Enzimas en Proteínas Recombinantes

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.

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.

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.

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

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.

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.

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.

Phosphorylase B is an enzymatic protein, specifically an isoform of glycogen phosphorylase, derived from rabbit muscle. This enzyme plays a critical role in glycogen metabolism by catalyzing the phosphorolytic cleavage of α(1→4) glycosidic bonds in glycogen, releasing glucose-1-phosphate. The rabbit muscle source provides a well-studied model due to its high enzyme activity and availability, facilitating in-depth biochemical and structural analysis.

Nitrile hydratase 23 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.

Sphingomyelinase (SMase, Sphingomyelin phosphodiesterase, systematic name sphingomyelin cholinephosphohydrolase; EC 3.1.4.12) is an enzyme that hydrolyses sphingomyelin into phosphocholine and ceramide. One unit of sphingomyelinase will hydrolyze 1.0 µmole of chromogenic substrate analogue per minute at pH 7.4 and 37 °C.

Nitrilase (nitrile aminohydrolase; EC 3.5.5.1) in an enzyme that catalyzes hydrolysis of nitriles to carboxilic acids and ammonia:  R-CN + 2 H2O → R-COO- + NH4+  One unit of nitrilase will yield 1.0 μmol of ammonia per minute under optimal reaction conditions using acrylonitrile as a substrate.

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.

α-Mannosidase (α-D-mannopyranosidase, 1,2-α-mannosidase, 1,2-α-D-mannosidase, exo-α-mannosidase, α-D-mannosidase, systematic name α-D-mannoside mannohydrolase; EC 3.2.1.24) is an enzyme that cleaves α-mannose to produce glucose. One unit of α-Mannosidase will hydrolyze 1.0 µmole of chromogenic phosphate mimic p-nitrophenyl-α-p-mannoside to p-nitrophenol in 1 minute at pH 5.0 and 37°C.

eXrase DNA endonuclease from enGenes is a recombinant endonuclease from Serratia marcescens produced in E. coli. Effectively and efficiently degrades all forms of DNA and RNA, reducing sample viscosity without proteolytic activity. As effective and efficient as other nucleases on the market, eXrase DNA endonuclease is the most cost-effective way to improve proteins yields and improve sample handing. Presented as a ready to use colourless liquid, formulated in Tris buffer at pH 8.0 with 50 % glycerol (v/v).  This research grade eXrase has low endotoxin, max 0.25 EU/kU.eXrase DNA endonuclease is suitable for the effective breakdown of nucleic acids in numerous biotech settings:  • Removal of residual host DNA from biotechnological products to meet regulatory standards • Reduction of viscosity and streamlined purification in downstream processing of fermentation procedures. • Reduction of viscosity in in upstream fermentation processes • Extraction and/or synthesis of flavouring nucleotides • Enhanced bioavailability of nucleotides in specific feed products • DNA degradation for the removal or prevention of biofilm formationeXrase DNA endonuclease from enGenes is made by a proprietary microbial fermentation process utilizing Escherichia coli cells. This enzyme facilitates the hydrolysis of phosphodiester bonds in various forms of DNA and RNA, including single-stranded, double-stranded, linear, circular, or supercoiled configurations, yielding smaller oligonucleotides typically composed of 2-4 base pairs. Unit-Definition: One unit (U) of the enzyme is defined as the amount required to digest calf thymus DNA, yielding acid-soluble oligonucleotides equivalent to a ΔA260nm of 1.0 within a 30-minute timeframe at pH 8.0 and 37°C. This standardization allows for consistent measurement of enzymatic activity across different batches.

Expression system: Baculovirus<br>Length: 1-415, Full Length<br>Activity: Not Tested

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.

Choline oxidase (EC 1.1.3.17) is an enzyme that catalyzes the following reaction: choline + O2 + H20 ⇌ betaine aldehyde + H2O2One unit of choline oxidase will form 1 μmole of H2O2 by oxidizing choline to betaine aldehyde per min at pH 8.0 and 37 °C. You can remove the build-up of hydrogen peroxide using catalase.

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

D-Alanine aminotransferase (L-glutamic-pyruvic transaminase; EC 2.6.1.21) is an enzyme that catalyzes the following reaction:  D-alanine + α-ketoglutarate ⇌ pyruvate + D-glutamate  Please enquire for more information about D-Alanine Aminotransferase, Bacilus subtilis, Recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page