Penicillium glucose oxidase

Kiess, M., Hecht, H.J. and Kalisz, H.M. (1998) Glucose oxidase from Penicillium amagasakiense primary structure and comparison with other glucose-methanol-choline (GMC) oxidoreductases. European Journal of Biochemistry, 252, 90-99. 

Glucose oxidase is obtained from molds such as Aspergillus niger and species of Penicillium, In its gross molecular properties at least, the enzyme from A. niger resembles l- rather than n-amino acid oxidase (19) since it is a dimer of 186,000 MW with two tightly, but noncovalently, bound FAD molecules per dimer. These FAD moieties are kinetically independent and probably, therefore, are present at an active site on each subunit. The enzyme is remarkably stable over a wide range of pH and other variables, which makes it ideal for analytical and bulk conversion applications. 

Kulys, J.T. and Cenas, N.K. (1983) Oxidation of glucose oxidase from Penicillium vitale by one- and two-electron acceptors. Biochimica et Biophysica Acta, 744, 57-63. 

Keston305-307 showed that the kidney, liver, and lens tissues of many animals contain an enzyme that catalyzes the mutarotation of a- and /3-D-glucose and other sugars it was called mutarotase.3 8,309 This, or a similar, enzyme had earlier been found in preparations of D-glucose oxidase from Penicillium notatum by Bentley and Neu-berger310 and Keilin and Hartree.309 The enzyme was extensively purified by Bentley and Bhate.140 The enzyme is also widely distributed in plant tissues.311... 

Kulys J J and Cenas N K 1983 Oxidation of glucose oxidase Penicillium vitale... 

Kulys, J. J., Cenas, N. K., Oxidation of Glucose Oxidase from Penicillium Vitale by One- and TVvo-Electron Acceptors , Biochim. Biophys. Acta 744 (1983) 57-63. 

Some of the chemical and immunological properties of the D-glucose oxidases from A. niger and Penicillium glaucum have been compared. Although c.d. spectroscopy indicated that the protein chains have essentially identical conformations, small variations in their structures were revealed by differences in the thermal stabilities, catalytic properties, and immunological activities of the enzymes. 

Kalisz, H. M., J. Hendle, and R. D. Schmid. 1997. Structural and Biochemical Properties of Glycosylated and Deglycosylated Glucose Oxidase from Penicillium Amagasakiense." Applied Microbiology and Biotechnology 47 (5) 502-507. 

Catalase-free glucose oxidase (GOD) from Penicillium notatum (E.C. 

C6H6O4, Mr 142.11. Prismatic crystal needles, mp. 153-154 °C, soluble in water K. is formed by Aspergillus species (e. g., A. albus, A. flavus, A. oryzae, A, fumigatus), Penicillium daleae and bacteria of the genus Acetobacter in carbohydrate rich nutrient media, it can also be synthesized from glucose and other hex-oses. K. has antibiotic and insecticidal activities and forms chelates. It inhibits polyphenol oxidases (tyro-... 

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