Glycerol Dehydrogenase from Cellulomonas sp.

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.

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-monochlorohydrin, ethylene
glycol and 2,3-butanediol. The oxidative reaction is stimulated by K⁺, NH⁺4 and Rb⁺.

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.

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.

Glycerol dehydrogenase catalyzes the conversion of glycerol to glycerone.

Lyophilized powder containing bovine serum albumin

One unit will oxidize 1.0 μmole of glycerol to dihydroxyacetone per min at 25 °C at pH 10.0.