Protein stability is a topic of major interest for the biotechnology, pharmaceutical and food
industries, in addition to being a daily consideration for academic researchers studying …

Escherichia coli is the most preferred microorganism to express heterologous proteins for
therapeutic use, as around 30% of the approved therapeutic proteins are currently being …

A novel method for the adaptation of target gene codon usage to most sequenced
prokaryotes and selected eukaryotic gene expression hosts was developed to improve …

Preparations enriched by a specific protein are rarely easily obtained from natural host cells.
Hence, recombinant protein production is frequently the sole applicable procedure. The …

Although it is usually possible to achieve a favorable yield of a recombinant protein in
Escherichia coli, obtaining the protein in a soluble, biologically active form continues to be a …

Reverse vaccinology (RV) was described at its inception in 2000 as an in silico process that
starts from the genomic sequence of the pathogen and ends with a list of potential protein …

Faithful translation of mRNA into the corresponding polypeptide is a complex multistep
process, requiring accurate amino acid selection, transfer RNA (tRNA) charging and mRNA …

Recombinant protein expression in Escherichia coli (E. coli) is simple, fast, inexpensive, and
robust, with the expressed protein comprising up to 50 percent of the total cellular protein …

The efficiency of heterologous protein production in Escherichia coli (E. coli) can be
diminished by biased codon usage. Approaches normally used to overcome this problem …

The efficient in vivo folding of many heterologous proteins is a major bottleneck of high level
production in bacterial hosts and simple optimisation protocols have not been available yet …