Pure, soluble and functional proteins are of high demand in modern biotechnology. Natural
protein sources rarely meet the requirements for quantity, ease of isolation or price and …

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 …

Micro-organisms react to a rapid temperature downshift by triggering a physiological
response to ensure survival in unfavourable conditions. Adaptation includes changes in …

Different species of microorganisms including yeasts, filamentous fungi and bacteria have
been used in the past 25 years for the controlled production of foreign proteins of scientific …

Despite its being a leading cause of nosocomal and community-acquired infections,
surprisingly little is known about Staphylococcus aureus stress responses. In the current …

Members of a family of small cold-shock proteins (CSPs) are induced during bacterial cell
response to a temperature decrease. Here we review available data about the structure …

The aggregation-prone fusion protein preS2–S′–β-galactosidase was used as a model
system to compare the efficiencies of the IPTG-inducibletacpromoter and the low …

The expression of correctly folded and functional heterologous proteins is important in many
biotechnological production processes, whether it is enzymes, biopharmaceuticals or …

Here we describe a method for controlled intracellular processing (CIP) of fusion proteins by
tobacco etch virus (TEV) protease. A fusion protein containing a TEV protease recognition …

Increasing evidence indicates that protein aggregation in bacteria does not necessarily
imply loss of biological activity. Here, we have investigated the effect of growth-temperature …