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Literature summary extracted from
- Structural and catalytic properties of immobilized alpha-amylase from Laceyella sacchari TSI-2 (2016), Int. J. Biol. Macromol., 85, 208-216 .
Activating Compound
| EC Number | Activating Compound | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.1 | Triton X 100 | the immobilized enzyme shows improved catalysis in presence of Triton X-100 | Laceyella sacchari |  |
| 3.2.1.1 | Tween 20 | the immobilized enzyme shows improved catalysis in presence of Tween 20 | Laceyella sacchari | |
Application
| EC Number | Application | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | industry | possible applications of the immobilized alpha-amylase in the starch processing industry | Laceyella sacchari |
Protein Variants
| EC Number | Protein Variants | Comment | Organism |
|---|---|---|---|
| 3.2.1.1 | additional information | immobilization of the alpha-amylase from Laceyella sacchari TSI-2 via entrapment, ionic binding and surface adsorption using 6 different matrices (Agar Agar, hydroxyapatite, Seralite SRA and SRC, silica + glutaraldehyde, and DEAE cellulose + glutaraldehyde), method evaluation, overview. The DEAE anion exchange cellulose with glutaraldehyde crosslinking method appears most effective for the immobilization with high operational stability. While the temperature optima and thermal stability of the immobilized alpha-amylase shift from 60°C to 70°C with increased half-life, the pH optimum remains unaltered while pH stability is shifted from pH 6.0 to pH 7.0. The stability of the immobilized enzyme improves in solvents. The enzyme catalysis in surfactants enhances, while the Km and Vmax are reduced after immobilization. Role of aliphatic amines, esters and alkenes in immobilization, structure analysis. Starch hydrolysis efficiency of the immobilized enzyme is 15.55% | Laceyella sacchari |
Inhibitors
| EC Number | Inhibitors | Comment | Organism | Structure |
|---|---|---|---|---|
| 3.2.1.1 | Tween 80 | adversely affects alpha-amylase in the immobilized state as compared to the free enzyme | Laceyella sacchari | |
KM Value [mM]
| EC Number | KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|---|
| 3.2.1.1 | additional information | - |
additional information | Lineweaver-Burke double reciprocal plot | Laceyella sacchari |
Localization
| EC Number | Localization | Comment | Organism | GeneOntology No. | Textmining |
|---|---|---|---|---|---|
| 3.2.1.1 | extracellular | the enzyme is secreted | Laceyella sacchari | - |
- |
Natural Substrates/ Products (Substrates)
| EC Number | Natural Substrates | Organism | Comment (Nat. Sub.) | Natural Products | Comment (Nat. Pro.) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | starch + H2O | Laceyella sacchari | - |
? | - |
? | |
| 3.2.1.1 | starch + H2O | Laceyella sacchari TSI-2 | - |
? | - |
? | |
Organism
| EC Number | Organism | UniProt | Comment | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | Laceyella sacchari | A0A2I7SX03 | i.e. Thermoactinomyces thalpophilus | - |
| 3.2.1.1 | Laceyella sacchari TSI-2 | A0A2I7SX03 | i.e. Thermoactinomyces thalpophilus | - |
Source Tissue
| EC Number | Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|---|
| 3.2.1.1 | additional information | bacterial strain TSI-2 is Gram-positive, with long and branching, filamentous hyphae. It grows optimally in the range of 45-60°C and pH 6-8, and it secretes alpha-amylase optimally at 50°C, pH 7.0, and 2 days of incubation time | Laceyella sacchari | - |
Substrates and Products (Substrate)
| EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|---|
| 3.2.1.1 | starch + H2O | - |
Laceyella sacchari | ? | - |
? | |
| 3.2.1.1 | starch + H2O | 0.1-2.0% starch solution | Laceyella sacchari | ? | - |
? | |
| 3.2.1.1 | starch + H2O | - |
Laceyella sacchari TSI-2 | ? | - |
? | |
| 3.2.1.1 | starch + H2O | 0.1-2.0% starch solution | Laceyella sacchari TSI-2 | ? | - |
? | |
Temperature Optimum [°C]
| EC Number | Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 50 | - |
- |
Laceyella sacchari |
Temperature Stability [°C]
| EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 50 | - |
half-life of free enzyme is 23 h, of immobilized enzyme 28 h | Laceyella sacchari |
| 3.2.1.1 | 60 | - |
half-life of free enzyme is 27 h, of immobilized enzyme 31 h | Laceyella sacchari |
| 3.2.1.1 | 70 | - |
half-life of free enzyme is 24 h, of immobilized enzyme 38 h | Laceyella sacchari |
| 3.2.1.1 | 80 | - |
half-life of free enzyme is 20 h, of immobilized enzyme 24 h | Laceyella sacchari |
pH Optimum
| EC Number | pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 7 | - |
- |
Laceyella sacchari |
pH Range
| EC Number | pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 5 | 9 | over 80% of maximal activity within this range for free and immobilized enzyme | Laceyella sacchari |
pH Stability
| EC Number | pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|---|
| 3.2.1.1 | 6 | - |
the free enzyme shows maximum stability at pH 6.0 with the residual activity at 68% after 12 h, while the immobilized enzyme at pH 7.0 retaining 80% of activity after 12 h. Overall, a 10% enhancement in the residual activities is evident for the immobilized alpha-amylase compared to the free enzyme | Laceyella sacchari |
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