Enzima

Lipase 77 recombinantly expressed in P. pastoris comes in a spray-dried formulation. It has its pH optimum at 4-5. Lipases belong to the family of esterases and naturally act on triglycerides at lipid-water interfaces catalyzing hydrolytic reactions, esterifications and transesterification reactions in industrial and food applications. Lipase 77 was shown to hydrolyze p-Nitrophenyl esters of butyrate and triglycerides.

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.

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.

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.

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.

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.

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

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

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

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

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

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

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.

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.

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