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Literature summary for 3.1.1.117 extracted from
- Expression and characterization of two glucuronoyl esterases from Thielavia terrestris and their application in enzymatic hydrolysis of corn bran (2019), Appl. Microbiol. Biotechnol., 103, 3037-3048 .
Application
| Application | Comment | Organism |
|---|---|---|
| synthesis | Thermothielavioides terrestris glucoronoyl esterases TtGEs can be used as promising accessory enzymes to improve the hydrolysis efficiency of commercial enzymes in saccharification of lignocellulosic materials due to their thermophilic characteristics | Thermothielavioides terrestris |
Cloned(Commentary)
| Cloned (Comment) | Organism |
|---|---|
| gene THITE_2055580, phylogenetic tree, recombinant expression of His-tagged TtGE2 isozyme in Pichia pastoris strain GS115, subcloning in Escherichia coli strain DH5alpha | Thermothielavioides terrestris |
| gene THITE_2117593, phylogenetic tree, recombinant expression of His-tagged TtGE1 isozyme in Pichia pastoris strain GS115, subcloning in Escherichia coli strain DH5alpha | Thermothielavioides terrestris |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Michaelis-Menten kinetics | Thermothielavioides terrestris |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Thermothielavioides terrestris | G2R8B5 | Thielavia terrestris | - |
| Thermothielavioides terrestris | G2RCM8 | Thielavia terrestris | - |
| Thermothielavioides terrestris ATCC 38088 | G2R8B5 | Thielavia terrestris | - |
| Thermothielavioides terrestris ATCC 38088 | G2RCM8 | Thielavia terrestris | - |
| Thermothielavioides terrestris NRRL 8126 | G2R8B5 | Thielavia terrestris | - |
| Thermothielavioides terrestris NRRL 8126 | G2RCM8 | Thielavia terrestris | - |
Posttranslational Modification
| Posttranslational Modification | Comment | Organism |
|---|---|---|
| glycoprotein | enzyme TtGE1 is N-glycosylated, and possesses three predicted N-glycosylation sites | Thermothielavioides terrestris |
| glycoprotein | enzyme TtGE2 is N-glycosylated, and possesses two predicted N-glycosylation sites | Thermothielavioides terrestris |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| recombinant His-tagged TtGE1 isozyme from Pichia pastoris strain GS115 by dialysis and nickel affinity chromatography | Thermothielavioides terrestris |
| recombinant His-tagged TtGE2 isozyme from Pichia pastoris strain GS115 by dialysis and nickel affinity chromatography | Thermothielavioides terrestris |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 12.47 | - |
purified recombinant isozyme TtGE2, pH 5.5, 55°C, substrate methyl (4-nitrophenyl beta-D-glucopyranoside)uronate | Thermothielavioides terrestris |
| 43.95 | - |
purified recombinant isozyme TtGE1, pH 5.5, 55°C, substrate methyl (4-nitrophenyl beta-D-glucopyranoside)uronate | Thermothielavioides terrestris |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O | - |
Thermothielavioides terrestris | methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate | - |
? |  |
| methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O | - |
Thermothielavioides terrestris ATCC 38088 | methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate | - |
? | |
| methyl (4-nitrophenyl beta-D-glucopyranoside)uronate + H2O | - |
Thermothielavioides terrestris NRRL 8126 | methanol + (4-nitrophenyl beta-D-glucopyranoside)uronate | - |
? | |
| methyl 4-O-methyl-D-glucuronate + H2O | - |
Thermothielavioides terrestris | methanol + 4-O-methylglucuronic acid | - |
? | |
| methyl 4-O-methyl-D-glucuronate + H2O | - |
Thermothielavioides terrestris ATCC 38088 | methanol + 4-O-methylglucuronic acid | - |
? | |
| methyl 4-O-methyl-D-glucuronate + H2O | - |
Thermothielavioides terrestris NRRL 8126 | methanol + 4-O-methylglucuronic acid | - |
? | |
| additional information | the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2 | Thermothielavioides terrestris | ? | - |
- |
|
| additional information | the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2 | Thermothielavioides terrestris | ? | - |
- |
|
| additional information | the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2 | Thermothielavioides terrestris ATCC 38088 | ? | - |
- |
|
| additional information | the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2 | Thermothielavioides terrestris ATCC 38088 | ? | - |
- |
|
| additional information | the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE1 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased by 9.2%, 92.6%, 58.8%, 43.5%, and 39.9%, respectively, when 1 mg TtGE1 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2 | Thermothielavioides terrestris NRRL 8126 | ? | - |
- |
|
| additional information | the enzyme shows no activity with benzyl-D-glucuronate, and with 4-nitrophenyl acetate and 4-nitrophenyl butyrate. The specific activity of isozyme TtGE2 is relatively low compared to that of isozyme TtGE1. Glucuronic acid and monosaccharides such as arabinose, galactose, glucose, and xylose are not released from the autohydrolysis residues of corn bran when TtGE2 is used alone. Both glucuronic acid and monosaccharides are released from the autohydrolysis residues of corn bran when commercial xylanase is used alone. The release of glucuronic acid, arabinose, galactose, glucose, and xylose is increased 4.0%, 51.9%, 54.8%, 36.3%, and 42.1%, respectively, when 1.5 mg TtGE2 is supplemented into the commercial xylanase during the enzymatic hydrolysis process compared to commercial xylanase alone. TtGE1 displays a better boosting effect on enzymatic hydrolysis than TtGE2 due to the higher catalytic activity of TtGE1 compared to TtGE2 | Thermothielavioides terrestris NRRL 8126 | ? | - |
- |
|
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| ? | x * 50000, about, recombinant glycosylated enzyme, SDS-PAGE, x * 39000, recombinant deglycosylated enzyme, SDS-PAGE | Thermothielavioides terrestris |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| carbohydrate esterase family 15 protein | UniProt | Thermothielavioides terrestris |
| glucuronoyl esterase | - |
Thermothielavioides terrestris |
| THITE_2055580 | - |
Thermothielavioides terrestris |
| THITE_2117593 | - |
Thermothielavioides terrestris |
| TtGE1 | - |
Thermothielavioides terrestris |
| TtGE2 | - |
Thermothielavioides terrestris |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 45 | - |
- |
Thermothielavioides terrestris |
| 55 | - |
- |
Thermothielavioides terrestris |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 30 | 60 | over 50% of maximal activity within this range, profile overview | Thermothielavioides terrestris |
| 42 | 60 | over 50% of maximal activity within this range, profile overview | Thermothielavioides terrestris |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 35 | 55 | purified isozyme TtGE1 exhibits high stability at 35°C and 45°C, and over 90% of the initial activity is retained after 100 min of incubation residual activity of about 60% is retained after incubation at 55°C for 12 h | Thermothielavioides terrestris |
| 45 | 65 | purified isozyme TtGE2 is completely stable at 45°C and 55°C for 100 min, more than 70% of the initial activity is retained after 100 min of incubation at 65°C | Thermothielavioides terrestris |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5 | - |
- |
Thermothielavioides terrestris |
| 5.5 | - |
- |
Thermothielavioides terrestris |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 3.5 | 7 | over 50% of maximal activity within the range of pH 4.5-6.7, profile overview | Thermothielavioides terrestris |
| 4.5 | 6.5 | over 50% of maximal activity within this range, profile overview | Thermothielavioides terrestris |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 3 | 10 | purified isozyme TtGE1 is relatively stable at pH between 4.0 and 6.0, with approximately 60-80% activity remaining. The enzyme is almost inactivated after incubation for12 h at a range of pH 9-10, profile overview | Thermothielavioides terrestris |
| 3 | 10 | purified isozyme TtGE2 retains 60-80% of its initial activity after preincubation at pH 3.0-6.0 for 12 h, but the residue activity decreases rapidly when treated with alkaline buffers at pH 7.0-10.0 | Thermothielavioides terrestris |
General Information
| General Information | Comment | Organism |
|---|---|---|
| evolution | glucuronoyl esterases (GEs) belong to the family 15 of carbohydrate esterases (CE15) | Thermothielavioides terrestris |
| physiological function | glucuronoyl esterases are considered to play a unique role as accessory enzymes in lignocellulosic material biodegradation by cleaving the covalent ester linkage between 4-O-methyl-D-glucuronic acid (MeGlcA) and lignin in lignin-carbohydrate complexes (LCCs). A substantial increase in the release of monomeric sugars and glucuronic acid from autohydrolysis of corn bran is observed by the supplementing TtGEs into commercial xylanase, demonstrating that the TtGEs play a significant role in this degradation process | Thermothielavioides terrestris |
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