Industrial Relevance of Trichoderma reesei as an Enzyme Producer.

Trichoderma reesei's potential as a rapid and efficient biomass degrader was first recognized in the 1950s when it was isolated from Army textiles during World War II. The microbe secreted cellulases that were degrading cotton-based tents and clothing of service members stationed on the Solomon Islands. In the 1970s, at the time of the first global oil crisis, research interest in T. reesei gained popularity as it was explored as part of the solution to the worlds growing dependence on fossil fuels. Much of this early work focused on classical mutagenesis and selection of hypercellulolytic strains. This early lineage was used as a starting point for both academic research with the goal of understanding secretion and regulation of expression of the complex mixture of enzymes required for cellulosic biomass decay as well as for its development as a host for industrial enzyme production. In 2001, at the onset of the second major oil crisis, the US Department of Energy supported research programs in microbial cellulases to produce ethanol from biomass which led to another surge in the study of T. reesei. This further accelerated the development of molecular biology and recombinant DNA tools in T. reesei. In addition to T. reesei's role in bio-ethanol production, it is used to produce industrial enzymes with a broad range of applications supporting the bio-based economy. To date there are around 243 commercially available enzyme products manufactured by fermentation of microorganisms; 30 of these are made using Trichoderma as a host, 21 of which are recombinant products sold for use in food, feed, and technical applications including textiles and pulp and paper.

Global transcriptional response of Bacillus subtilis to treatment with subinhibitory concentrations of antibiotics that inhibit protein synthesis.

Global gene expression patterns of Bacillus subtilis in response to subinhibitory concentrations of protein synthesis inhibitors (chloramphenicol, erythromycin, and gentamicin) were studied by DNA microarray analysis. B. subtilis cultures were treated with subinhibitory concentrations of protein synthesis inhibitors for 5, 15, 30, and 60 min, and transcriptional patterns were measured throughout the time course. Three major classes of genes were affected by the protein synthesis inhibitors: genes encoding transport/binding proteins, genes involved in protein synthesis, and genes involved in the metabolism of carbohydrates and related molecules. Similar expression patterns for a few classes of genes were observed due to treatment with chloramphenicol (0.4x MIC) or erythromycin (0.5x MIC), whereas expression patterns of gentamicin-treated cells were distinct. Expression of genes involved in metabolism of amino acids was altered by treatment with chloramphenicol and erythromycin but not by treatment with gentamicin. Heat shock genes were induced by gentamicin but repressed by chloramphenicol. Other genes induced by the protein synthesis inhibitors included the yheIH operon encoding ABC transporter-like proteins, with similarity to multidrug efflux proteins, and the ysbAB operon encoding homologs of LrgAB that function to inhibit cell wall cleavage (murein hydrolase activity) and convey penicillin tolerance in Staphylococcus aureus.