lldD E. coli

L-Lactate Dehydrogenase E.Coli Recombinant
Cat. No.
BT11429
Source
E.coli.
Synonyms
L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.
Appearance
Sterile Filtered colorless solution.
Purity
Greater than 90% 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.
Shipped with Ice Packs
In Stock

Description

lldD E.Coli Recombinant produced in E.coli is a single, non-glycosylated polypeptide chain containing 420 amino acids (1-396) and having a molecular mass of 45.3kDa.
lldD is fused to a 24 amino acid His-tag at N-terminus & purified by proprietary chromatographic techniques.

Product Specs

Introduction
L-lactate dehydrogenase (lldD), found in various organisms like plants and animals, is an oxidoreductase enzyme. It catalyzes the reversible conversion of pyruvate to lactate, simultaneously interconverting NADH and NAD+. Due to its ability to oxidize hydroxybutyrate, lldD is also sometimes referred to as Hydroxybutyrate Dehydrogenase (HBD).
Description
Recombinant lldD from E. coli is produced as a single, non-glycosylated polypeptide chain. It consists of 420 amino acids (residues 1-396), resulting in a molecular weight of 45.3 kDa. The protein includes an N-terminal 24 amino acid His-tag and is purified using proprietary chromatographic methods.
Physical Appearance
Clear, colorless solution, sterile filtered.
Formulation
The lldD solution is provided at a concentration of 1 mg/ml in a buffer composed of 20 mM Tris-HCl (pH 8.0), 10% glycerol, and 1 mM DTT.
Stability
For short-term storage (2-4 weeks), the product can be stored at 4°C. For extended storage, freeze at -20°C. Adding a carrier protein like 0.1% HSA or BSA is recommended for long-term storage. Avoid repeated freeze-thaw cycles.
Purity
Purity is determined to be greater than 90% by SDS-PAGE analysis.
Synonyms
L-lactate dehydrogenase [cytochrome], lldD, lctD, b3605, JW3580.
Source
E.coli.
Amino Acid Sequence
MGSSHHHHHH SSGLVPRGSH MGSHMIISAA SDYRAAAQRI LPPFLFHYMD GGAYSEYTLR RNVEDLSEVA LRQRILKNMS DLSLETTLFN EKLSMPVALA PVGLCGMYAR RGEVQAAKAA DAHGIPFTLS TVSVCPIEEV APAIKRPMWF QLYVLRDRGF MRNALERAKA AGCSTLVFTV DMPTPGARYR DAHSGMSGPN AAMRRYLQAV THPQWAWDVG LNGRPHDLGN ISAYLGKPTG LEDYIGWLGN NFDPSISWKD LEWIRDFWDG PMVIKGILDP EDARDAVRFG ADGIVVSNHG GRQLDGVLSS ARALPAIADA VKGDIAILAD SGIRNGLDVV RMIALGADTV LLGRAFLYAL ATAGQAGVAN LLNLIEKEMK VAMTLTGAKS ISEITQDSLV QGLGKELPAA LAPMAKGNAA.

Product Science Overview

Engineering E. Coli for L-Lactate Production

To enable E. coli to produce L-lactate, scientists have employed genetic engineering techniques. This involves cloning and expressing L-lactate dehydrogenase genes from different bacteria into E. coli. The process typically includes the following steps :

  1. Gene Cloning: L-LDH genes from various bacteria are cloned into plasmids.
  2. Gene Expression: These plasmids are then introduced into E. coli strains, enabling the expression of L-LDH.
  3. Metabolic Engineering: Specific genes in E. coli are deleted or modified to enhance L-lactate production. For example, deleting the ldhA gene to block D-lactate formation and deleting the lldD gene to prevent the conversion of L-lactate to pyruvate .
Recombinant L-Lactate Dehydrogenase

Recombinant L-LDH produced in E. coli is a single, non-glycosylated polypeptide chain. It typically contains 420 amino acids and has a molecular mass of approximately 45.3 kDa. The recombinant enzyme is often fused with a His-tag at the N-terminus to facilitate purification using chromatographic techniques .

Applications and Significance

The production of L-lactate using engineered E. coli has significant biotechnological applications. L-lactic acid is an important chiral molecule used in various industries, including food, pharmaceuticals, and biodegradable plastics. The ability to produce L-lactate efficiently through microbial fermentation offers a sustainable and cost-effective alternative to traditional chemical synthesis methods .

Challenges and Future Directions

One of the main challenges in producing L-lactate using E. coli is balancing the competition between cell growth and lactate synthesis. The enzymatic properties, especially the thermodynamics of L-LDH, play a crucial role in regulating metabolic pathways and optimizing lactate production. Future research aims to further enhance the efficiency of L-lactate production by exploring new genetic modifications and optimizing fermentation processes .

In conclusion, the recombinant L-Lactate Dehydrogenase from E. coli represents a significant advancement in metabolic engineering, offering promising solutions for sustainable production of valuable biochemicals.

Quick Inquiry

Personal Email Detected
Please use an institutional or corporate email address for inquiries. Personal email accounts ( such as Gmail, Yahoo, and Outlook) are not accepted. *
© Copyright 2024 Thebiotek. All Rights Reserved.