Enzima

Lipase 13 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°C. 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 13 was shown to hydrolyze p-Nitrophenyl esters of butyrate (87 % activity compared to octanoate), octanoate (100 %), palmitate (44 %), stearate (21 %) and arachidate (2 %).

Catalyst for signal development in immunoassays

Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, PPA; systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyzes hydrolysis of large polysaccharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Porcine pancreatic Alpha Amylase is supplied as lyophilized, off-white to white powder, lyophilized from tris chloride and mannitol, pH 7.2. Activity is ≥70U/mL, specific activity ≥100 U/mg protein. Store at -20°C on arrival.

Please enquire for more information about alpha-Chymotrypsin, freeze-dried, from bovine pancreas including the price, delivery time and more detailed product information at the technical inquiry form on this page

(R)-Mandelonitrile lyase (systematic name mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming), other names are D-oxynitrilase, D-alpha-hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, mandelonitrile benzaldehyde-lyase, ydroxynitrile lyase; EC 4.1.2.10) is the enzyme that catalyzes the following reaction:mandelonitrile ⇌ hydrogen cyanide + benzaldehydeOne unit of (R)-mandelonitrile lyase will convert 1.0 μmol of mandelonitrile per minute under optimal conditions.

Alpha Amylase, powder, is an enzyme preparation that acts as a catalyst for the hydrolysis of starch, breaking it down into simpler sugars like maltose and glucose. This enzyme is derived from microbial or fungal sources, commonly via fermentation processes using strains of bacteria or fungi specifically optimized for enzyme production.

PAIRED PRODUCTS AVAILABLE:

Lipase CR 03 is an industrial-grade enzyme product that is derived from microbial sources, specifically engineered for robust and efficient catalytic activity. The enzyme is extracted utilizing advanced fermentation techniques that capitalize on the prolific nature of specific strains known for lipase production. Its mode of action involves the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. This catalytic process is critical in various biochemical pathways and industrial reactions.

o-Glycosidase (O-Glycanase, endo-a-acetylgalactosaminidase, endo-a-N-acetylgalactosaminidase; EC 3.2.1.97) is an enzyme that specifically removes N-acetylgalactosamine disaccharides, that were attached to serine's or threonine's side-chain oxygen (hence o-Glycosidase). One unit of o-Glycosidase will hydrolyze 1.0 mmole of of substrate per minute at 37 °C and pH 5.0.

Lipase immo Kit 01 is an advanced biochemical tool designed for the immobilization of lipase, an enzyme commonly sourced from microorganisms. This innovative kit utilizes a sophisticated immobilization matrix to enhance enzyme stability and reusability. By binding the enzyme to a solid support, the kit facilitates repeated and continuous use in various reactions without significant loss of activity.

Test sample of Cymit Quimica's Phospholipase D 040 Halal and Kosher Food grade bulk enzyme (EPLD840.6). With one of the most competitive activity rates on the global market and manufactured in Europe, this enzyme is perfect for use in food, diagnostic, therapeutic and nutraceutical industries worldwide.  Phospholipase D is an enzyme that is expressed in almost all types of organisms and whose activity can be harnessed to synthesize critical raw materials, for example phosphatidylserine. Phosphatidylserine has shown itself to be an important functional ingredient in reducing cognitive dysfunction and dementia in the field of nutraceuticals. As a Halal and Kosher food grade enzyme, Cymit Quimica's Phospholipase D is an excellent candidate for a diverse variety of food industry applications. Furthermore our enzyme can be used in diagnostic assays, creating first-class drug delivery systems and APIs. Product is a lyopholised solid

Peroxidase 013 belongs to the class of the heme-family peroxidases and can be utilized for catalyzing oxidation/epoxidation of unsaturated C-C bonds, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase 12 has a temperature optimum in the 20 - 40 °C range and pH optimum between pH 5 and 8.

Xanthine oxidase is an enzyme that catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acid

Creatinine amidohydrolase (also sometimes reffered as creatininase, EC 3.5.2.10) is an enzyme that catalyses the following reaction: creatinine + H2O ⇌ creatine  One unit of creatinine amidohydrolase will produce 1.0 µmole of creatine at pH 7.5 and 37 °C.

Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°C. 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 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).

Urokinase (urokinase-type plasminogen activator, uPA; EC 3.4.21.73) is as serine protease. Its physiological substrate is plasminogen. Urokinase converts plasminogen into an active enzyme, plasmin, which is also a serine protease. In its active form plasmin plays an important role in dissolving blood clots. Despite its name, Urokinase is not a kinase.

Lysozyme, lyophilized powder, min 45000 FIP U/mg, is an enzymatic product derived primarily from egg white. It is a versatile and potent enzyme known for its ability to hydrolyze the β(1-4) glycosidic bonds in the peptidoglycan layer of bacterial cell walls. This mechanism of action is particularly effective against Gram-positive bacteria due to the accessibility of their peptidoglycan layer.

The main protease Mpro is a key protein in the lifecycle of the SARS-CoV-2 virus. Mpro cleaves the viral polyproteins at the C-terminal end of a glutamine residue in recognition sequences containing Leu-Gln-(Ser, Ala, Gly) motifs (Rut et al, 2020).  As SARS-CoV-2 MPro has no closely related homologues in humans, it represents an attractive drug target (Ullrich and Nitsche, 2020). In summary, the Mpro protease is a chymotrypsin-like cysteine protease, requires homodimerisation for proteolytic activity, cleaves the viral polyproteins in 11 distinct sites, exclusively after a glutamine residue. A fluorogenic substrate for Mpro assays is Ac-Abu-Tle-Leu-Gln-AMC.The protein amount or better its concentration in solution is quantified using either A280 (absorption at 280 nm with its specific absorption coefficient) or using the Bradford assay (uses the dye Coomassie Brilliant Blue). Both of these methods quantify the total amount of protein in a sample, no matter what the oligomerization state is.