Enzima

Leucine aminopeptidase (L-leucine aminopeptidase, Leucyl aminopeptidase, leucyl peptidase, peptidase S; EC 3.4.11.1) is an exopeptidase enzyme. It preferentially catalyses the removal of N-terminal leucine residues from proteins and peptides.

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.

<p>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.</p>

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.

<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>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>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>

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.

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)

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.

<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>

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.

<p>Ready to use beta-lactamase solution targeting beta-lactam antibiotics such as penicillins, carbapenems and cephalosporins. According to US Pharmacopeia (USP &lt;71&gt;) 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</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.

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.

<p>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.</p>

<p>Lipase 31 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 40-80°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 31 was shown to hydrolyze p-Nitrophenyl esters of acetate (100 % activity) and butyrate (23 %).</p>

<p>Ultra nuclease (EC 3.1.30.2) is an enzyme that digests DNA and RNA in any form: single- and double-stranded, linear, circular and supercoiled. The ultimate reaction product is 5'-monophosphate oligonucleatides that are mostly three, four and five bases long. Please enquire for more information about Ultra nuclease, liquid, recombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Lipase Y 01 is an enzymatic catalyst, which is derived from microbial fermentation with a specific mode of action involving the hydrolysis of triglycerides into glycerol and free fatty acids. This enzyme operates by breaking ester bonds in fats, facilitating their breakdown and conversion into simpler molecules.</p>

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

CalB 01 is an industrial biocatalyst that is derived from microbial sources, specifically engineered through recombinant DNA technology. Its primary component is the lipase enzyme from the yeast Candida antarctica, which has been optimized for high performance in various biotransformations. This enzyme functions by catalyzing the hydrolysis and synthesis of esters, facilitating transesterification and resolution of chiral molecules. The mode of action involves the selective cleavage of ester bonds in aqueous and non-aqueous media, which is crucial for modifying substrates in complex chemical reactions.

CalB 10 is an industrial enzyme, specifically a lipase, which is derived from microbial sources, most commonly expressing the lipase B from Candida antarctica. It operates through the hydrolysis of ester bonds in lipids, enabling the conversion of triglycerides into glycerol and free fatty acids. This catalytic action is facilitated via its active site, where the nucleophilic serine residue attacks the carbonyl carbon of the substrate, forming a tetrahedral intermediate that eventually results in bond cleavage and product release.

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.

Tyrosinase (EC 1.14.18.1) is an enzyme that oxydises phenol derivatives (e.g. tyrosine, dopamine). One unit of tyrosinase dissolved in 3mL reaction mixture will cause the absorbance at 280nm to increase by 0.001 in the presence of L-tyrosine at pH 6.5 and 25 °C. L-tyrosine is available here.Lyophilized, from mushroom. Activity ≥1000 unit/mg

<p>Lipase 65 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30-40°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 65 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (87 %), laurate (5 %), palmitate (0.2 %) and stearate (0.1 %).</p>

Sialic acid aldolase - Aqueous solution is an enzyme preparation used extensively in biochemical and biotechnological applications. It is derived from microbial sources, where it is expressed and purified to high levels for research purposes. Sialic acid aldolase acts by catalyzing the reversible aldol reaction between N-acetylneuraminic acid (sialic acid) and pyruvate, facilitating the cleavage or synthesis of sialic acid.

<p>LacBuster® Settle Plates contain a general purpose growth medium (tryptone soya agar) supplemented with LacBuster®, a high-performing beta-lactamase to effectively neutralize beta-lactam antibiotics. The media plates are suitable for the cultivation of a wide variety of microorganisms in environmental monitoring within the pharmaceutical industry.</p>

<p>Lipoxidase, from soybean</p>

BspQI is a Type IIS restriction endonuclease which only cleave one strand when binding to a DNA sequence.

<p>Beta-lactamase enzyme targeting beta-lactam antibiotics</p>

Peroxidases can be utilized as enzymes catalyzing e.g. aromatic ring hydroxylation, epoxidation, halogenation, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions.

<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>Triose-phosphate isomerase (TPI, TIM; EC 5.3.1.1) is an enzyme that catalyzes the reversible isomerization of dihydroxyacetone phosphate and D-glyceraldehyde 3-phosphate:  DHAP ⇌ GADP  The reaction mechanism involves the formation of an enediol intermediate. One unit of Triose-phosphate isomerase will convert 1.0 μmole glyceraldehyde 3-phosphate to dihydroxyacetone phosphate per min at pH 7.6 and 25 °C. Please enquire for more information about Triosephosphate Isomerase, freeze-dried, from rabbit Muscle including the price, delivery time and more detailed product information at the technical inquiry form on this page</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

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>Pectin is an enzyme that breaks down pectin, a complex polysaccharide found in plant cell walls. It widely used in food and beverage, wine and brewing and textile and paper industries</p>

<p>Lipase 37 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8-9 and temp. optimum at &lt;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 37 was shown to hydrolyze p-Nitrophenyl esters of butyrate (48 % activity), octanoate (100 %), laurate (85 %), palmitate (5 %) and stearate (1 %).</p>

Lipase CR 01 is an enzymatic product, which is derived from microbial sources, specifically selected strains of microorganisms. It exhibits a highly efficient mode of action by catalyzing the hydrolysis of triglycerides into glycerol and free fatty acids. This reaction is facilitated by its ability to target the ester bonds within lipid molecules, improving lipid solubilization and breakdown.

<p>As a member of the family of hydrolases this enzyme acts on carbon-nitrogen bonds and may be used in the commercial production of semisynthetic penicillin.</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>Hydrolytic enzyme; biocatalyst in production of beta-lactam antibiotics</p>

Creatine kinase (also known phosphocreatine kinase or creatine phosphokinase, EC 2.7.3.2) in an enzyme that catalyzes the following reaction:creatine + ATP ⇌ phosphocreatine + ADPOne unit of creatine kinase will transfer 1.0 μmole of phosphate from phosphocreatine to ADP per min at pH 7.4 and 30 °C.

<p>Trypsin (EC 3.4.21.4) is a protease that hydrolyses proteins by cleaving the peptide bond at the carboxyl side of the positively charged amino acid (Lysine or Arginine). Trypsin belongs to a family of serine proteases, as it has a serine in its active site.</p>