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