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Literature summary for 3.4.21.63 extracted from
- Partial purification of an alkaline protease from a new strain of Aspergillus oryzae AWT 20 and its enhanced stabilization in entrapped Ca-alginate beads (2006), Internet J. Microbiol., 2, 0000.
No PubMed abstract available
Activating Compound
| Activating Compound | Comment | Organism | Structure |
|---|---|---|---|
| additional information | stabilization of the enzyme in entrapped Ca-alginate beads, activity maximal (ca. 48%) at 2% (w/v) sodium alginate concentration | Aspergillus oryzae |
Application
| Application | Comment | Organism |
|---|---|---|
| industry | immobilization of the enzyme as an important biotechnological aspect | Aspergillus oryzae |
Inhibitors
| Inhibitors | Comment | Organism | Structure |
|---|---|---|---|
| Hg2+ | strongly inhibits | Aspergillus oryzae |  |
| Mn2+ | slightly inhibits | Aspergillus oryzae | |
| additional information | not inhibited by Cu2+, Sn2+, Ba2+, Co2+, Li+, benzamidine, beta-ME, cysteine, EDTA and 1,10-phenathroline | Aspergillus oryzae | |
| NaN3 | slightly inhibits | Aspergillus oryzae | |
| phenylmethylsulfonyl fluoride | completely inhibits | Aspergillus oryzae | |
| TLCK | moderately inhibits | Aspergillus oryzae | |
| TPCK | moderately inhibits | Aspergillus oryzae | |
| Trypsin inhibitor | moderately inhibits | Aspergillus oryzae |
KM Value [mM]
| KM Value [mM] | KM Value Maximum [mM] | Substrate | Comment | Organism | Structure |
|---|---|---|---|---|---|
| additional information | - |
additional information | Km for the immobilized enzyme is 1.5fold higher than for the free enzyme | Aspergillus oryzae |
Metals/Ions
| Metals/Ions | Comment | Organism | Structure |
|---|---|---|---|
| Ca2+ | activates 35% at 1 mM | Aspergillus oryzae | |
| Mg2+ | activates 19% at 1 mM | Aspergillus oryzae | |
Molecular Weight [Da]
| Molecular Weight [Da] | Molecular Weight Maximum [Da] | Comment | Organism |
|---|---|---|---|
| 33000 | - |
gel filtration | Aspergillus oryzae |
Organism
| Organism | UniProt | Comment | Textmining |
|---|---|---|---|
| Aspergillus oryzae | - |
- |
- |
| Aspergillus oryzae AWT20 | - |
- |
- |
Purification (Commentary)
| Purification (Comment) | Organism |
|---|---|
| partially purified by ion exchange chromatography and gel filtration, 30fold | Aspergillus oryzae |
Specific Activity [micromol/min/mg]
| Specific Activity Minimum [µmol/min/mg] | Specific Activity Maximum [µmol/min/mg] | Comment | Organism |
|---|---|---|---|
| 25.7 | - |
crude extract | Aspergillus oryzae |
| 750 | - |
30fold purified enzyme | Aspergillus oryzae |
Substrates and Products (Substrate)
| Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
|---|---|---|---|---|---|---|
| casein + H2O | active centre of the enzyme contains serine residues | Aspergillus oryzae | hydrolyzed casein | - |
? | |
| casein + H2O | active centre of the enzyme contains serine residues | Aspergillus oryzae AWT20 | hydrolyzed casein | - |
? | |
Subunits
| Subunits | Comment | Organism |
|---|---|---|
| monomer | 1 * 33000, SDS-PAGE | Aspergillus oryzae |
Synonyms
| Synonyms | Comment | Organism |
|---|---|---|
| Alkaline protease | - |
Aspergillus oryzae |
Temperature Stability [°C]
| Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
|---|---|---|---|
| 55 | - |
immobilized enzyme retains 86% of its activity while the free enzyme retains only 10% | Aspergillus oryzae |
pH Optimum
| pH Optimum Minimum | pH Optimum Maximum | Comment | Organism |
|---|---|---|---|
| 9.5 | - |
immobilized enzyme | Aspergillus oryzae |
pH Stability
| pH Stability | pH Stability Maximum | Comment | Organism |
|---|---|---|---|
| 5.5 | 10 | immobilized enzyme, shows enhanced stability in acidic as well as alkaline environments in comparison to the free enzyme (stable between pH 7.0-9.0) | Aspergillus oryzae |
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