PRODUCT IN FOCUS
Use of catalase as a supplement in media plates offers a more effective and reliable solution for safe and secure environmental monitoring of sterilization in clean rooms, isolators or production facilities by also removing remaining traces and spots of high concentration of H2O2.
Lipase screening kit (25 enzymes):
A collection of more than 25 unique lipases of microbial origin, carefully selected, and engineered for academic research and applications in the pharmaceutical, cosmetic and fine chemical industry. Our lipases cover a broad range of substrates and are suitable for hydrolysis in aqueous solutions and esterifications in organic solvents. + many more Lipase applications!
Nitrile Hydratase screening kit (10 enzymes):
The enzymes perform highly specific nitrile hydrolysis and show unique properties regarding substrate specificities, reaction conditions and stabilities.
Phospholipase D screening kit (4 enzymes):
Phospholipases D belong to the family of esterases and act naturally on phosphatidyl-choline in the plasma membrane to release phosphatidic acid and choline.
Peroxidase screening kit (2 enzymes):
Peroxidases can be utilized as enzymes catalyzing oxidation reactions like e.g., aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. Peroxidases in this kit belong to the class of the heme-family peroxidases (heme-thiolate, peroxidockerin, DyP-type, hybrid, versatile, tyrosine-ring hydroxylase and chlorite dismutase). Peroxidases can be used in any oxygenation reactions using hydrogen peroxide as a co-substrate with heme as the prosthetic group. The broad range of industrial applications include wastewater treatment (oxidation of chemical effluents from industrials waste), fabric industry (colorizing and decolorizing dyes), food and flavor industry (synthesis of aromatics), cosmetics (perfumes), green plastics industry (dicarboxylic acid synthesis), as well as pharmaceutical applications (API synthesis, e.g., antibiotics synthesis).
These enzymes belong to the family of hydrolases, those acting on carbon-nitrogen bonds other than peptide bonds, specifically in linear or branched amides. The systematic name of this enzyme class is acylamide amidohydrolase. Amidases are used in catalyzing hydrolysis of amides to their corresponding free acids and are therefore widely used tools to obtain the free acids under mild conditions without affecting other functional groups in the substrates. Amidases are used in the synthesis of small molecules in pharma, fine chemistry and cosmetics.
Isoamylase has been isolated from P. amyloderamosa and catalyzes the hydrolysis of O-glycosyl bonds of branches in carbohydrates like glycogen or amylopectin. The hydrolysis of the (1-6)-α-D-glucosidic branch linkages is used industrially to create linear carbohydrates with more defined physical and chemical properties, e.g. for starch debranching.
Carboxypeptidase Y from the yeast S. cerevisiae is an enzyme with a broad specificity unlike other carboxypeptidases and can therefore be applied e.g. for sequence analysis of proteins. Its main function is to remove carboxyterminal residues from polypeptide chains.
Asparaginase has a history as drug for treatment of acute lymphoblastic leukemia (ALL) and in food industry to reduce the formation of acrylamide during food processing, EUCODIS mainly supplies this enzyme for research and diagnostics applications. Asparaginases hydrolyze asparagine to aspartate and ammonia.