Enzimi nelle Proteine Ricombinanti

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

Protease enzymes break down proteins and are essential for many biological processes, including digestion, cellular regulation and blood clotting. They are also used in many industrial and biotechnological applications for example in food processing and in detergents.

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

Invertase is an enzyme that catalyzes the hydrolysis of sucrose to glucose and fructose and can be found in plants and microorganisms

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

Cocarboxylase hydrochloride is a coenzyme derivative, which is primarily sourced from thiamine (vitamin B1). It plays a crucial role in biochemical processes by facilitating the enzymatic decarboxylation of alpha-keto acids within the cellular environment. This action is fundamental in energy production as it aids in the conversion of pyruvate to acetyl-CoA, subsequently entering the citric acid cycle. Cocarboxylase hydrochloride’s involvement in carbohydrate metabolism is especially vital for tissues with high metabolic rates, such as the heart and brain.

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.

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

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

Oxalate Oxidase, freeze-dried, is an enzymatic preparation that serves as a catalyst in biochemical reactions. This enzyme is derived from wheat, a common plant source, ensuring a naturally occurring origin. Its primary mode of action is the oxidation of oxalate into carbon dioxide and hydrogen peroxide. This biochemical activity is significant in various scientific applications, specifically in the breakdown of oxalate, which plays a crucial role in metabolic and environmental processes.

Triose-phosphate isomerase (TPI, TIM; EC 5.3.1.1) is an enzyme that catalyzes the reversible isomerisation of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate:  DHAP ⇌ GADP  The reaction mechanism involves the formation of an enediol intermediate. One unit of Triose-phosphate isomerase will convert 1.0 μmole glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 and 25 °C.

Sulfatase from Helix pomatia is a highly potent enzyme that is capable of hydrolyzing sulfated compounds and sulfate esters. It has been widely used in various applications such as glucosinolate analysis, genistein extraction preparation, and regiospecificity studies. With a concentration of ≥10,000 units per gram of solid, this sulfatase offers exceptional enzymatic activity for sulfatase assays. It effectively catalyzes the hydrolysis of sulfated substrates, including p-nitrocatechol sulfate, naphthyl sulfate and phenyl sulfates.The enzyme can be incubated with the desired sample to facilitate the release of sulfate groups from sulfated compounds. Sulfatase from Helix pomatia is a valuable tool for researchers and scientists working in diverse fields requiring efficient and reliable enzymatic hydrolysis capabilities. Additionally the enzyme has been found to have industrial applications, such as in the bioconversion of industrial chemicals, where it can be used as a catalyst.

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.