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Literature summary for 1.4.3.3 extracted from

  • Betancor, L.; Hidalgo, A.; Fernandez-Lorente, G.; Mateo, C.; Rodriguez, V.; Fuentes, M.; Lopez-Gallego, F.; Fernandez-Lafuente, R.; Guisan, J.M.
    Use of physicochemical tools to determine the choice of optimal enzyme: stabilization of D-amino acid oxidase (2003), Biotechnol. Prog., 19, 784-788.
    View publication on PubMed

General Stability

General Stability Organism
multisubunit immobilization on highly activated glyoxyl agarose improves stability of the enzyme 1500fold, at a protein concentration of 0.0067 mg/ml. Rhodotorula toruloides
multisubunit immobilization on highly activated glyoxyl agarose marginally improves stability of the enzyme, 15-20fold, at a protein concentration of 0.0067 mg/ml. Dissociation of FAD is not prevented by immobilization Trigonopsis variabilis

Organism

Organism UniProt Comment Textmining
Rhodotorula toruloides
-
-
-
Trigonopsis variabilis
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
cephalosporin C + H2O + O2
-
Rhodotorula toruloides 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?
cephalosporin C + H2O + O2
-
Trigonopsis variabilis 7-(5-oxoadipoamido)cephalosporanic acid + NH3 + H2O2
-
?

Synonyms

Synonyms Comment Organism
RgDAAO
-
Rhodotorula toruloides
TvDAAO
-
Trigonopsis variabilis

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40
-
50 h, pH 7.5, about 45% loss of activity of enzyme after multisubunit immobilization on highly activated glyoxyl agarose, protein concentration 0.0067 mg/ml Rhodotorula toruloides
40
-
50 h, pH 7.5, about 45% loss of activity of enzyme after multisubunit immobilization on highly activated glyoxyl agarose, protein concentration 0.2 mg/ml Trigonopsis variabilis
42
-
50 h, pH 7.5, about 60% loss of activity of enzyme after multisubunit immobilization on highly activated glyoxyl agarose, protein concentration 0.067 mg/ml and 50 mM FAD, 95% loss of activity without FAD Trigonopsis variabilis