A thorough characterisation of the genetics, physiology and metabolism of Escherichia coli
has led to the availability of a large number of strains and vectors suitable for recombinant …

Virtually all recombinant proteins are now prepared using fusion domains also known as
“tags”. The use of tags helps to solve some serious problems: to simplify procedures of …

Many goals in synthetic biology, including the elucidation and refactoring of biosynthetic
pathways and the engineering of regulatory circuits and networks, require knowledge of …

The self-assembly of micellar structures from diblock polymers that contain hydrophilic and
hydrophobic domains has been of great interest for the encapsulation of drugs and other …

Purification of recombinant proteins is often achieved using a purification tag which can be
located either at the N-or C-terminus of a passenger protein of interest. Many purification …

Short-chain esters have broad utility as flavors, fragrances, solvents, and biofuels.
Controlling selectivity of ester microbial biosynthesis has been an outstanding metabolic …

(1) Background: Producing active antimicrobial peptides with disulfide bonds in bacterial
strains is challenging. The cytoplasm of Escherichia coli has a reducing environment, which …

Background The high level of excretion and rapid folding ability of β-fructofuranosidase (β-
FFase) in Escherichia coli has suggested that β-FFase from Arthrobacter arilaitensis …

Advances in structural biology have been fueled in part by developing techniques for large-
scale heterologous expression and purification of proteins. Nevertheless, this step is still a …

Abstract Heparinase I (Hep I) can efficiently depolymerize heparin and heparin sulfate to
oligosaccharides or unsaturated disaccharides, which resulted in loss of physiological …