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Literature summary for 3.2.1.73 extracted from
- A novel thermostable beta-1,3-1,4-glucanase from Thermoascus aurantiacus and its application in oligosaccharide production from oat bran (2018), Carbohydr. Res., 469, 31-37 .
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Ag+ | 57.8% inhibition | Thermoascus aurantiacus |  |
| Hg2+ | complete inhibition | Thermoascus aurantiacus | |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km and Vmax values of the purified TaGlu34 for barley beta-D-glucan and oat beta-glucan are determined to be 2.09 mg/ml and 13.18 mmol/min/mg, and 1.36 mg/ml and 0.0165 mmol/min/mg, respectively | Thermoascus aurantiacus |
Localization
| Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|
| extracellular | the enzyme is secreted | Thermoascus aurantiacus | - |
- |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Co2+ | activates 59.8% | Thermoascus aurantiacus | |
| Mg2+ | activates 22.1% | Thermoascus aurantiacus | |
| Mn2+ | activates 32.1% | Thermoascus aurantiacus | |
| additional information | Ca2+, Cu2+, Ni2+, Ba2+, EDTA, and 2-mercaptoethanol show no obvious effect on the enzyme activity | Thermoascus aurantiacus | |
| Sn2+ | activates 41.2% | Thermoascus aurantiacus | |
| Zn2+ | activates 39.2% | Thermoascus aurantiacus | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 31000 | - |
gel filtration | Thermoascus aurantiacus |
Natural Substrates/ Products (Substrates)
| Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| additional information | Thermoascus aurantiacus | reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34 | ? | - |
? | |
| additional information | Thermoascus aurantiacus CAU830 | reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34 | ? | - |
? | |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermoascus aurantiacus | - |
- |
- |
| Thermoascus aurantiacus CAU830 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| native extracellular enzyme from cell culture supernatant 7.3fold to homogeneity by ammonium sulfate fractionation, and anion exchange and hydrophobic interaction chromatography | Thermoascus aurantiacus |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| mycelium | submerged culture, optimization of enzyme production, under optimized conditions viz. 5% w/v corncob as carbon source, 1% w/v peptone as nitrogen source, initial pH of 5.0, 1% w/v of Tween 40, cultivation temperature of 50°C, and incubation time of 7 d, the highest beta-1,3-1,4-glucanase activity of 3741 U/ml is obtained | Thermoascus aurantiacus | - |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 9225 | - |
purified native enzyme, pH 6.0, 65°C, substrate lichenan | Thermoascus aurantiacus |
| 12502 | - |
purified native enzyme, pH 6.0, 65°C, substrate oat beta-glucan | Thermoascus aurantiacus |
| 13527 | - |
purified native enzyme, pH 6.0, 65°C, substrate barley beta-glucan | Thermoascus aurantiacus |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| barley beta-glucan + H2O | best substrate | Thermoascus aurantiacus | ? | - |
? | |
| barley beta-glucan + H2O | best substrate | Thermoascus aurantiacus CAU830 | ? | - |
? | |
| lichenan + H2O | 68.2% of the activity with barley beta-glucan | Thermoascus aurantiacus | ? | - |
? | |
| lichenan + H2O | 68.2% of the activity with barley beta-glucan | Thermoascus aurantiacus CAU830 | ? | - |
? | |
| additional information | reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34 | Thermoascus aurantiacus | ? | - |
? | |
| additional information | no activity towards other tested polysaccharides including laminarin, CMC, birchwood xylan, pullulan, soluble starch and locust bean gum, and 4-nitrophenyl derivates such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-galactopyranoside, 4-nitrophenyl alpha-galactopyranoside, 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl-alpha-glucopyranoside | Thermoascus aurantiacus | ? | - |
? | |
| additional information | reported fungal eta-1,3-1,4-glucanases exhibit strict substrate specificity toward barley beta-glucan, oat beta-glucan and lichenan, of which the structures are all beta-(1,4)-linked glucose interrupted with beta-(1,3)-linkages. beta-1,3-1,4-Glucanases (lichenases) specifically hydrolyze the beta-1,4 glycosidic linkages adjacent to beta-1,3 bonds, yielding disaccharides, trisaccharides and tetrasaccharides as the major products. Enzyme TaGlu34 hydrolyzes barley beta-glucan and lichanan to produce mainly disaccharide and trisaccharide without formation of tetrasaccharide. Production of glucan oligosaccharides from oat bran by TaGlu34 | Thermoascus aurantiacus CAU830 | ? | - |
? | |
| additional information | no activity towards other tested polysaccharides including laminarin, CMC, birchwood xylan, pullulan, soluble starch and locust bean gum, and 4-nitrophenyl derivates such as 4-nitrophenyl-beta-xylopyranoside, 4-nitrophenyl-beta-galactopyranoside, 4-nitrophenyl alpha-galactopyranoside, 4-nitrophenyl beta-glucopyranoside and 4-nitrophenyl-alpha-glucopyranoside | Thermoascus aurantiacus CAU830 | ? | - |
? | |
| oat beta-glucan + H2O | 92.4% of the activity with barley beta-glucan | Thermoascus aurantiacus | ? | - |
? | |
| oat beta-glucan + H2O | 92.4% of the activity with barley beta-glucan | Thermoascus aurantiacus CAU830 | ? | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 34400, SDS-PAGE | Thermoascus aurantiacus |
| More | peptide mapping | Thermoascus aurantiacus |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| beta-1,3-1,4-glucanase | - |
Thermoascus aurantiacus |
| TaGlu34 | - |
Thermoascus aurantiacus |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 75 | - |
- |
Thermoascus aurantiacus |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | 85 | over 50% of maximal activity within this range, profile overview | Thermoascus aurantiacus |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | 70 | the purified native enzyme shows half-lives of 209, 130 and 69 min at 50, 60 and 70°C, respectively | Thermoascus aurantiacus |
| 70 | - |
purified native enzyme, 30 min, over 80% activity remaining | Thermoascus aurantiacus |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 6 | - |
- |
Thermoascus aurantiacus |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 8 | over 50% of maximal activity within this range, profile overview | Thermoascus aurantiacus |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 9 | purified native enzyme TaGlu34 exhibits excellent stability at pH 4.0-9.0, retaining more than 80% of its maximal activity | Thermoascus aurantiacus |
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Release 2023.1 (January 2023)
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