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Literature summary for 3.2.1.1 extracted from
- Immobilization of a thermostable alpha-amylase by covalent binding to an alginate matrix increases high temperature usability (2009), Biotechnol. Prog., 25, 436-445.
Application
| Application | Comment | Organism |
|---|---|---|
| industry | the high cumulative activity and seven successive reuses obtained at liquefaction temperature render the covalently bound thermostable enzyme to calcium alginate matrix, a promising candidate for use in industrial starch hydrolysis process | Bacillus licheniformis |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
potato starch | free enzyme, Km: 0.4 mg/ml, Vmax: 25 mg starch degraded/ml/min/mg protein, immobilized enzyme, first use, Km: 0.98 mg/ml, Vmax: 23.3 mg starch degraded/ml/min/mg protein, first reuse, Km: 1.75 mg/ml, Vmax: 10.4 mg starch degraded/ml/min/mg protein. The higher Km value and the lower affinity for the substrate caused by diffiusional limitations and steric effects leading to a decrease in the accessibility of substrate to the enzyme active site | Bacillus licheniformis |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| CaCl2 | the reusability of the immobilized enzymes are similar in starch hydrolysis reaction medium containing either 5 mM or 0.25 mM CaCl2 | Bacillus licheniformis |  |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Bacillus licheniformis | - |
- |
- |
Source Tissue
| Source Tissue | Comment | Organism | Textmining |
|---|---|---|---|
| commercial preparation | - |
Bacillus licheniformis | - |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| potato starch + H2O | - |
Bacillus licheniformis | ? | - |
? | |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| liquozyme | commercial preparation, free and immobilzed enzyme, covalently bound to calcium alginate matrix | Bacillus licheniformis |
| thermostable alpha-amylase | free and immobilzed enzyme, covalently bound to calcium alginate matrix | Bacillus licheniformis |
Temperature Optimum [°C]
| Temperature Optimum [°C] | Temperature Optimum Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
assay at | Bacillus licheniformis |
Temperature Range [°C]
| Temperature Minimum [°C] | Temperature Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 50 | - |
ca. 40% of the activity at 95°C is attained | Bacillus licheniformis |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 95 | - |
covalent binding of thermostable alpha-amylase on calcium alginate provides a 80% activity based on the immobilized protein for the first cycle and hydrolyzes a total of 51 mg starch/s/mg protein after seven cycles at 95°C | Bacillus licheniformis |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | - |
optimum of free enzyme and assay at | Bacillus licheniformis |
| 6 | - |
optimum of immobilized enzyme | Bacillus licheniformis |
pH Range
| pH Minimum | pH Maximum | Comment | Organism |
|---|---|---|---|
| 4 | 8 | free enzyme, pH 4: ca. 5% relative activity, pH 8.0: ca. 12% relative activity, pH-optimum: 5.5 | Bacillus licheniformis |
| 4.5 | 8 | first and second use of immobilzed enzyme, first use: pH 4.5 ca. with 4% relative activity, pH 8.0 with ca. 25% relative activity, second use: pH 4.5 with ca. 22% relative activity, pH 8.0 with ca. 11% relative activity, pH-optimum: 6.0 | Bacillus licheniformis |
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