Enzyme

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.

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.

Glucose-6-phosphate isomerase (GPI, phosphoglucose isomerase/phosphoglucoisomerase, PGI, phosphohexose isomerase, PHI; EC 5.3.1.9) is an enzyme that catalyses isomerisation between Glucose-6-phosphate and Fructose-6-phosphate:  G6P ⇌ F6P  One unit of GPI will convert 1.0 mmole of Fructose-6-phosphate to Glucose-6-phosphate per minute at pH 7.4 and 25 °C.

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)

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.

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.

Alcohol dehydrogenase (EC 1.1.1.1) is the enzyme that catalyzes interconversion between alcohols and aldehydes or ketones, using NAD+/NADH as a cofactor in the following reaction: CH3CH2OH + NAD+ ⇔ CH3CHO + NADH + H+     One unit of alcohol dehydrogenase will convert 1.0 µmol of ethanol to acetaldehyde per minute at pH 8.8 and 25 °C.

Neuron-specific enolase human (ENO2, Enolase 2, Neural enolase, Gamma-enolase, Phosphopyruvate hydratase, 2-phospho-D-glycerate hydro-lyase; EC 4.2.1.11) is the enzyme that is catalyzes the following reaction:  2-phospho-D-glycerate ⇌ phosphoenolpyruvate + H2O  One unit of enolase will convert 1.0 μmole of 2-phosphoglycerate to phosphoenolpyruvate per min.

Superoxide dismutase is an enzyme that catalyzes the conversion of harmful superoxide into hydrogen peroxide and oxygen.

E. coli recombinant sialic acid aldolase (EC 4.1.3.3) from Pasteurella multocida.  One unit is defined as the amount of enzyme that catalyses the formation of 1 umol Neu5Ac from ManNAc and Pyruvate per minute at 37 ℃.Activity: 9U/mg

E. coli recombinant α-2,6 sialyltransferase from Neisseria meningitidis. One unit is defined as the amount of enzyme that catalyses the formation of 1 μmol CMP-Neu5Ac from CTP and Neu5Ac per minute at 37 ºC.Activity: 100U/mg

A protease enzyme from bacillus subtilis which catalyzed proteolysis, a process that breaks down proteins and peptides to small polypeptides or amino acids

Glucosidases are enzymes belonging to the family of oxidoreductases. They catalyse the hydrolysis of starches to simple sugars. Glucosidase is widely used in the food, carbohydrate and biofuels industries. In recent years, its applicability has expanded to biotechnology for its potential application in bioenzymatic fuel cells.

A proteolytic enzyme synthesized by the HIV cell as part of the GagPol polyprotein

DNase I (Deoxyribonuclease I, EC 3.1.21.1) is an endonuclease that cleaves DNA, yielding 5'-phosphate-terminated polynucleotides with a free hydroxyl group on position 3'. On average it produces tetranucleotides. One unit of the DNase I will increase the absorbance of 260nm light at a rate of 0.001/minute in 1 ml reaction volume at 25°C.

From pigeon breast muscle - Carnitine acetyltransferase (EC 2.3.1.7, also Carnitine O-acetyltransferase) is an enzyme that catalyzes the following chemical reaction: acetyl-CoA + carnitine ⇌ CoA + acetylcarnitine

Cholesterol oxidase (EC 1.1.3.6) is an enzyme that catalyzes the following reaction: cholesterol + O2 ⇌ cholest-4-en-3-one + H2O2One unit of cholesterol oxidase will convert 1.0 μmole of cholesterol into cholest-4-en-3-one per min at pH 7.5 and 25 °C. You can remove the build-up of hydrogen peroxide using catalase.

Poly(ethylene terephthalate) hydrolase is an enzyme involved in the breakdown of Polyethylene terephthalate which is present in many plastics Polyethylene terephthalate hydrolytic enzymes may be useful in biotechnology, for use in waste treatment, biocatalysis and biorecycling