Effect of supplementing Moringa oleifera essential oils on milk quality and fatty acid profile in dairy sheep

Abstract

Escherichia coli is the most extensively used organism in recombinant protein production. It has several advantages including a very short life cycle, ease of genetic manipulation and the well-known cell biology etc. which makes E. coli as the perfect host for recombinant protein expression. Despite many advantages, E. coli also have few disadvantages such as coupled transcription and translation and lack of eukaryotic post-translational modifications. These challenges can be overcome by adopting several strategies such as, using different E. coli expression vectors, changing the gene sequence without altering the functional domain, modified E. coli strain usage, changing the culture parameters and co-expression with a molecular chaperone. In this review, we present the level of strategies used to enhance the recombinant protein expression and its stability in E. coli.

Hyper‐production of porcine contagious pleuropneumonia subunit vaccine proteins in Escherichia coli by developing a bicistronic T7 expression system

“…Recombinant protein production has been achieved through various expression systems, including mammalian cells, insects, plants, yeast, and bacteria. [13,33,34] Among these system, E. coli has been widely utilized as a "workhorse" for the production of recombinant proteins due to its ease of manipulation, rapid growth, well-defined genetic background, and high yield capacity. [35,36] Typically, strong promoters are favored to achieve satisfactory protein yields, which is why the T7 promoter and its derived pET expression vectors are the most commonly used systems in E. coli.…”

“…These include the development of strong promoters and ribosome binding sites (RBSs), modification of host cells, and optimization of fermentation conditions. [13][14][15][16] Promoters are deemed the most effective way of controlling gene expression and can determine nearly 80% of the protein levels. Promoters from different origins, such as bacteria (Lac, tac, trp, and araBAD) and bacteriophage (T7, T5, and SP6), are commonly utilized in E. coli.…”

Hyper-production of porcine contagious pleuropneumonia subunit vaccine proteins in Escherichia coli by developing a bicistronic T7 expression system

“…To date, various expression systems have been developed for the production of recombinant proteins, including mammalian cells, insects, plants, yeast, and bacteria. [13,33,34] Among them, the Gram-negative E. coli has long been the "workhorse" of recombinant proteins due to its easy manipulation, rapid growth, clear genetic background, and high-yielding recombinant protein expression, etc. [35,36] For the recombinant expression inE.…”

“…To improve the production of recombinant proteins in E. coli , several strategies have been adopted by researchers, including developing strong promoters and ribosome binding sites (RBSs), modifying host cells, and optimizing fermentation conditions, etc. [13][14][15][16] Among them, the operation of promoters is considered the most effective way, as promoters confer direct control of the mRNA abundance for protein translation and can determine nearly 80% of the protein expression level. To date, promoters from different origins, such as bacteria (Lac, tac, trp, and araBAD) and bacteriophage (T7, T5, and SP6), have been developed and applied in E. coli .…”

Improved antimicrobial spectrum of the N-acetylmuramoyl-L-alanine amidase from Latilactobacillus sakei upon LysM domain deletion

“…Among the disadvantages of the expression of recombinant proteins is coupled transcription and translation. The variation in posttranslational modi cations or the lack of these modi cations that may be related to the loss of activity warrants thorough exploration by different strategies to explain this function (Hemamalini et al 2020).…”