GLDA E.coli
Glycerol dehydrogenase E.coli Recombinant
Cat. No.
BT8831
Source
Escherichia Coli.
Synonyms
ECK3937,
JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 95.0% as determined by SDS-PAGE.
Usage
THE BioTek's products are furnished for LABORATORY RESEARCH USE ONLY. The product may not be used as drugs, agricultural or pesticidal products, food additives or household chemicals.
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Description
GLDA E.coli Recombinant produced in E.Coli is a single, non-glycosylated polypeptide chain containing 390 amino acids (1-367 a.a) and having a molecular mass of 41.1kDa.
GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
GLDA is fused to a 23 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.
Product Specs
Introduction
Glycerol dehydrogenase (GldA) is an enzyme that catalyzes the reversible oxidation of glycerol to dihydroxyacetone using NAD+ as a cofactor. This allows microorganisms like E.coli to utilize glycerol as a carbon source in anaerobic environments. In E.coli, GldA also plays a crucial role in regulating the intracellular concentration of dihydroxyacetone by catalyzing the reverse reaction, converting dihydroxyacetone back to glycerol. GldA exhibits broad substrate specificity, enabling it to oxidize 1,2-propanediol and reduce glycolaldehyde, methylglyoxal, and hydroxyacetone to ethylene glycol, lactaldehyde, and 1,2-propanediol, respectively.
Description
Recombinant GLDA from E.coli, expressed in E.Coli, is a single, non-glycosylated polypeptide chain containing 390 amino acids. A 23 amino acid His-tag is fused to the N-terminus of the 367 amino acid GLDA protein, resulting in a molecular mass of 41.1kDa. The protein has been purified using proprietary chromatographic techniques.
Physical Appearance
A clear, colorless solution that has been sterilized by filtration.
Formulation
The GLDA protein is supplied as a 1mg/ml solution in phosphate-buffered saline (pH 7.4) with 10% glycerol.
Stability
For short-term storage (2-4 weeks), the protein can be stored at 4°C. For long-term storage, it is recommended to store the protein at -20°C. The addition of a carrier protein such as HSA or BSA (0.1%) is recommended for extended storage. Avoid repeated freeze-thaw cycles.
Purity
The purity of the GLDA protein is greater than 95.0% as determined by SDS-PAGE analysis.
Synonyms
ECK3937,
JW5556, Glycerol dehydrogenase, GDH, GLDH, b3945.
Source
Escherichia Coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSMDRIIQS PGKYIQGADV INRLGEYLKP LAERWLVVGD KFVLGFAQST
VEKSFKDAGL VVEIAPFGGE CSQNEIDRLR GIAETAQCGA ILGIGGGKTL DTAKALAHFM GVPVAIAPTI
ASTDAPCSAL SVIYTDEGEF DRYLLLPNNP NMVIVDTKIV AGAPARLLAA GIGDALATWF EARACSRSGA
TTMAGGKCTQ AALALAELCY NTLLEEGEKA MLAAEQHVVT PALERVIEAN TYLSGVGFES GGLAAAHAVH
NGLTAIPDAH HYYHGEKVAF GTLTQLVLEN APVEEIETVA ALSHAVGLPI TLAQLDIKED VPAKMRIVAE
AACAEGETIH NMPGGATPDQ VYAALLVADQ YGQRFLQEWE.
Product Science Overview
Recombinant Expression in E. coli
The recombinant expression of GDH in E. coli involves the insertion of the gene encoding GDH into the bacterial genome. This process is facilitated by the use of plasmids, which are small, circular DNA molecules that can replicate independently within bacterial cells. The gene encoding GDH is typically obtained from other microorganisms, such as Klebsiella pneumoniae, and inserted into E. coli using a shuttle vector .
Significance in Biotechnology
The recombinant expression of GDH in E. coli has several biotechnological applications:
- Biofuel Production: GDH is used to convert glycerol, a by-product of biodiesel production, into valuable chemicals like 2,3-butanediol. This conversion process not only helps in managing the surplus glycerol but also produces a compound that can be used as a fuel additive .
- Protein Production: Recombinant E. coli strains expressing GDH are employed in the production of various recombinant proteins. The manipulation of glycerol metabolism in these strains can lead to a significant increase in protein yield, making the process more economically viable .
- Metabolic Engineering: The expression of GDH in E. coli is a key step in metabolic engineering efforts aimed at optimizing the bacterial metabolism for the production of specific compounds. By rewiring the glycerol metabolism pathway, researchers can enhance the production of target metabolites .
Challenges and Solutions
One of the primary challenges in the recombinant expression of GDH in E. coli is the efficient utilization of glycerol. E. coli naturally has a limited ability to metabolize glycerol, which can hinder the overall efficiency of the process. To address this, researchers have developed strategies to rewire the glycerol metabolism pathway, thereby improving the utilization of glycerol and enhancing the production of desired compounds .
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