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Literature summary extracted from

  • Sukyai, P.; Rezic, T.; Lorenz, C.; Mueangtoom, K.; Lorenz, W.; Haltrich, D.; Ludwig, R.
    Comparing soluble and co-immobilized catalysts for 2-ketoaldose production by pyranose 2-oxidase and auxiliary enzymes (2008), J. Biotechnol., 135, 281-290.
    View publication on PubMed

Application

EC Number Application Comment Organism
1.1.3.10 biotechnology studies on stabilization of enzymatic activity by immobilization Trametes ochracea

Cloned(Commentary)

EC Number Cloned (Comment) Organism
1.1.3.10 expressed in Escherichia coli BL21-DE3, recombinant protein, expression vector pET21 Trametes ochracea

Inhibitors

EC Number Inhibitors Comment Organism Structure
1.1.3.10 2-keto-D-glucose 5% reduction at 100 mM, 10% reduction at 200 mM, no deactivating effect determined Trametes ochracea
1.1.3.10 H2O2 slow inactivation at 20 mM Trametes ochracea
1.1.3.10 hydrogen peroxide inactivation determined Trametes ochracea

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
1.1.3.10 0.11
-
 O2 soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0 Trametes ochracea
1.1.3.10 0.3
-
 1,4-benzoquinone soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0 Trametes ochracea
1.1.3.10 0.79
-
 glucose immobilized enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0 Trametes ochracea
1.1.3.10 0.85
-
 glucose soluble enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0 Trametes ochracea

Organism

EC Number Organism UniProt Comment Textmining
1.1.3.10 Trametes ochracea
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
1.1.3.10 recombinant protein, gel purified to specific activity of 4.2 U/mg Trametes ochracea

Specific Activity [micromol/min/mg]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
1.1.3.10 additional information
-
 report on immobilization of pyranose 2-oxidase on agarose or acrylic resins using different coupling methods, enzyme activity determined by a peroxidase-coupled assay or by measuring initial rate of oxygen consumption, molecular properties of immobilized enzymes and binding capacities summarized Trametes ochracea

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
1.1.3.10 D-glucose + O2 immobilized and soluble pyranose 2-oxidase analyzed Trametes ochracea 2-dehydro-D-glucose + H2O2
-
 ?

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
1.1.3.10 30
-
 activity assay at Trametes ochracea

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
1.1.3.10 additional information
-
 thermal inactivation of free and immobilized enzyme activity investigated at 40, 50, 60 and 70°C in 50 mM phosphate buffer at pH 6.0 over 7 days, stability of immobilized enzyme shown to be significantly higher at 60°C, no stabilizing effect observed at 70°C Trametes ochracea

Turnover Number [1/s]

EC Number Turnover Number Minimum [1/s] Turnover Number Maximum [1/s] Substrate Comment Organism Structure
1.1.3.10 49
-
 glucose soluble enzyme, O2 used as electron acceptor, determined in cuvette assay, pH 5.0 Trametes ochracea
1.1.3.10 70
-
 O2 soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0 Trametes ochracea
1.1.3.10 324
-
 1,4-benzoquinone soluble enzyme, 500 mM glucose used as electron acceptor, pH 5.0 Trametes ochracea

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
1.1.3.10 5
-
 activity assay at Trametes ochracea

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
1.1.3.10 additional information
-
 stability of soluble and immobilized enzymes examined by incubating samples at 30°C for 7 days in citrate-phosphate buffer ranging from pH 4 to 8, similar stability obtained in free or immobilized form Trametes ochracea