Application | Comment | Organism |
---|---|---|
synthesis | yeast alcohol dehydrogenase with its cofactor NAD+ can be stably encapsulated in liposomes composed of 1-palmitoyl-2-oleoyl-sn-glycero-3-phosphocholine. The liposomes are 100 nm in mean diameter, the liposomal ADH and NAD+ concentrations are 2.3 mg/ml and 3.9 mM, respectively. Free ADH is increasingly deactivated during its incubation at 45°C for 2 h with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric ADH into its subunits. Both liposomal enzyme systems, in presence and absence of NAD+, show stabilities at both 45 and 50°C much higher than those of the free enzyme systems, implying that the liposome membranes stabilize the enzyme tertiary and quaternary structures. The enzyme activity of the liposomes in presence of NAD+ show a stability higher than that in absence of NAD+ with a more remarkable effect of NAD+ at 50°C than at 45°C | Saccharomyces cerevisiae |
General Stability | Organism |
---|---|
even at 50°C the stabilization effect of lipid membranes on the tertiary and quaternary structures of the liposomal YADH allows the enzyme to form its thermostable complex with NAD+ in liposomes | Saccharomyces cerevisiae |
Organism | UniProt | Comment | Textmining |
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Saccharomyces cerevisiae | - |
- |
- |
Source Tissue | Comment | Organism | Textmining |
---|---|---|---|
commercial preparation | - |
Saccharomyces cerevisiae | - |
Synonyms | Comment | Organism |
---|---|---|
YADH | - |
Saccharomyces cerevisiae |
Temperature Stability Minimum [°C] | Temperature Stability Maximum [°C] | Comment | Organism |
---|---|---|---|
45 | - |
2 h, free YADH is increasingly deactivated during its incubation with decrease of the enzyme concentration from 3.3 to 0.01 mg/ml because of the dissociation of tetrameric YADH into its subunits | Saccharomyces cerevisiae |