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Literature summary extracted from
- Efficient hydrolysis of raw starch and ethanol fermentation a novel raw starch-digesting glucoamylase from Penicillium oxalicum (2016), Biotechnol. Biofuels, 9, 216 .
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | food industry | the enzyme performs highly efficient hydrolysis of raw starches and direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol suggesting that the enzyme has a number of potential applications in industrial starch processing and starch-based ethanol production. Effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase | Penicillium oxalicum |
Cloned(Commentary)
| EC Number | Cloned (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | gene PoGA15A, DNA and amino acid sequence determination and analysis, phylogenetic tree, recombinant expression of codon-optimized His-tagged enzyme the sequence coding for the signal peptide in Pichia pastoris strain GS115 under control of AOX1 promoter. The recombinant enzyme is secreted | Penicillium oxalicum |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | additional information | effective hydrolysis of raw starch flour by the recombinant rPoGA15A preparation and alpha-amylase. Deletion of the starch-binding domain for raw starch-digesting glucoamylase rPoGA15A leads to reduced activity of the truncated enzyme with raw starches | Penicillium oxalicum |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | Ag+ | - |
Penicillium oxalicum |  |
| 3.2.1.3 | Cu2+ | - |
Penicillium oxalicum | |
| 3.2.1.3 | SDS | - |
Penicillium oxalicum | |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.3 | extracellular | the enzyme contains a signal peptide, it is secreted | Penicillium oxalicum | - |
- |
Metals/Ions
| EC Number | Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.3 | Fe2+ | slightly stimulating | Penicillium oxalicum | |
| 3.2.1.3 | Mn2+ | slightly stimulating | Penicillium oxalicum | |
| 3.2.1.3 | additional information | calcium ions has no obvious influence on enzyme activity. Most of the metal ions and chemical reagents do not have an obvious influence on PoGA15A activity | Penicillium oxalicum |
Molecular Weight [Da]
| EC Number | Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 75400 | - |
about, native PAGE | Penicillium oxalicum |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | starch + H2O | Penicillium oxalicum | raw starch | ? | - |
? | |
| 3.2.1.3 | starch + H2O | Penicillium oxalicum GXU20 | raw starch | ? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.3 | Penicillium oxalicum | A0A1D8DGR2 | - |
- |
| 3.2.1.3 | Penicillium oxalicum GXU20 | A0A1D8DGR2 | - |
- |
Posttranslational Modification
| EC Number | Posttranslational Modification | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | glycoprotein | glycosylation may occur during enzyme protein expression | Penicillium oxalicum |
Purification (Commentary)
| EC Number | Purification (Comment) | Organism |
|---|---|---|
| 3.2.1.3 | native enzyme 60.61fold by ethanol precipitation, hydrophobic interaction chromatography, and cation exchange chromatography, recombinant secreted His-tagged truncated enzyme from Pichia pastoris strain GS115 culture supernatant by nickel affinity chromatography | Penicillium oxalicum |
Specific Activity [micromol/min/mg]
| EC Number | Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4.5 | - |
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw rice starch | Penicillium oxalicum |
| 3.2.1.3 | 5.1 | - |
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw potato starch | Penicillium oxalicum |
| 3.2.1.3 | 5.3 | - |
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw cassava starch | Penicillium oxalicum |
| 3.2.1.3 | 6.8 | - |
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate raw corn starch | Penicillium oxalicum |
| 3.2.1.3 | 9.9 | - |
purified native enzyme, pH 4.5, 40°C, substrate raw potato starch | Penicillium oxalicum |
| 3.2.1.3 | 11.2 | - |
purified native enzyme, pH 4.5, 40°C, substrate raw cassava starch | Penicillium oxalicum |
| 3.2.1.3 | 22.7 | - |
purified native enzyme, pH 4.5, 40°C, substrate raw corn starch | Penicillium oxalicum |
| 3.2.1.3 | 24.7 | - |
purified native enzyme, pH 4.5, 40°C, substrate raw rice starch | Penicillium oxalicum |
| 3.2.1.3 | 57.9 | - |
purified recombinant enzyme mutant lacking the starch-binding domain, pH 4.5, 40°C, substrate soluble starch | Penicillium oxalicum |
| 3.2.1.3 | 80.5 | - |
purified native enzyme, pH 4.5, 40°C, substrate soluble starch | Penicillium oxalicum |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.3 | additional information | the enzyme shows a broad substrate specificity | Penicillium oxalicum | ? | - |
? | |
| 3.2.1.3 | additional information | the enzyme shows a broad substrate specificity | Penicillium oxalicum GXU20 | ? | - |
? | |
| 3.2.1.3 | starch + H2O | raw starch | Penicillium oxalicum | ? | - |
? | |
| 3.2.1.3 | starch + H2O | starch-digesting glucoamylase PoGA15A shows high enzymatic activity with raw starch from raw corn and cassava flours and towards various raw starches. Enzymatic activities towards raw rice (211.3%), corn (206.7%), and cassava (100%) are much higher than for other tested raw starches, including potato (90.8%), buck wheat (59.9%), and sweet potato (25.3%). Direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol. Best substrate is soluble starch (706.8%). Effective hydrolysis of raw starch flour by the recombinant rPoGA15A enzyme preparation and alpha-amylase, kinetics at pH 4.5 and 40°C, detailed overview | Penicillium oxalicum | ? | - |
? | |
| 3.2.1.3 | starch + H2O | raw starch | Penicillium oxalicum GXU20 | ? | - |
? | |
| 3.2.1.3 | starch + H2O | starch-digesting glucoamylase PoGA15A shows high enzymatic activity with raw starch from raw corn and cassava flours and towards various raw starches. Enzymatic activities towards raw rice (211.3%), corn (206.7%), and cassava (100%) are much higher than for other tested raw starches, including potato (90.8%), buck wheat (59.9%), and sweet potato (25.3%). Direct conversion of raw corn and cassava flours via simultaneous saccharification and fermentation to ethanol. Best substrate is soluble starch (706.8%). Effective hydrolysis of raw starch flour by the recombinant rPoGA15A enzyme preparation and alpha-amylase, kinetics at pH 4.5 and 40°C, detailed overview | Penicillium oxalicum GXU20 | ? | - |
? | |
Subunits
| EC Number | Subunits | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | ? | x * 75400, SDS-PAGE, x* 65400, polypeptide without the signal peptide (616 amino acid residues), sequence calculation | Penicillium oxalicum |
| 3.2.1.3 | More | the sequences from 1-19, 39-454, and 533-629 belong to the signal peptide, the catalytic domain of the glycosyl hydrolase family 15, and the starch-binding domain, respectively. Construction of a three-dimensional structure of PoGA15A by modelling using the known crystal structure of the glucoamylase from Hypocrea jecorina (PDB 2vn7). The three-dimensional structure shows that the catalytic domain is predicted to mainly contain an alpha-helix and a beta-propeller, which form the barrel structure. The starch-binding domain is predicted to have a beta-sandwich fold with eight beta-strands distributed in the two beta-sheets | Penicillium oxalicum |
Synonyms
| EC Number | Synonyms | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | glucoamylase | - |
Penicillium oxalicum |
| 3.2.1.3 | PoGA15A | - |
Penicillium oxalicum |
| 3.2.1.3 | RSDG | - |
Penicillium oxalicum |
| 3.2.1.3 | starch-digesting glucoamylase | - |
Penicillium oxalicum |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 65 | - |
- |
Penicillium oxalicum |
Temperature Range [°C]
| EC Number | Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 55 | 75 | over 60% activity within this range, profile overview | Penicillium oxalicum |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 50 | - |
purified native enzyme, pH 4.5, 1 h, completely stable up to | Penicillium oxalicum |
| 3.2.1.3 | 55 | - |
purified native enzyme, pH 4.5, 1 h, 90% activity remaining | Penicillium oxalicum |
| 3.2.1.3 | 60 | - |
purified native enzyme, pH 4.5, 1 h, 30% activity remaining | Penicillium oxalicum |
| 3.2.1.3 | 65 | - |
purified native enzyme, pH 4.5, 1 h, 20% activity remaining | Penicillium oxalicum |
| 3.2.1.3 | 70 | - |
purified native enzyme, pH 4.5, 1 h, inactivation | Penicillium oxalicum |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 4.5 | - |
- |
Penicillium oxalicum |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 3 | 7 | over 60% activity within this range, broad pH optimum, profile overview | Penicillium oxalicum |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.3 | 2 | 10.5 | stability range, over 80% activity remaining at pH 2.0-9.5, 75-80% activity remaining at pH 10.0-10.5, 20% at pH 11.0, inactivation above | Penicillium oxalicum |
pI Value
| EC Number | Organism | Comment | pI Value Maximum | pI Value |
|---|---|---|---|---|
| 3.2.1.3 | Penicillium oxalicum | polypeptide without the signal peptide (616 amino acid residues), sequence calculation | - |
5.5 |
General Information
| EC Number | General Information | Comment | Organism |
|---|---|---|---|
| 3.2.1.3 | evolution | the enzyme belongs to the glycosyl hydrolase family 15, GH15 | Penicillium oxalicum |
| 3.2.1.3 | malfunction | the starch-binding domain (SBD) deletion analysis reveals that SBD plays a very important role in raw starch hydrolysis by the enzyme PoGA15A | Penicillium oxalicum |
| 3.2.1.3 | additional information | the starch-binding domain (SBD) plays a very important role in raw starch hydrolysis by the enzyme PoGA15A | Penicillium oxalicum |
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Release 2023.1 (January 2023)
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