Enzymes dans les Protéines Recombinantes

<p>Poly(ADP-ribose) glycohydrolase is an enzyme, which is derived from various organisms, including eukaryotic cells. It plays a crucial role in the regulation of poly(ADP-ribose) (PAR) metabolism. This enzyme functions by hydrolyzing the glycosidic bonds in poly(ADP-ribose) chains, thereby regulating the cellular levels of PAR by converting it back to ADP-ribose units.</p>

<p>D-Ribulose 1,5-diphosphate carboxylase, commonly known as RuBisCO, is an essential enzyme that catalyzes the first major step of carbon fixation, a process by which inorganic carbon from the atmosphere is converted into organic molecules. This enzyme is derived from spinach, a common model organism used in plant biology research due to its accessibility and well-characterized photosynthetic pathways.</p>

<p>Nitrile hydratase 05 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.</p>

<p>β-1,4-Galactosyltransferase 1 is an enzyme that catalyzes the synthesis of the glycosaminoglycan-protein linkage in proteoglycans.</p>

<p>Creatinase (EC 3.5.3.3) is an enzyme that catalyzes the fellowing reaction: creatine + H2O ⇌ sarcosine + ureaOne unit of creatinase will hydrolyze 1.0 µmole of creatine into sarcosine and urea per min at pH 7.5 and 37 °C.</p>

<p>Ribonuclease A (RNase A) is widely used to break down RNA in DNA purification. RNase A catalyzes the endonucleolytic cleavage of phosphodiester bonds of RNA.</p>

<p>Amidase (EC 3.5.1.4) is a hydrolase acting on carbon-nitrogen bonds in linear amides and can be used in the hydrolysis of amides to acids. Amidase 02 is of bacterial origin (R. erythropolis and has been produced in E.coli).</p>

<p>Cellulose catalase is an enzyme-based product, designed specifically to act as a catalyst in the oxidative processes associated with cellulose applications. It is derived from a microbial source, where bacilli or fungi are employed to produce robust catalase enzymes in a fermentation process. The mode of action involves the catalase enzyme’s ability to facilitate the decomposition of hydrogen peroxide into water and oxygen, thereby reducing oxidative damage during cellulose processing.</p>

<p>Diaphorase (lipoyl dehydrogenase, EC 1.8.1.4) is an NAD+/NADH-dependent oxidoreductase. One unit of diaphorase will convert 1.0 μmole NADH into NAD+ the presence of substrate at pH 7.5 and 25 °C.</p>

<p>Citrate synthase (E.C. 2.3.3.1) is an enzyme that catalyzes the following reaction: acetyl-CoA + oxaloacetate + H2O → citrate + CoA-SHOne unit of citrate synthase will form 1.0 μmole of citrate from acetyl-CoA and oxalacetate per min at pH 8.0 and 37 °C.Origin is porcine heart.Molecular weight ~ 49kDa (monomer) and  ~ 98kDa (dimer)</p>

<p>One unit of alkaline phosphatase (EC 3.1.3.1) will hydrolyze 1.0 µmol of 4-nitrophenyl phosphate per min at 25°C and pH 9.6.</p>

<p>Recombinant Isocitrate Dehydrogenase is a bioengineered enzyme, which is derived from microbial or eukaryotic expression systems designed to mirror its naturally occurring form. This enzyme catalyzes the oxidative decarboxylation of isocitrate to alpha-ketoglutarate, utilizing NADP+ as a cofactor in the process. Its mode of action involves the conversion of isocitrate to alpha-ketoglutarate with the concomitant reduction of NADP+ to NADPH.</p>

<p>Lipoxidase is an enzyme, which is typically sourced from various plant tissues, animals, and some microorganisms. It functions by catalyzing the oxidation of polyunsaturated fatty acids in the presence of oxygen. This enzymatic action results in the formation of lipid hydroperoxides, which are key intermediates in various biochemical pathways, including those involved in cell signaling and the modulation of gene expression.</p>

<p>Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces. Lipases/esterases can be used as versatile tools in hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. The immobilized Lipase kit contains 7 different lipases, immobilised on a hydrophobic carrier either by adsorption or covalent linkage. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</p>

<p>Chymase (alternative names mast cell protease 1, mast cell serine proteinase, skeletal muscle protease, EC 3.4.21.39) is a serine protease, found in mast cells and basophil granulocytes.</p>

<p>Proteinase, Bacillus subtilis, sutilain is a proteolytic enzyme, which is derived from the bacterium Bacillus subtilis. This enzyme exhibits a serine-type mechanism of action, characterized by its ability to cleave peptide bonds in proteins efficiently. It catalyzes the hydrolysis of proteins into peptides and amino acids, facilitating the breakdown of complex proteins into simpler, soluble forms.</p>

<p>Urate Oxidase, also known as uricase, catalizes the following reaction: Uric acid + O2 + H2O → 5-hydroxyisourate + H2O2.</p>