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Literature summary extracted from

  • Ogawa, K.; Nakajima-Kambe, T.; Nakahara, T.; Kokufuta, E.
    Coimmobilization of gluconolactonase with glucose oxidase for improvement in kinetic property of enzymatically induced volume collapse in ionic gels (2002), Biomacromolecules, 3, 625-631.
    View publication on PubMed

Application

EC Number Application Comment Organism
3.1.1.17 molecular biology coimmobilization with glucose oxidase in polyelectrolyte gels for improvement of kinetic properties, active enzymes in the gel undergo a shrinking process due to a sudden drop in pH, gel volume phase transition, overview Aspergillus niger

Organism

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

Purification (Commentary)

EC Number Purification (Comment) Organism
3.1.1.17 100fold Aspergillus niger

Reaction

EC Number Reaction Comment Organism Reaction ID
3.1.1.17 D-glucono-1,5-lactone + H2O = D-gluconate Acts on a wide range of hexose-1,5-lactones. The hydrolysis of L-gulono-1,5-lactone was previously listed as EC 3.1.1.18, aldonolactonase. Aspergillus niger
a

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.1.1.17 D-glucono-1,5-lactone + H2O
-
 Aspergillus niger D-gluconate
-
 ?

Synonyms

EC Number Synonyms Comment Organism
3.1.1.17 GL
-
 Aspergillus niger