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1.1.3.13: alcohol oxidase

This is an abbreviated version!
For detailed information about alcohol oxidase, go to the full flat file.

Word Map on EC 1.1.3.13

Reaction

a primary alcohol
+
O2
=
an aldehyde
+
H2O2

Synonyms

alcohol oxidase 1, alcohol oxidase 2, alcohol oxidase A, alcohol oxidase B, alcohol oxidase I, alcohol: O2 oxidoreductase, alcohol:dioxygen-oxidoreductase, alcohol:O2 oxidoreductase, AlcOx, AOd, AOD1, AOext, AOint, AOX, AOX1, AOX2, AOXI, broad substrate specific alcohol oxidase, EC 1.1.3.31, ethanol oxidase, extracellular alcohol oxidase, FAD-dependent alcohol oxidase, FAO1, GLRG_05590, intracellular alcohol oxidase, long chain fatty alcohol oxidase, methanol oxidase, Mod1p, Mod2p, oxidase, alcohol, P-AOD, peroxisomal alcohol oxidase, primary alcohol oxidase, SCAO, short chain alcohol oxidase, short-chain alcohol oxidase, VAO, veratryl alcohol oxidase

ECTree

     1 Oxidoreductases
         1.1 Acting on the CH-OH group of donors
             1.1.3 With oxygen as acceptor
                1.1.3.13 alcohol oxidase

General Stability

General Stability on EC 1.1.3.13 - alcohol oxidase

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GENERAL STABILITY
ORGANISM
UNIPROT
LITERATURE
0°C, stable in 2% v/v acetonitrile up to 2 h
-
30°C, partially inactivated by 6 M urea or 3.5 M KBr after 1-2 h, complete inactivation in a mixture of theses agents
-
7.7 mM NaN3, 30°C, enzyme retains activity for at least 35 days, inactivated completely after 10 days without NaN3
-
ethanol stabilizes the protein structure and increased the melting temperature
-
free enzyme is stable under the processing conditions during immobilization on electrospun fibers and retains more than 90% of its initial activity after 4 h of incubation
-
freezing at -20°C and thawing leads to 25% loss of activity
Poria contigua
-
freezing leads to loss of activity
-
rapid freezing at -80°C and thawing has no significant effect on the enzyme’s activity
rapid inactivation by repeated freezing and thawing
-
rapidly inactivated by freezing and thawing
-
stabilizing immobilization by ionic adsorption on agarose coated with 600 kDa polyethylenimine. The adsorption of the proteins on the polymeric bed allows the stabilization of the quaternary structure. The effect of the enzyme concentration on thermal enzyme stability disappears in these immobilized preparations. A high stability is obtained without a significant decrease in enzyme activity during immobilization (recovered activity was over 50%)
the enzyme has increased stability in phosphate-citrate buffer and low stability in Tris-HCl and phosphate buffers. Its stability is increased 10fold in the presence of sucrose, mannitol, polyethylene glycol, polyvinyl alcohol, polyvinylpyrrolidone, and EDTA. Sucrose at 50% concentration (w/v) enhances stability of the enzyme 10fold at 50°C
Pichia putida
-