Application | Comment | Organism |
---|---|---|
additional information | stabilization of enzyme against thermal denaturation by intermolecular and intramolecular crosslinking of the surface nucleophilic functional groups with diisocyanate homobifunctional reagents of various lengths. Crosslinking with 1,4-diisocyanatobutane is most effective in enhancing thermostability. Stability is improved dramatically by crosslinking 0.5 mg/ml of protein with 30 micromol/ml of the reagent. Molecular engineering by crosslinking reduces the first-order thermal denaturation constant at 60°C from 1.567 per min for the native enzyme to 0.437 per min for the stabilized enzyme. The best crosslinking treatment increases the activation energy for denaturation from 391 kJ per mol for the native protein to 466 kJ per mol for the stabilized enzyme | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
---|---|---|---|
Saccharomyces cerevisiae | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Saccharomyces cerevisiae | - |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
additional information | - |
stabilization of enzyme against thermal denaturation by intermolecular and intramolecular crosslinking of the surface nucleophilic functional groups with diisocyanate homobifunctional reagents of various lengths. Crosslinking with 1,4-diisocyanatobutane is most effective in enhancing thermostability. Stability is improved dramatically by crosslinking 0.5 mg/ml of protein with 30 micromol/ml of the reagent. Molecular engineering by crosslinking reduces the first-order thermal denaturation constant at 60°C from 1.567 per min for the native enzyme to 0.437 per min for the stabilized enzyme. The best crosslinking treatment increases the activation energy for denaturation from 391 kJ per mol for the native protein to 466 kJ per mol for the stabilized enzyme | Saccharomyces cerevisiae |