Enzima

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.

Bromelain is a group of proteolytic enzymes found in the fruit and stem of pineapple plants. It is used in a topical drug product approved by the FDA to treat severe burns. However, its oral consumption to treat sinusitis, postoperative pain after the extraction of wisdom teeth, and osteoarthritis is still being researched.

Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.

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.

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.

CalB 02 is a lipase enzyme, which is a biocatalyst derived from the yeast Candida antarctica. It functions primarily by catalyzing the hydrolysis of ester bonds. This enzymatic action is due to the unique structure of the active site, which allows for precise substrate specificity and stereoselectivity.

Endoglycosidase H (systematic name glycopeptide-D-mannosyl-N4-(N-acetyl-D-glucosaminyl)2-asparagine 1,4-N-acetyl-β-glucosaminohydrolase, EC 3.2.1.96) is a highly specific enzyme, that cleaves asparagine-linked mannose rich oligosaccharides. One unit of Endoglycosidase H will remove >95% of the carbohydrate from 10μg of denatured RNase B in 1 hour at 37°C in a total reaction volume of 10μl.The product EEH01.7 is available as a large-scale bulk supply of liquid enzyme solution and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.For removal of all N-linked carbohydrates from proteins see Cymit Quimica's PNGase F enzymes (PNG01.3 - vials for research and PNG01.7 - large-scale bulk supply)

Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.

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.

Proteinase K, freeze-dried, recombinant is an enzyme preparation used extensively in molecular biology and biochemistry. It is derived through recombinant DNA technology, producing a highly pure enzyme that is expressed in a non-pathogenic host. Its mode of action involves the non-specific cleavage of peptide bonds in proteins, making it a critical tool for protein digestion.

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.

Lipase CR 02 is a high-purity enzyme preparation, which is derived from the microbial fermentation of selected fungal strains. With a mechanism involving the hydrolysis of ester bonds in lipids, Lipase CR 02 facilitates the conversion of triglycerides into glycerol and free fatty acids. This catalytic activity positions it as an essential tool in various biochemical and industrial applications.

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.

Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP <71>) and EP, LacBusterTM-L is suitable for sterility testing methods such as membrane filtration and direct inoculation.beta lactamase I activity - min. 25.0 IU/mLbeta lactamase II activity - min. 10.0 IU/mL

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.

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.

Carboxypeptidase G (EC 3.4.17.11, alternative name γ-Glutamyl hydrolase) is a protease that cuts γ-glutamyl bonds with high specificity. One unit of Carboxypeptidase G will hydrolyze (+)amethopterin to generate 1.0 μmole of L-glutamic acid.

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.

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.