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Literature summary for 1.11.1.10 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

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

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
-
-
-

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
thioanisole + H2O2
-
Leptoxyphium fumago methyl phenyl sulfoxide + H2O
-
?

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
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