EC Number | General Stability | Organism |
---|---|---|
3.2.1.2 | immobilization of beta-amylase through gel-entrapment and covalent crosslinking brings about a remarkable increase in thermotolerance with about a 14-fold increase in catalytic half-life | Priestia megaterium |
EC Number | Organism | UniProt | Comment | Textmining |
---|---|---|---|---|
3.2.1.2 | Priestia megaterium | - |
- |
- |
3.2.1.2 | Priestia megaterium B6 | - |
- |
- |
EC Number | Substrates | Comment Substrates | Organism | Products | Comment (Products) | Rev. | Reac. |
---|---|---|---|---|---|---|---|
3.2.1.2 | starch + H2O | - |
Priestia megaterium | maltose + ? | - |
? | |
3.2.1.2 | starch + H2O | - |
Priestia megaterium B6 | maltose + ? | - |
? |
EC Number | Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|---|
3.2.1.2 | additional information | - |
increased thermoresistance of beta-amylase is achieved through stabilization of thiol groups present at the active site by manipulating the enzymes environment by the addition of Mn2+ and 2-mercaptoethanol, and through immobilization. Both of which would increase the enzymes practical importance and industrial utility | Priestia megaterium |
3.2.1.2 | 60 | - |
the thermoinactivated enzyme (exposed to 60°C for 10 min) could be partially reactivated by the addition of 1 mM 2-mercaptoethanol (7.3% increase) and 4 mM Mn2+ (14% increase) | Priestia megaterium |