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Literature summary for 1.11.1.10 extracted from

  • Jung, D.; Streb, C.; Hartmann, M.
    Covalent anchoring of chloroperoxidase and glucose oxidase on the mesoporous molecular sieve SBA-15 (2010), Int. J. Mol. Sci., 11, 762-778.
    View publication on PubMedView publication on EuropePMC

General Stability

General Stability Organism
covalently bonded CPO on the mesoporous material SBA-15 exhibits a higher operational stability in a continuously operated fixed-bed reactor compared to a catalyst prepared by physisorption of the enzyme. Chloroperoxidase immobilization into SBA-15 shows a remaining activity of about 9% Leptoxyphium fumago

Organism

Organism UniProt Comment Textmining
Leptoxyphium fumago
-
-
-

Storage Stability

Storage Stability Organism
4°C, CPO immobilized into glutaraldehyde-3-aminopropyltrimethoxysilane-SBA-15 in a buffer at pH 3.4, storage results in leaching of the enzyme from the support due to hydrolytic cleavage of the imino bond Leptoxyphium fumago
4°C, CPO immobilized into glutaraldehyde-3-aminopropyltrimethoxysilane-SBA-15 in a buffer at pH 7.0, a few days, complete loss of enzyme activity Leptoxyphium fumago

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
indole + H2O2
-
Leptoxyphium fumago 2-oxindole + H2O
-
?

Synonyms

Synonyms Comment Organism
CPO
-
Leptoxyphium fumago

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
3.8
-
pH optimum for CPO adsorbed on SBA-15 Leptoxyphium fumago

pI Value

Organism Comment pI Value Maximum pI Value
Leptoxyphium fumago isoelectric focusing
-
4