Glycerol Dehydrogenase from Cellulomonas sp.
SIGMA/G3512 - lyophilized powder, ≥50 units/mg protein
Synonym: Glycerol:NAD+ 2-oxidoreductase
EC Number: 232-824-3
MDL Number: MFCD00131206
Product Type: Chemical
Figure 1. Stability (powder form); kept under dry conditions
Figure 2. Stability (liquid form at 37 °C); buffer composition: 50 mM K-phosphate buffer buffer containing: 3.2 M ammonium sulfate and 0.2% BSA, pH 7.0
Figure 3. pH Activity; 25 °C, in 0.1 M K2CO3-NaHCO3 buffer
Figure 4. Temperature activity; in 0.1 M K2CO3-NaHCO3 buffer, pH 10.5
Figure 5. pH Stability; 25 °C, 20-hr treatment with 50 mM buffer solution: pH 4.0–6.0, acetate; pH 6.0–8.5, K2CO3-NaHCO3
Figure 6. Thermal stability; 15-min. treatment with 50 mM K-phosphate buffer, pH 7.5
This picture is provided solely for illustration purposes. Optical properties of the actual product may deviate. Relevant product information is printed on labeled products and other accompanying or available information material. This image depicts SKU: G3512-1KU
| biological source | bacterial (Cellulomonas spp.) |
| composition | Protein, ≥60% biuret |
| form | lyophilized powder |
| mol wt | ~390 kDa |
| Quality Level | 200  |
| specific activity | ≥50 units/mg protein |
| storage temp. | −20°C |
| Application: | Glycerol Dehydrogenase (GDH) from Cellulomonas sp. has been used in the determination of glycerol by sequential injection analysis (SIA) method. It has also been used in the preparation of pyrroloquinoline quinone (PQQ) based biosensor for the determination of glycerol. |
| Application: | This enzyme is useful for enzymatic determination of glycerol and of triglyceride when coupled with lipoprotein lipase in clinical analysis. Formation of NADH from the reaction of glycerol and NAD+ was catalyzed by the enzyme glycerol dehydrogenase. |
| Biochem/physiol Actions: | Glycerol dehydrogenase catalyzes the conversion of glycerol to glycerone. |
| General description: | Glycerol Dehydrogenase belongs to iron-containing alcohol dehydrogenase family. It is made up of eight identical subunits which are about 42,000 Da each. The C-terminal has histidine and the N-terminal has serine amino acid. |
| General description: | Isoelectric point : 4.4 ± 0.1 Michaelis constants : 1.1 x 10¯2M (Glycerol), 8.9 x 10¯5M (NAD+) Structure : 10 subunits (42,000) per mol of enzyme Inhibitors : p-Chloromercuribenzoate, o-phenanthroline, monoiodoacetate, heavy metal ions (Co++, Ni++, Cu++, Zn++, Cd++) Optimum pH : 10.0 – 10.5 Optimum temperature : 50°C pH Stability : pH 7.5 – 10.5 (25°C, 20hr) Thermal stability : below 55°C (pH 7.5, 15min) Substrate specificity : This enzyme has the highest specificity for glycerol and 1,2-propanediol, and also oxidizes glycerol-α-monochlorohydr glycol and 2,3-butanediol. The oxidative reaction is stimulated by K+, NH+4 and Rb+. |
| Other Notes: | One unit will oxidize 1.0 μmole of glycerol to dihydroxyacetone per min at 25 °C at pH 10.0. |
| Packaging: | 250, 1000 units in poly bottle |
| Physical form: | Lyophilized powder containing bovine serum albumin |
| RIDADR | NONH for all modes of transport |
| WGK Germany | WGK 3 |
| Flash Point(F) | Not applicable |
| Flash Point(C) | Not applicable |
| activity | specific activity: ≥50 units/mg protein |
| Storage Temp. | −20°C |
| Enzyme Commission (EC) Number | 1.1.1.6 ( BRENDA  | IUBMB ) |
| UNSPSC | 12352204 |