Enzimas en Proteínas Recombinantes

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

Proteinase K, high-quality, liquid, recombinant is an advanced enzymatic product, which is a serine protease derived through recombinant DNA technology. It cleaves peptide bonds to facilitate protein digestion with broad substrate specificity. Its robust proteolytic activity is optimal under various conditions, including a wide range of temperatures and pH levels, making it incredibly versatile.

Glucosyltransferase210-freeze dried is an enzyme preparation that catalyzes the transfer of glucose molecules. Derived from specific microorganisms, it facilitates biochemical reactions by adding glucose residues to various substrates, thereby modifying their structure and function. The enzyme functions through the glucosylation process, which is essential in synthesizing different polysaccharides and glycoconjugates.

Carboxypeptidase P (EC 3.4.17.16, also Membrane Pro-Xaa carboxypeptidase, microsomal carboxypeptidase) is a C-terminal exopeptidase, that preferentially cuts at C-terminal amino acid next to proline: ~-Pro-X → ~-Pro + X.

Glucosyltransferase206-freeze dried is an enzymatic preparation designed for specific biochemical applications. It is derived from microbial sources, where it is produced and purified through advanced biotechnological processes. The enzyme functions by catalyzing the transfer of glucosyl units from donor molecules to specific acceptors, thereby forming glycosidic bonds. This mode of action is crucial in various biosynthetic pathways, particularly in the production of polysaccharides and structural carbohydrates.

Lipase 03 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 20-50°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 03 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (90 %), laurate (28 %), palmitate (14 %), stearate (9 %), arachidate (2 %) and behenate (3 %).

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.

Color: beigeForm: lyophilisateProtein content: 0.5 mg/mgThe glucosyltransferase was tested in a glucosylation reaction of a preferred substrate. High conversion after up to 24 h reaction time was observed.

Glucosyltransferase201-freeze dried is an enzymatic preparation that is primarily sourced from bacterial or plant organisms. It functions by catalyzing the transfer of glucose moieties from donor molecules, such as UDP-glucose, to specific acceptor molecules, thus forming glycosidic bonds. This mode of action is crucial in the biosynthesis and modification of polysaccharides and glycoconjugates.

Lipase CalA, wildtype, freeze-dried, recombinant, from Candida antarctica is an enzymatic product, which is a highly purified form of lipase enzyme. It is derived from the yeast species Candida antarctica through recombinant DNA technology, ensuring consistency and purity by expressing the enzyme in a controlled microbial system.

Endonuclease, liquid, food grade is a biochemical enzyme, which is derived from microbial or bovine sources, with precision in hydrolyzing phosphodiester bonds within nucleic acids. This endonuclease cleaves the internal bonds of DNA and RNA, enabling the breakdown of these molecules into smaller nucleotide fragments. Its catalytic action is particularly useful in the controlled degradation of nucleic acids without affecting other macromolecules in the substrate.

Neutral Endopeptidase is an enzymatic product in liquid form, classified as food grade, which is derived from microbial fermentation or animal sources. Its primary mode of action involves the hydrolysis of peptide bonds within proteins, resulting in the breakdown of these macromolecules into smaller peptides and amino acids. This process is facilitated through the enzyme's specificity for neutral pH environments, where it effectively cleaves internal bonds within a protein chain.

Endopeptidase, powder, is a proteolytic enzyme, which is typically derived from microbial, plant, or animal sources, each imparting unique specificities. This enzyme functions by cleaving peptide bonds within polypeptide chains, rather than terminal bonds, thereby facilitating the breakdown of proteins into smaller, more manageable peptide fragments. The mode of action involves recognizing specific amino acid sequences within the substrate, leading to targeted bond hydrolysis.

Beta-lactamase enzymes demonstrate activity against clinically relevant beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. This product may be of particular interest for laboratory teams who require the sterility testing of biological specimens or for environmental monitoring applications.

Luciferase enzyme from Photinus pyralis (firefly), which catalyzes the oxidation of firefly luciferin. This reaction depends on the presence of oxygen and ATP and causes the bioluminescence seen in fireflies

Hyaluronidase (EC 3.2.1.35) is an enzyme that cleaves (1→4)-linkages between N-acetylglucosamine and glucuronate. One unit of hyaluronidase will increase turbidimetric absorbance at A600 by 0.330 at pH 5.7 and 37°C in 2mL reaction volume.

Citrate lyase (also known as ATP citrate synthase, EC 2.3.3.8) is an enzyme that catalyzes the following reaction:citrate + ATP + CoA → oxaloacetate + Acetyl-CoA + ADP + Pi

6-Phosphogluconic dehydrogenase is an enzyme from yeast, which is a key component of the oxidative phase of the pentose phosphate pathway. It catalyzes the oxidative decarboxylation of 6-phosphogluconate to ribulose 5-phosphate, with the concurrent reduction of NADP+ to NADPH. This enzyme is sourced from yeast, a model organism extensively used in biochemical studies due to its eukaryotic nature and ease of genetic manipulation.