Any feedback?
Please rate this page
(literature.php)
(0/150)

BRENDA support

Literature summary extracted from

  • Yoshimoto, M.; Miyazaki, Y.; Sato, M.; Fukunaga, K.; Kuboi, R.; Nakao, K.
    Mechanism for high stability of liposomal glucose oxidase to inhibitor hydrogen peroxide produced in prolonged glucose oxidation (2004), Bioconjug. Chem., 15, 1055-1061.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.4 biotechnology the enzyme encapsulated in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine is a useful biocatalyst for the prolonged glucose oxidation Aspergillus niger

General Stability

EC Number General Stability Organism
1.1.3.4 encapsulation of the enzyme in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine increases the enzyme stability through its decreased inhibition because of H2O2 produced in glucose oxidation Aspergillus niger

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.4 H2O2 encapsulation of the enzyme in the liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine increases the enzyme stability through its decreased inhibition because of H2O2 produced in glucose oxidation. The glucose oxidase-containing liposomes are completely free of the inhibition even in the complete conversion of 10 mM glucose at 25°C because the H2O2 concentration is kept negligible low both outside and inside liposomes throughout the reaction Aspergillus niger

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.4 Aspergillus niger
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.4 beta-D-glucose + O2
-
 Aspergillus niger D-glucono-1,5-lactone + H2O2
-
 ?