G4783
Glycerol Dehydrogenase from Enterobacter aerogenes
lyophilized powder, 20-80 units/mg protein, pH 10.0
Synonym(s):
Glycerol:NAD+ 2-oxidoreductase
form
lyophilized powder
specific activity
20-80 units/mg protein, pH 10.0
composition
Protein, 50-75% biuret
storage temp.
−20°C
Application
Glycerol dehydrogenase was used in the kinetic enzymatic determination of glycerol in wine and beer.
Biochem/physiol Actions
Glycerol dehydrogenase catalyzes the conversion of glycerol to glycerone.
Physical form
Lyophilized powder containing potassium phosphate buffer salts
Other Notes
One unit will oxidize 1.0 μmole of glycerol to dihydroxyacetone per min at 25 °C at pH 10.0.
Signal Word
Danger
Hazard Statements
Precautionary Statements
Hazard Classifications
Resp. Sens. 1
Storage Class Code
11 - Combustible Solids
WGK
WGK 3
Flash Point(F)
Not applicable
Flash Point(C)
Not applicable
Personal Protective Equipment
dust mask type N95 (US), Eyeshields, Gloves
Regulatory Information
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Hugo M Oliveira et al.
Journal of agricultural and food chemistry, 54(12), 4136-4140 (2006-06-08)
A sequential injection system for the automatic determination of glycerol in wine and beer was developed. The method is based on the rate of formation of NADH from the reaction of glycerol and NAD+ catalyzed by the enzyme glycerol dehydrogenase
Lian Hua Luo et al.
Journal of industrial microbiology & biotechnology, 38(8), 991-999 (2010-09-24)
Previously, we constructed a glycerol oxidative pathway-deficient mutant strain of Klebsiella pneumoniae by inactivation of glycerol dehydrogenase (dhaD) to eliminate by-product synthesis during production of 1,3-propanediol (1,3-PD) from glycerol. Although by-product formation was successfully blocked in the resultant strain, the
A glycerol dehydrogenase from Escherichia coli.
R E ASNIS et al.
The Journal of biological chemistry, 203(1), 153-159 (1953-07-01)
Won-Kyung Hong et al.
Bioprocess and biosystems engineering, 34(2), 231-236 (2010-09-08)
Currently, 1,3-propanediol (1,3-PD) is an important chemical widely used in polymer production, but its availability is being restricted owing to its expensive chemical synthesis. A methylotrophic yeast Hansenula polymorpha was engineered by expression of dhaB1, dhaB2, dhaB3, dhaB(RA1) and dhaB(RA2)
Hiroshi Habe et al.
Bioscience, biotechnology, and biochemistry, 74(11), 2330-2332 (2010-11-13)
To prevent dihydroxyacetone (DHA) by-production during glyceric acid (GA) production from glycerol using Gluconobacter frateurii, we used a G. frateurii THD32 mutant, ΔsldA, in which the glycerol dehydrogenase subunit-encoding gene (sldA) was disrupted, but ΔsldA grew much more slowly than
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