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Literature summary for 1.1.3.13 extracted from

  • Chung, H.; Cho, H.; Kong, K.
    Immobilization of Hansenula polymorpha alcohol oxidase for alcohol biosensor applications (2009), Bull. Korean Chem. Soc., 30, 57-60.
No PubMed abstract available

Application

Application Comment Organism
analysis the enzyme is useful in alcohol biosensor applications Ogataea angusta

Protein Variants

Protein Variants Comment Organism
additional information enzyme immobilization on DEAE-cellulose particles for alcohol biosensor applications, substrate specificity and the optimum pH of the immobilized enzyme are similar to those of the free enzyme, while Km and temperature optimum differ, overview Ogataea angusta

KM Value [mM]

KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
6.66
-
ethanol free enzyme Ogataea angusta
14.45
-
ethanol immobilized enzyme Ogataea angusta

Natural Substrates/ Products (Substrates)

Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
ethanol + O2 Ogataea angusta
-
acetaldehyde + H2O2
-
?

Organism

Organism UniProt Comment Textmining
Ogataea angusta
-
ATCC 26012
-

Purification (Commentary)

Purification (Comment) Organism
native enzyme to homogeneity by two different steps of anion exchange chromatography Ogataea angusta

Specific Activity [micromol/min/mg]

Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
0.21
-
free native enzyme, substrate n-propanol Ogataea angusta
0.33
-
immobilized native enzyme, substrate n-propanol Ogataea angusta
0.48
-
immobilized native enzyme, substrate crotyl alcohol Ogataea angusta
0.68
-
free native enzyme, substrate crotyl alcohol Ogataea angusta
6.68
-
immobilized native enzyme, substrate methanol Ogataea angusta
8.18
-
immobilized native enzyme, substrate ethanol Ogataea angusta
9.48
-
free native enzyme, substrate methanol Ogataea angusta
10.23
-
free native enzyme, substrate ethanol Ogataea angusta

Storage Stability

Storage Stability Organism
25°C, purified free enzyme, 10 weeks, 20% remaining actiivty Ogataea angusta
25°C, purified immobilized enzyme, 10 weeks, 60% remaining actiivty Ogataea angusta
4°C, purified free enzyme, 10 weeks, 70% remaining actiivty Ogataea angusta
4°C, purified immobilized enzyme, 10 weeks, 90% remaining actiivty Ogataea angusta
the immobilized enzyme shows a high stability against long storage Ogataea angusta

Substrates and Products (Substrate)

Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
crotyl alcohol + O2
-
Ogataea angusta (2E)-but-2-enal + H2O2
-
?
ethanol + O2
-
Ogataea angusta acetaldehyde + H2O2
-
?
methanol + O2
-
Ogataea angusta formaldehyde + H2O2
-
?
additional information no or poor activity with 1-butanol, 2-butanol, 3-butanol, isoamyl alcohol, 2-propanol, and 2,2,2-trichloroethanol Ogataea angusta ?
-
?
n-propanol + O2
-
Ogataea angusta propanaldehyde + H2O2
-
?

Synonyms

Synonyms Comment Organism
AOd
-
Ogataea angusta

Temperature Optimum [°C]

Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
50
-
free enzyme Ogataea angusta
65
-
immobilized enzyme Ogataea angusta

Temperature Range [°C]

Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
30 80 activity range of the immobilized enzyme, 25% of maximal activity at 80°C Ogataea angusta

Temperature Stability [°C]

Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
40 80 the immobilized enzyme is fairly stable at temperature up to 60°C. Above 70°C, its activity declines rapidly as the temperature increased, but the immobilized enzyme is not completely inactivated even at 80°C Ogataea angusta

pH Optimum

pH Optimum Minimum pH Optimum Maximum Comment Organism
7.5
-
assay at Ogataea angusta

pH Range

pH Minimum pH Maximum Comment Organism
4 10 the free and immobilized enzyme show less than 45% of their maximum activities below pH 4.0 and approximately 85% at pH 10.0 Ogataea angusta

Expression

Organism Comment Expression
Ogataea angusta methanol induces at 0.5% up