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Literature summary extracted from

  • Spreti, N.; Germani, R.; Incani, A.; Savelli, G.
    Stabilization of chloroperoxidase by polyethylene glycols in aqueous media: kinetic studies and synthetic applications (2004), Biotechnol. Prog., 20, 96-101.
    View publication on PubMed

General Stability

EC Number General Stability Organism
1.11.1.10 di(ethylene glycol) and di(propylene glycol) stabilize the enzyme towards denaturation by H2O2 Leptoxyphium fumago

Organism

EC Number Organism UniProt Comment Textmining
1.11.1.10 Leptoxyphium fumago
-
-
-

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.11.1.10 thioanisole + H2O2
-
Leptoxyphium fumago methyl phenyl sulfoxide + H2O
-
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Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.11.1.10 25
-
about 95% loss of activity of the pure enzyme in 0.05 M citrate buffer, pH 5, about 60% loss of activity in presence of 0.1 M PEG 200 and PEG 400, about 40% loss of activity in presence of 0.1 M di(ethylene glycol), about 80% loss of activity in presence of 0.1 M di(propylene glycol) Leptoxyphium fumago