Enzimas em Proteínas Recombinantes

<p>Glucosyltransferase227-freeze dried is an enzyme-derived product, originating from microbial sources known for its role in catalyzing the transfer of glucose moieties from a donor molecule to specific acceptor molecules. The enzyme operates by facilitating covalent bond formation between glucose and target substrates, displaying specificity that can be exploited in various biochemical pathways.</p>

<p>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.</p>

<p>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.</p>

<p>Glucosyltransferase205-freeze dried is an enzyme preparation that is commonly used in biochemical and molecular biology research. It is derived from microbial sources, often from bacteria or fungi that are known for producing extracellular enzymes. The primary mode of action of Glucosyltransferase205 involves catalyzing the transfer of glucose residues from donor molecules, such as UDP-glucose, to acceptor molecules, forming glycosidic bonds. This enzymatic activity is crucial in the biosynthesis of polysaccharides, which are essential components in various biological structures and processes.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Glucose-6-phosphate dehydrogenase (G6PD, G6PDH; EC 1.1.1.49) is an enzyme that catalises the following reaction:  D-glucose 6-phosphate + NADP+ + H2O ⇌ 6-phospho-D-glucono-1,5-lactone + NADPH + H+  One unit of G6PD will oxidize 1.0 µmole of D-glucose 6-phosphate to 6-phospho-D-glucono-1,5-lactone per min in the presence of NAD+ at pH 7.8 and 30 °C. NADP+ is available here.</p>

<p>LacBuster®-S 50 is a solid and Gamma-irradiated, freeze-dried, broad range beta-lactamase formulation with 50 IU beta-lactamase II and 500 IU beta-lactamase I activity per vial.</p>

<p>Carboxypeptidase B is an enzyme responsible for the cleavage of arginine and lysine from a peptide's C-terminus</p>

<p>Endopeptidase, liquid, food grade is an enzymatic product that functions as a crucial component in the hydrolysis of protein substrates. This enzyme is typically derived from microbial sources, such as bacteria or fungi, and is cultivated under controlled fermentation processes to ensure high purity and activity levels. The primary mode of action of endopeptidases involves the cleavage of peptide bonds within protein molecules, effectively breaking down long protein chains into smaller peptides and amino acids.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>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.</p>

<p>Pancreatin is an enzyme preparation, which is derived from the porcine pancreas. This product contains a mixture of several digestive enzymes, including amylase, lipase, and protease. It is typically obtained through the extraction and purification of these enzymes from the pancreas of pigs, providing a natural and effective source for enzymatic activity.</p>

<p>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</p>

<p>Multi-copper oxidase from the family of polyphenol oxidades. It can be also found in many plants and bacteria. Laccase catalyses the oxidation of phenolic compounds such as lignin. It can oxidase non phenolic groups too with the use of mediators, chemical agents involved in the transfer of the electrons during the reaction. In some cases, laccase can also oxidise halogenated compounds. This enzyme is used for enzymatic assays, lignol screening tests and for waste water treatment to remove biodegrdable pollutants.</p>