G4783
甘油脱氢酶 来源于产气肠杆菌
lyophilized powder, 20-80 units/mg protein, pH 10.0
别名:
甘油:NAD+ 2-氧化还原酶
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
含磷酸钾缓冲盐的冻干粉
Other Notes
在 25°C 和 pH 10.0 下，一单位每分钟可氧化 1.0μmol 的甘油生成二羟基丙酮。
signalword
Danger
hcodes
pcodes
Hazard Classifications
Resp. Sens. 1
存储类别
11 - Combustible Solids
wgk
WGK 3
flash_point_f
Not applicable
flash_point_c
Not applicable
ppe
Eyeshields, Gloves, type N95 (US)
法规信息
新产品
此项目有
Yuanhao Wang et al.
Journal of industrial microbiology & biotechnology, 38(6), 705-715 (2010-09-03)
The microbial production of 1,3-propaneidol (1,3-PD) by Klebsiella pneumoniae in continuous fermentation was investigated under low, medium and high glycerol concentrations in the absence and presence of oxygen. The production of 1,3-PD increased with increasing glycerol concentrations, reaching a maximum
Longpan Tang et al.
Wei sheng wu xue bao = Acta microbiologica Sinica, 51(4), 504-509 (2011-07-30)
To improve expression level of glycerol dehydrogenase gene gldA in Escherichia coli by means of codon optimization. For immediately downstream region of initiation codon in gldA, we designed optimized sequence by choosing higher AT-content synonymous, in order that this region's
Min Wu et al.
ACS applied materials & interfaces, 3(9), 3300-3307 (2011-08-05)
Microfloccules of TiO(2) nanoparticles, on which glycerol-dehydrogenase (GDH), 1,3-propanediol-oxidoreductase (PDOR), and glycerol-dehydratase (GDHt) were coimmobilized, were prepared by adsorption-flocculation with polyacrylamide (PAM). The catalytic activity of immobilized enzyme in the glycerol redox reaction system, the enzyme leakage, stabilities of pH
Shuo Yao et al.
Applied microbiology and biotechnology, 88(1), 199-208 (2010-06-17)
Thermoanaerobacter mathranii can produce ethanol from lignocellulosic biomass at high temperatures, but its biotechnological exploitation will require metabolic engineering to increase its ethanol yield. With a cofactor-dependent ethanol production pathway in T. mathranii, it may become crucial to regenerate cofactor
A NAD specific glycerol dehydrogenase from Aerobacter aerogenes.
R.M. Burton & N.O. Kaplan
Journal of the American Chemical Society, 75, 1005-1007 (1953)
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