The present invention provides an application of a cold-active bacteriophage protein in a room temperature nucleic acid amplification reaction; the cold-active bacteriophage is selected from vB_EcoM-VR5, vB_EcoM-VR7, and vB_EcoM-VR20,vB_EcoM-VR25, or vB_EcoM-VR26, and the cold-active bacteriophage protein is a uvsX protein, a uvsY protein and a gp32 protein and/or a variant protein having corresponding functions. Preferably, the uvsX protein and the variant protein thereof are selected from any sequence of SEQ ID Nos. 1-23 or 30, the uvsY protein and the variant protein thereof are selected from any sequence of SEQ ID Nos.27-29 or 32, and the gp32 protein and the variant protein thereof are selected from any sequence of SEQ ID Nos.24-26 or 31. The present invention further provides a room temperature nucleic acid amplification reaction system containing the cold-active bacteriophage protein.

The present invention relates to a cell comprising a first nucleic acid sequence encoding a first polypeptide fused to the N-terminus of a first variant of a histidine kinase comprising a DHp domain and a CA domain, wherein said first variant does not comprise a transmembrane domain, a second nucleic acid sequence encoding a second polypeptide fused to the N-terminus of a second variant of said histidine kinase comprising a DHp domain and a CA domain, wherein said second variant does not comprise a transmembrane domain, and a third nucleic acid sequence encoding a response regulatory protein specifically phosphorylatable by said DHp domain of said first or said second variant. The present invention further relates to uses of the cell of the invention.

A portable fluidic platform for rapid and flexible end-to-end production of recombinant protein biologics includes a bioreactor system hosting stable and robust cell-free translation systems that is fluidically integrated with modular protein separation functionalities (e.g., size exclusion, ion exchange or affinity chromatography systems) for purification of the cell-free expressed product and which are configurable for process-specific isolation of different proteins, as well as for formulation. The bioreactor utilizes lysates from engineered eukaryotic (e.g., yeast) or prokaryotic (e.g., bacterial) strains that contain factors for protein folding and posttranslational modifications. Combination of various purification modules on the same fluidic platform allows flexibility of re-routing for purification of different proteins depending on specific target requirements. Protein synthesis and purification modules are integrated into self-contained disposable fluidic cartridge that eliminates cross-contamination between runs. The platform allows for flexible production of protein biologics within 24 hours (from DNA to purified product).

A biosensor for detecting nitrotoluenes. Two P. putida host populations (H-I and H-II) are engineered. H-1 undergoes fluorescence when a nitrotoluene is detected but it is also engineered to metabolize nitrotoluenes to toluene as its sole nitrogen-source. H-I is 1-ACC Deaminase inactive and is further engineered to efflux toluene and provide toluene to adjacent H-II. In H-II, ACC is the N-source and metabolizes toluene as the sole carbon and energy source available. The H-II cells are engineered to not be able to use medium fructose. The H-II population has a promoter/GFP construct with a promoter sensitive to toluene and thus they fluoresce from that first nitrotoluene metabolite i.e. toluene, produced by the H-I cells. This is achieved by making H-II cells mutants unable to transport and phosphorylate fructose i.e. PTSFRU gene knock-out.

A portable fluidic platform for rapid and flexible end-to-end production of recombinant protein biologics includes a bioreactor system hosting stable and robust cell-free translation systems that is fluidically integrated with modular protein separation functionalities (e.g., size exclusion, ion exchange or affinity chromatography systems) for purification of the cell-free expressed product and which are configurable for process-specific isolation of different proteins, as well as for formulation. The bioreactor utilizes lysates from engineered eukaryotic (e.g., yeast) or prokaryotic (e.g., bacterial) strains that contain factors for protein folding and posttranslational modifications. Combination of various purification modules on the same fluidic platform allows flexibility of re-routing for purification of different proteins depending on specific target requirements. Protein synthesis and purification modules are integrated into self-contained disposable fluidic cartridge that eliminates cross-contamination between runs. The platform allows for flexible production of protein biologics within 24 hours (from DNA to purified product).

A portable fluidic platform for rapid and flexible end-to-end production of recombinant protein biologics includes a bioreactor system hosting stable and robust cell-free translation systems that is fluidically integrated with modular protein separation functionalities (e.g., size exclusion, ion exchange or affinity chromatography systems) for purification of the cell-free expressed product and which are configurable for process-specific isolation of different proteins, as well as for formulation. The bioreactor utilizes lysates from engineered eukaryotic (e.g., yeast) or prokaryotic (e.g., bacterial) strains that contain factors for protein folding and posttranslational modifications. Combination of various purification modules on the same fluidic platform allows flexibility of re-routing for purification of different proteins depending on specific target requirements. Protein synthesis and purification modules are integrated into self-contained disposable fluidic cartridge that eliminates cross-contamination between runs. The platform allows for flexible production of protein biologics within 24 hours (from DNA to purified product).

A portable fluidic platform for rapid and flexible end-to-end production of recombinant protein biologics includes a bioreactor system hosting stable and robust cell-free translation systems that is fluidically integrated with modular protein separation functionalities (e.g., size exclusion, ion exchange or affinity chromatography systems) for purification of the cell-free expressed product and which are configurable for process-specific isolation of different proteins, as well as for formulation. The bioreactor utilizes lysates from engineered eukaryotic (e.g., yeast) or prokaryotic (e.g., bacterial) strains that contain factors for protein folding and posttranslational modifications. Combination of various purification modules on the same fluidic platform allows flexibility of re-routing for purification of different proteins depending on specific target requirements. Protein synthesis and purification modules are integrated into self-contained disposable fluidic cartridge that eliminates cross-contamination between runs. The platform allows for flexible production of protein biologics within 24 hours (from DNA to purified product).

The present disclosure provides enzymatic methods for the production of 3-phosphate-nucleoside-5-triphosphate (NQP). The present disclosure further provides enzymatic methods for the production of nucleotide-5-triphosphates.

The invention relates to a method for homo-ethanol production from lactose using a genetically modified lactic acid bacterium of the invention, where the cells are provided with a substrate comprising dairy waste supplemented with an amino nitrogen source (such as acid hydrolysed corn steep liquor). The invention further relates to genetically modified lactic acid bacterium and its use for homo-ethanol production from lactose in dairy waste. The lactic acid bacterium comprises both genes (lacABCD, LacEF, lacG) encoding enzymes catalysing the lactose catabolism pathway; and transgenes (pdc and adhB) encoding enzymes catalysing the conversion of pyruvate to ethanol. Additionally a number of genes (ldh, pta and adhE) are deleted in order to maximise homo-ethanol production as compared to production of lactate, acetoin and acetate production.

Provided are bacterial cells genetically modified to improve their tolerance to certain commodity chemicals, such as polyamines, and methods of preparing and using such bacterial cells for production of polyamines and other compounds.