Enzymes in Recombinant Proteins

<p>Glutathione peroxidase (EC 1.11.1.9) is an enzyme that reduces peroxides to limit oxidative damage, by catalyzing the following reaction:  2 GSH + H2O2 → GS–SG + 2 H2O  One unit of glutathione peroxidase will catalyze the conversion of 1.0 µmole of H2O2 per minute at pH 7.0 and 25 °C in the presence of reduced glutathione. Reduced glutahione is available here.</p>

<p>Cytochrome C oxidase (originally assigned EC 1.9.3.1, now re-assigned EC 7.1.1.9) is an enzyme that catalyzes the following reaction: 4 Fe2+ – cytochrome c + 4 H+ + O2 → 4 Fe3+ – cytochrome c + 2 H2O</p>

Protein phosphatase 2C is a key enzyme, which is a serine/threonine-specific phosphatase, derived from various organisms including humans, plants, and bacteria. This enzyme plays a pivotal role in cellular signaling by removing phosphate groups from serine and threonine residues on target proteins, a process known as dephosphorylation. This action is crucial for the regulation of diverse cellular functions, including stress responses, cell division, and apoptosis.

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 Lipase 02 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.

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 Lipase 01 from the yeast Candida rugosa has a temperature optimum in the 30 - 50 °C range and pH optimum between pH 7 and 8.

<p>Oxalate Oxidase, freeze-dried, from Wheat is an enzyme preparation which is derived from wheat and functions through the oxidative degradation of oxalate. This enzyme catalyzes the conversion of oxalate into carbon dioxide and hydrogen peroxide, utilizing oxygen as a co-substrate in the process. The activity of Oxalate Oxidase is crucial in biological and biochemical applications where oxalate degradation is required.</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 CalB01 IA lipase has been immobilized on a hydrophobic carrier by adsorption. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.

An enzyme that catalyzes the formation and breakage of disulfide bonds in the folding of proteins

<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 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>

<p>One unit will hydrolyse 1.0μmol of 4-nitrophenyl phosphate per minute at 37°C and pH 4.8.  Substrate for enzyme analysis is the 4-nitrophenyl phosphate disodium hexahydrate (EN08508).</p>

<p>L-Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: L-Asparagine + H2O → L-Aspartate + NH4+   One unit will yield 1.0 μmole of ammonia from L-asparagine per min at pH 8.6 and 37 °C.</p>

Asparaginase (EC 3.5.1.1) is an enzyme that catalyzes the following reaction: Asparagine + H2O → Aspartate + NH4+   Industrially, asparaginase is used to reduce the formation of acrylamide in starch-containing food ingredients and products during production processes. Asparaginase has a temperature optimum in the 30 – 50 °C range and pH optimum between pH 8 and 9. One unit will yield 1.0 μmole of ammonia from asparagine per min.

<p>Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications. The Phospholipase D Kit contains 4 enzymes with a broad pH range for transphosphatidylation activity.</p>

<p>Chloroperoxidase (also known as chloride peroxidase, systemic name chloride:hydrogen-peroxide oxidoreductase, EC 1.11.1.10) is an enzyme that catalyzes chlorination of organic compounds. Overall reaction is the following:R-H + Cl− + H2O2 + H+ → R-Cl + 2 H2O; reaction intermediate is hypochlorous acid (HOCl). One unit of chloroperoxidase will convert 1.0 μmole of substrate per minute.</p>

<p>Plasmin, human is a serin protease which present in the blood and is involved in the cleavage of cross-linked fibrin, a process known as fibrinolysis.One unit will produce one micromole of P-Nitroanilide from D-Val-Leu-Lys-P-Nitroanilide per minute at pH 7.5 at 37°C</p>

Lipoxidase, from glycine max (soybean)

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

<p>Aspartic acid proteinase is a type of proteolytic enzyme, which originates from various biological sources including humans, fungi, and plants. It is characterized by its action via two critical aspartic acid residues in the active site, which facilitate the hydrolysis of peptide bonds in proteins. This enzyme operates optimally in acidic environments, making it crucial in processes like digestion and protein processing within cellular compartments such as lysosomes.</p>

<p>Lipase from *Candida antarctica* is an enzyme-based biocatalyst, which is derived from the yeast *Candida antarctica*. This enzyme operates via a catalytic mechanism that involves the hydrolysis of ester bonds in lipid substrates, thereby facilitating the breakdown of fats into glycerol and free fatty acids. Its catalytic efficiency and stability in various conditions make it highly versatile for industrial applications.</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 CalB01 ICE lipase has been immobilized on a hydrophobic carrier by a covalent linkage. The immobilized CalB01 lipase has a temperature optimum in the 40 - 50 °C range and pH optimum between pH 5 and 8.</p>