Enzymes dans les Protéines Recombinantes

<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>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 CalB02 ICE lipase has been immobilized on a hydrophobic carrier by a covalent linkage. The immobilized CalB02 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</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>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>

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>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>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>

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>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>

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.

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.

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.

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.

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

Aconitase catalyzes isomerization of citrate to isocitrate via cis-aconitate. Systemic enzyme name is aconitate hydratase; EC 4.2.1.3.

<p>Specific activity: &gt;500 units/mg-protein.Unit definition: One unit will polymerize 1.0 micro mole of ADP, releasing 1.0 micro mole of inorganic phosphate in 15 minutes at pH 9.1 at 37 °C.</p>

Aminopeptidase I is a specialized proteolytic enzyme derived from the actinobacterium Streptomyces griseus. This enzyme functions by catalyzing the cleavage of amino acids from the N-terminus of peptides, which plays a pivotal role in protein metabolism and regulation. The source of this enzyme, Streptomyces griseus, is well-regarded for producing a variety of bioactive compounds owing to its rich genetic and biochemical repertoire.