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Literature summary extracted from

  • Yan, Q.; Yang, H.; Jiang, Z.; Liu, E.; Yang, S.
    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 .
    View publication on PubMed

Inhibitors

EC Number Inhibitors Comment Organism Structure
3.2.1.73 Ag+ 57.8% inhibition Thermoascus aurantiacus
3.2.1.73 Hg2+ complete inhibition Thermoascus aurantiacus

KM Value [mM]

EC Number KM Value [mM] KM Value Maximum [mM] Substrate Comment Organism Structure
3.2.1.73 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

EC Number Localization Comment Organism GeneOntology No. Textmining
3.2.1.73 extracellular the enzyme is secreted Thermoascus aurantiacus
-
-

Metals/Ions

EC Number Metals/Ions Comment Organism Structure
3.2.1.73 Co2+ activates 59.8% Thermoascus aurantiacus
3.2.1.73 Mg2+ activates 22.1% Thermoascus aurantiacus
3.2.1.73 Mn2+ activates 32.1% Thermoascus aurantiacus
3.2.1.73 additional information Ca2+, Cu2+, Ni2+, Ba2+, EDTA, and 2-mercaptoethanol show no obvious effect on the enzyme activity Thermoascus aurantiacus
3.2.1.73 Sn2+ activates 41.2% Thermoascus aurantiacus
3.2.1.73 Zn2+ activates 39.2% Thermoascus aurantiacus

Molecular Weight [Da]

EC Number Molecular Weight [Da] Molecular Weight Maximum [Da] Comment Organism
3.2.1.73 31000
-
 gel filtration Thermoascus aurantiacus

Natural Substrates/ Products (Substrates)

EC Number Natural Substrates Organism Comment (Nat. Sub.) Natural Products Comment (Nat. Pro.) Rev. Reac.
3.2.1.73 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 ?
-
 ?
3.2.1.73 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

EC Number Organism UniProt Comment Textmining
3.2.1.73 Thermoascus aurantiacus
-
-
-
3.2.1.73 Thermoascus aurantiacus CAU830
-
-
-

Purification (Commentary)

EC Number Purification (Comment) Organism
3.2.1.73 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

EC Number Source Tissue Comment Organism Textmining
3.2.1.73 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]

EC Number Specific Activity Minimum [µmol/min/mg] Specific Activity Maximum [µmol/min/mg] Comment Organism
3.2.1.73 9225
-
 purified native enzyme, pH 6.0, 65°C, substrate lichenan Thermoascus aurantiacus
3.2.1.73 12502
-
 purified native enzyme, pH 6.0, 65°C, substrate oat beta-glucan Thermoascus aurantiacus
3.2.1.73 13527
-
 purified native enzyme, pH 6.0, 65°C, substrate barley beta-glucan Thermoascus aurantiacus

Substrates and Products (Substrate)

EC Number Substrates Comment Substrates Organism Products Comment (Products) Rev. Reac.
3.2.1.73 barley beta-glucan + H2O best substrate Thermoascus aurantiacus ?
-
 ?
3.2.1.73 barley beta-glucan + H2O best substrate Thermoascus aurantiacus CAU830 ?
-
 ?
3.2.1.73 lichenan + H2O 68.2% of the activity with barley beta-glucan Thermoascus aurantiacus ?
-
 ?
3.2.1.73 lichenan + H2O 68.2% of the activity with barley beta-glucan Thermoascus aurantiacus CAU830 ?
-
 ?
3.2.1.73 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 ?
-
 ?
3.2.1.73 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 ?
-
 ?
3.2.1.73 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 ?
-
 ?
3.2.1.73 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 ?
-
 ?
3.2.1.73 oat beta-glucan + H2O 92.4% of the activity with barley beta-glucan Thermoascus aurantiacus ?
-
 ?
3.2.1.73 oat beta-glucan + H2O 92.4% of the activity with barley beta-glucan Thermoascus aurantiacus CAU830 ?
-
 ?

Subunits

EC Number Subunits Comment Organism
3.2.1.73 monomer 1 * 34400, SDS-PAGE Thermoascus aurantiacus
3.2.1.73 More peptide mapping Thermoascus aurantiacus

Synonyms

EC Number Synonyms Comment Organism
3.2.1.73 beta-1,3-1,4-glucanase
-
 Thermoascus aurantiacus
3.2.1.73 TaGlu34
-
 Thermoascus aurantiacus

Temperature Optimum [°C]

EC Number Temperature Optimum [°C] Temperature Optimum Maximum [°C] Comment Organism
3.2.1.73 75
-
-
 Thermoascus aurantiacus

Temperature Range [°C]

EC Number Temperature Minimum [°C] Temperature Maximum [°C] Comment Organism
3.2.1.73 45 85 over 50% of maximal activity within this range, profile overview Thermoascus aurantiacus

Temperature Stability [°C]

EC Number Temperature Stability Minimum [°C] Temperature Stability Maximum [°C] Comment Organism
3.2.1.73 50 70 the purified native enzyme shows half-lives of 209, 130 and 69 min at 50, 60 and 70°C, respectively Thermoascus aurantiacus
3.2.1.73 70
-
 purified native enzyme, 30 min, over 80% activity remaining Thermoascus aurantiacus

pH Optimum

EC Number pH Optimum Minimum pH Optimum Maximum Comment Organism
3.2.1.73 6
-
-
 Thermoascus aurantiacus

pH Range

EC Number pH Minimum pH Maximum Comment Organism
3.2.1.73 4 8 over 50% of maximal activity within this range, profile overview Thermoascus aurantiacus

pH Stability

EC Number pH Stability pH Stability Maximum Comment Organism
3.2.1.73 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