Enzyme

<p>Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.</p>

<p>Fructose-6-phosphate kinase (Phosphofructokinase, PFK, EC 2.7.1.11) is an enzyme that catalyzes the following reaction:  F6P + ATP ⇌ F1,6BP + ATP  One unit of PFK will convert 1.0 μmole of fructose 6-phosphate and ATP to fructose 1,6-diphosphate and ADP per minute at pH 9.0 at 30 °C.</p>

<p>Lipase 64 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 40-50°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 64 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (0.5 %) and laurate (0.1 %).</p>

<p>Endoglycosidase H (Endo H) is a highly specific enzyme that cleaves N-linked oligosaccharides from glycoproteins, targeting high-mannose and certain hybrid-type N-glycans. It does not act on complex-type N-glycans, which are typically processed further in the Golgi apparatus. Due to its specificity, Endo H is widely used in research to study intracellular protein trafficking and post-translational modifications, particularly those occurring during glycoprotein maturation.This product is available as vials for research applications with pre-defined quantities (&gt;250 kU/vial) of liquid enzyme solutionSee our EndoH (EEH01.7) available for large-scale bulk supply of liquid enzyme solution for the deglycosylation of proteins in manufacture.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)</p>

<p>Xylanase (Endo-1,4-β-xylanase, 1,4-β-D-Xylanxylanohydrolase, systematic name 4-β-D-xylan xylanohydrolase; EC 3.2.1.8) is an enzyme that digests polysaccharide xylan by hydrolyzing (1→4)-β-D-xylosidic linkages. One unit of Xylanase will hydrolyze 1.0 μmole of chromogenic substrate mimic per minute (available here) under optimal reaction conditions.</p>

<p>PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application.<br>PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as vials for research applications with pre-defined quantities (&gt;250 kU/vial) of liquid enzyme solution . See our large-scale bulk supply of PNGase F for the deglycosylation of proteins in manufacture.Also available is our endoH enzymes (EEH01.3 - vials for research and EEH01.7 - large scale bulk supply).</p>

<p>Heat Labile Uracil-DNA Glycosylase, 500 units, is an enzyme designed for molecular biology applications, primarily derived from a recombinant bacterial source. This enzyme effectively removes uracil from DNA molecules at temperatures that preserve the integrity of the DNA. With its heat-labile properties, the enzyme can be inactivated at moderately elevated temperatures, making it ideal for processes that require precise control over enzyme activity.</p>

<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>

<p>PNGase F is an endoglycosidase that can remove all N-linked carbohydrates from proteins, which is useful if you are uncertain whether the carbohydrate is N-linked or O-linked to the protein or is a high mannose type. It is also the enzyme of choice when you need to study or use the naked protein in your application.<br>PNGase functions as a glycoamidase and hydrolyzes the amide bond between the innermost GlcNac of mammalian asparagine-linked mannose oligosaccharides, whether they are high, complex or hybrid. Specifically, the glycan is removed from the asparagine residue which through the deamination reactions becomes aspartic acid.This enzyme is available as a large-scale bulk supply of liquid enzyme solution. See our PNGase F available as vials for research applications with pre-defined quantities (&gt;250 kU/vial) of liquid enzyme solution.Also available is our endoH enzymes (EEH01.3 - research quantities and EEH01.7 - large scale bulk supply).</p>

<p>Cellulase, powder is an enzymatic product derived from microbial fermentation, specifically sourced from fungi or bacteria known for their cellulolytic activity. Cellulase acts by catalyzing the hydrolysis of cellulose, breaking it down into smaller polysaccharides and glucose. This decomposition occurs through synergistic action by three main components: endoglucanases, exoglucanases, and β-glucosidases, each targeting specific bonds in the cellulose structure, resulting in its complete breakdown.</p>

<p>Xylanase is an enzymatic product, which is typically derived from microbial sources such as fungi or bacteria. Its primary function involves catalyzing the hydrolysis of xylan, a major hemicellulose component found in plant cell walls. Through breaking down xylan into xylose and other oligosaccharides, xylanase significantly modifies plant material structure.</p>

<p>Lipase 17 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8. 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 17 was shown to hydrolyze p-Nitrophenyl esters of butyrate (2 % activity compared to octanoate), octanoate (100 %), laurate (20 %), palmitate (3 %), stearate (1 %), arachidate (1 %) and behenate (1 %).</p>

<p>Protein kinase LATS2 is a serine/threonine kinase, which is a crucial component sourced intrinsically from cellular kinase cascades involved in cell regulation. This protein kinase is pivotal in the Hippo signaling pathway, which regulates cell growth, apoptosis, and stem cell renewal. LATS2 is part of the core kinase cascade that, upon activation, phosphorylates and inhibits the activity of the transcriptional co-activators YAP and TAZ, thereby controlling their transcriptional activity. This inhibition is key to maintaining proper cell proliferation and preventing uncontrolled cell growth that could lead to tumorigenesis.</p>

<p>Lipase 09 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 35-55°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 09 was shown to hydrolyze p-Nitrophenyl esters of acetate (18 % activity compared to octanoate), butyrate (80 %), octanoate (100 %) and capate (40 %).</p>

<p>A proprietary potent and stable alternative to chemical neutralizers such as pyruvate - for the utilization in environmental monitoring applications. 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. Currently, agar plates for monitoring disinfection or sterilization are supplemented with pyruvate, which is consumed during the neutralization of hydrogen peroxide. One of the main benefits of this catalase is its high stability in agar media at 50°C, which allows easy preparation of media and processing into plates. Due to the high stability no special storage conditions are needed and a shelf-life of &gt; 6 months at 4-25°C can be guaranteed.<br>Key features are:</p>

<p>Hexokinase (EC 2.7.1.1) in an enzyme that catalyses the following reaction:  Glucose + ATP → Glucose-6-phosphate + ADP  One unit of hexokinase will phosphorylate 1.0 µmole of glucose per min at pH 7.6 and 25 °C in the presence of ATP.  The product is a lyophilized powder, ≥30 units/mg protein.</p>

<p>Elastase (EC 3.4. 21.36) is a serine protease that breaks down elastin fibers. One unit of Elastase release 1 nmol of p-nitrophenol per sec from BOC-L-alanine p-nitrophenyl ester at pH 6.5 and 37°C</p>

<p>Cymit Quimica’s econoLuciferase™ (econoLuc Cymit Quimica Cat. No. L-8090) is a recombinant luciferase from the firefly Luciola lateralis that has been expressed as a luciferase-GFP fusion protein in E. coli.The luciferase enzyme has been optimized for increased thermo-stability by genetic modification to be stable for one hour at 37°C and up to two days at room temperature.Stabilized econoLuciferase™ thus overcomes the disadvantages and limitations of wild-type Luciferase, notably its short active life, outperforming enzyme from the Photinus pyralis firefly for both performance and stability.This optimized luciferase is the perfect enzyme for ATP detection assays in hygiene control, microbial tests using caged luciferins and it is the luciferase of choice for biochemical tests measuring ATP consumption and production in diverse enzymatic reactions.The product L-8090 is available on a large scale and is intended for use in the chemical, diagnostic, pharmaceutical and related industries.</p>

<p>Supplied as lyophilisate containing 1% w/w X-Shining™ Luciferase. The improved, thermostable X-Shining™ Luciferase is suitable for any luciferin-luciferase-based assay using D-luciferin (dLuc) or synthetic pro-luciferins (caged luciferins). Examples of its typical applications include ATP tests in hygiene monitoring, ATP tests in drug screenings and bacteria identification in microbial assays. The termostable luciferase X-Shining™ has been optimised by genetic engineering for strongly increased thermostability and storage stability. In temperature stress tests, the enzyme survives temperatures of 60°C for over an hour, whereas a wild type luciferase from firefly is inactivated after only a few minutes. The extraordinary stability makes it user-friendly and eliminates some of the main disadvantages and limitations of the commonly used wild type luciferase. X-Shining™ Luciferase is supplied as a lyophilisate (1% w/w X-Shining™ Luciferase) or as aqueous solution with glycerol (BX174908), and it may be stored for months at room temperature without significant loss of function. Find out more about our innovative X-Shining range here X-Shining | Innovation | Cymit Quimica Carbosynth.</p>

<p>Penase (Penicillinase) is an enzyme, which is a type of β-lactamase sourced from various bacterial strains capable of deactivating penicillin. It accomplishes this by targeting the β-lactam ring, a crucial structural component of penicillin antibiotics, and hydrolyzing it, thereby neutralizing the antibiotic effect. This enzymatic action is a defense mechanism employed by certain bacteria to survive in environments saturated with penicillin-based antibiotics.</p>

<p>α-Glucosidase (EC 3.2.1.20) is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues to produce α-D-glucose. This enzyme has been isolated from Bacillus stearothermophilus and is used as an industrial catalyst in the production of glucose syrups.  One Unit of α-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic 4-nitrophenyl α-D-glucopyranoside per minute under optimum conditions.</p>

<p>Adenosine deaminase catalyzes deamination of adenosine, converting it to inosine. It happens by the substituting of the amino group by a keto group. One Unit of the enzyme converts one micromole of adenosine to inosine per minute at 25°C, pH 7.4. Adenosine deaminase is also known by names of adenosine aminohydrolase, and ADA, EC 3.5.4.4.</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>

<p>Lipase 20 recombinantly expressed in P. pastoris comes in a spray-dried formulation. It has its pH optimum at 7-8. 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 20 was shown to hydrolyze p-Nitrophenyl esters of butyrate (3 % activity compared to octanoate), octanoate (100 %), laurate (85 %), palmitate (52 %), stearate (29 %), arachidate (22 %) and behenate (8 %).</p>

<p>Elastase is a proteolytic enzyme that breaks down elastin</p>

<p>CS2 hydrolase (Carbon disulfide hydrolase; E.C. 3.13.1.5) is an enzyme that catalyzes the following reaction:  CS2 + 2 H2O → CO2 + 2 H2S  thus converting carbon disulfide into hydrogen sulfide and carbon dioxide.</p>

<p>Immobilized lipase is an advanced enzymatic product, which is derived from lipases, enzymes primarily sourced from microbial, plant, or animal origins. This product operates through a catalytic mechanism where the lipase is attached to a solid support, enhancing its stability and reusability in various reactions. This immobilization allows the enzyme to maintain activity over a wide range of conditions, including different pH levels and temperatures.</p>

<p>3-Oxo-5β-steroid Δ4-dehydrogenase is an enzyme crucial in the metabolic pathway of steroid hormones, facilitating the conversion of androgens and estrogens. It is predominantly found in the liver, but also in other tissues where steroid biosynthesis occurs. This enzyme catalyzes the dehydrogenation at the Δ4 position of 3-oxo-5β-steroids, playing a significant role in the modulation and regulation of steroid hormone levels within cells.</p>

<p>L-Leucine dehydrogenase (Leucine dehydrogenase, systematic name L-leucine:NAD+ oxidoreductase (deaminating); EC 1.4.1.9) is an enzyme that catalyzes the following reaction:  L-leucine + H2O + NAD+ ⇌ 4-methyl-2-oxopentanoate + NH3 + NADH + H+  One unit of L-Leucine dehydrogenase will convert 1.0 µmole of L‑leucine into 4-methyl-2-oxopentanoate per min at pH 10.5 and 37 °C in the presence of NAD+. The enzyme requires NAD+ as a cofactor, it is available here.</p>

<p>Lipase 08 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 20-60°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 08 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (60 %), laurate (7 %), palmitate (0.5 %), stearate (0.2 %), arachidate (0.1 %) and behenate (0.1 %).</p>

<p>Entorokinase (also known as enteropeptidase; EC 3.4.21.9) is a proteolytic enzyme (proteinase) that activates trypsinogen into its active form, trypsin. One unit of  Entorokinase will produce 1.0 nmole of trypsin from trypsinogen per min at pH 5.6 and 25 °C.</p>

<p>DNA ligase (ATP) is an enzyme (EC 6.5.1.1) that ligates DNA strands, repairing nicks in double-standed DNA and coupling blunt-ended or cohesive DNA fragments. It requires 3′ hydroxyl and 5′ phosphate nucleoside ends for ligation and ATP as a cofactor.</p>

<p>LacBuster™-S 5000 is an enzymatic product, specifically a beta-lactamase, which originates from microbial sources known for their ability to produce enzymes that break down antibiotics. This product functions by hydrolyzing the beta-lactam ring of relevant antibiotics, thereby neutralizing their antibacterial activity.</p>

<p>LacBuster™-S 2000 is an enzyme preparation, specifically a beta-lactamase, which is derived from bacterial sources known for their capacity to degrade beta-lactam antibiotics. Through hydrolytic cleavage of the beta-lactam ring, this enzyme neutralizes the efficacy of beta-lactam antibiotics, thereby rendering them inactive.</p>

<p>LacBuster™-S 1000 is an enzymatic product derived from microbial sources, specifically engineered for precision and efficiency. It is a beta-lactamase, which catalyzes the hydrolysis of the beta-lactam ring found in beta-lactam antibiotics such as penicillins and cephalosporins, rendering them inactive. The enzyme achieves this by breaking the amide bond within the beta-lactam ring, a critical structural component necessary for antibiotic activity.</p>

<p>LacBuster™-S 50 is a beta-lactamase formulation, which is an enzyme of microbial origin with the ability to hydrolyze beta-lactam antibiotics. This enzymatic product is derived from specific bacterial species known for their resistance mechanisms, providing a robust capability to deactivate compounds such as penicillins and cephalosporins. Its mode of action involves the cleavage of the beta-lactam ring, a crucial structural component of these antibiotics, effectively neutralizing their antibacterial properties.</p>

<p>Creatinine deiminase (EC 3.5.4.21) in an enzyme that catalyzes the following reaction:  Creatinine + H2O → N-Methylhydantoin + NH3  One unit of creatinine deiminase will hydrolyze 1.0 µmole of creatinine to N-methylhydantoin and ammonia per minute at pH 7.5 and 37°C.</p>

<p>DNA polymerase is an essential enzymatic protein, derived from various organisms including bacteria, archaea, and eukaryotes, which plays a pivotal role in the replication and repair of DNA. This enzyme functions by adding nucleotides to the growing DNA strand in a template-dependent manner, ensuring the accurate duplication of the genetic material. It operates through a polymerization mechanism, where nucleotides are selected and incorporated complementary to the template strand, facilitating the elongation of the new DNA strand in the 5' to 3' direction.</p>

<p>Please enquire for more information about Horseradish Peroxidase 01, rekombinant including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.</p>

<p>Lipase 12 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7.5 and temp. optimum at &gt;60°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 12 was shown to hydrolyze p-Nitrophenyl esters of butyrate (60 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (30 %), stearate (14 %), arachidate (0.2 %) and behenate (0.2 %).</p>

<p>Ribonuclease H from Escherichia Coli is the enzyme that breaks down RNA strand in RNA-DNA duplexes. It acts by cleaving the phosphodiester bonds of RNA and produces 3' hydroxyl and a 5' phosphate groups at the cleavage site. A common use of Ribonuclease H is to remove RNA template after reverse transcription reaction.</p>

<p>Lipase 67 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7-8 and temp. optimum at 30°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 67 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (37 %), laurate (3 %) and palmitate (0.2 %).</p>

<p>Lipase 13 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°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 13 was shown to hydrolyze p-Nitrophenyl esters of butyrate (87 % activity compared to octanoate), octanoate (100 %), palmitate (44 %), stearate (21 %) and arachidate (2 %).</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. The lipase from the yeast Y. lipolytica has a temperature optimum in the 30 - 40 °C range and pH optimum between pH 7 and 8.</p>

<p>Catalyst for signal development in immunoassays</p>

<p>Alpha-L-iduronidase is a glycoside hydrolase enzyme that cleaves the non-reducing, terminal alpha-L-iduronic acid residues from polysaccharides and oligosaccharides. Alpha-L-iduronidase is involved in the lysosomal degradation of glycosaminoglycans and its deficiency leads to the accumulation of dermatan sulphate and heparan sulphate in tissues, a condition known as mucopolysaccharidosis I (MPS I). Alpha-L-iduronidase activity can be detected and quantified in an assay using a fluorogenic substrate 4MU-alpha-L-idopyranosiduronic acid. Alpha-L-iduronidase is also used in a 2-step assay for Hunter syndrome (MPS II) testing in combination with 4-MU-alpha-L-idopyranosiduronic acid 2-sulphate.<br>This enzyme is supplied as a 2 mg/mL aqueous solution in 25 mM sodium acetate, 150 mM NaCl, 50% glycerol, pH 5.0 from a bacterial source, recombinantly expressed in Escherichia coli (see application notes for more details). Alpha-L-iduronidase is also available as lyophilisate (FA181881)</p>

<p>(R)-Mandelonitrile lyase (systematic name mandelonitrile benzaldehyde-lyase (hydrogen cyanide-forming), other names are D-oxynitrilase, D-alpha-hydroxynitrile lyase, (R)-oxynitrilase, oxynitrilase, mandelonitrile benzaldehyde-lyase, ydroxynitrile lyase; EC 4.1.2.10) is the enzyme that catalyzes the following reaction:mandelonitrile ⇌ hydrogen cyanide + benzaldehydeOne unit of (R)-mandelonitrile lyase will convert 1.0 μmol of mandelonitrile per minute under optimal conditions.</p>

<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>

<p>OXA-11 (β-Lactamase) is an enzyme of the β-lactamase class, which is primarily derived from Gram-negative bacteria. This enzyme is characterized by its ability to hydrolyze β-lactam antibiotics, rendering them ineffective by breaking the β-lactam ring, a crucial component of these antibiotics. OXA-11 is a notable member of the oxacillinase group within class D β-lactamases, known for its resistance to penicillins and cephalosporins.</p>

<p>NMCA (β-Lactamase) is an enzyme, specifically acclaimed for its role in conferring antibiotic resistance. It is derived from bacterial sources, where it naturally occurs as part of the bacterial defense mechanism against β-lactam antibiotics. NMCA (β-Lactamase) functions by hydrolyzing the β-lactam ring present in these antibiotics, effectively rendering them inactive. This mode of action disrupts the antibiotic's ability to inhibit cell wall synthesis within bacteria, thereby permitting bacterial survival and proliferation.</p>

<p>Collagenase is an enzymes that is responsible for breaking peptide bonds in collagen</p>

<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. Trypsin can be inhibited by using trypsin inhibitor Alpha 1 Antitrypsin.</p>

<p>A proteolytic enzyme synthesized by the HIV cell as part of the GagPol polyprotein</p>

<p>SPM-1 (β-Lactamase) is an enzyme, which is a type of metallo-beta-lactamase enzyme, derived from bacterial origins, specifically from pathogens associated with nosocomial infections. This enzyme acts by hydrolyzing the amide bond in the beta-lactam ring of antibiotics, rendering β-lactam antibiotics ineffective. SPM-1 participates in antibiotic resistance by facilitating the degradation of a wide range of β-lactam antibiotics, including penicillins and cephalosporins, thereby nullifying their therapeutic effects.</p>

<p>KPC-1 (β-Lactamase) is an enzyme that breaks down β-lactam antibiotics, rendering them ineffective. It originates from strains of bacteria, particularly Klebsiella pneumoniae, which are significant sources of hospital-acquired infections. The mode of action involves hydrolyzing the β-lactam ring found in antibiotics such as penicillins and cephalosporins, neutralizing their antibacterial effects.</p>

<p>VIM-15 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from bacterial sources, particularly Gram-negative bacteria. Its mode of action involves the hydrolysis of β-lactam antibiotics, facilitating bacterial resistance. This enzyme employs zinc ions as cofactors to break the β-lactam ring, rendering these antibiotics ineffective against the bacteria that produce the enzyme. The hydrolysis process disrupts the antibiotic's structural integrity, crucial for its antibacterial activity, thereby nullifying its therapeutic effects.</p>

<p>NMCA (β-Lactamase) is an enzyme that hydrolyzes β-lactam antibiotics, a type of product crucial for studies in antibiotic resistance mechanisms. This enzyme is derived from bacterial sources, specifically those strains known for their role in beta-lactam drug resistance. The mode of action of β-Lactamase involves the enzymatic breakdown of the β-lactam ring found in penicillins and cephalosporins, thereby neutralizing the antibiotic's efficacy. This catalytic process is an essential focus for researchers studying bacterial defense mechanisms and the development of resistant strains.</p>

<p>OXA-11 is a β-lactamase enzyme, which is a type of protein produced by certain bacteria. These enzymes are derived from the bacterial source and are responsible for antibiotic resistance. The primary mode of action of OXA-11 is the hydrolysis of the β-lactam ring found in various antibiotics, such as penicillins and cephalosporins, rendering them ineffective. This enzymatic activity allows bacteria to survive exposure to these antimicrobial agents, posing a significant challenge in clinical settings.</p>

<p>Penase is an enzyme, specifically a type of beta-lactamase, which is derived from bacterial sources. Its mode of action involves the hydrolysis of the beta-lactam ring present in penicillin molecules. This enzymatic activity renders penicillin inactive by breaking its critical structural component that is essential for its antibacterial activity.</p>

<p>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.</p>

<p>β-Glucuronidase (EC 3.2.1.31) is an enzyme that hydrolyzes glucuronides. It can also be used to cleave benzodiazepine and steroid conjugates. One unit of β-Glucuronidase will hydrolyze a chromogenic substrate mimic 4-nitrophenyl-β-D-glucuronide to produce 1.0 μmole of 4-nitrophenol per minute at pH 5.0 and 37 °C.</p>

<p>The main protease Mpro is a key protein in the lifecycle of the SARS-CoV-2 virus. Mpro cleaves the viral polyproteins at the C-terminal end of a glutamine residue in recognition sequences containing Leu-Gln-(Ser, Ala, Gly) motifs (Rut et al, 2020).  As SARS-CoV-2 MPro has no closely related homologues in humans, it represents an attractive drug target (Ullrich and Nitsche, 2020). In summary, the Mpro protease is a chymotrypsin-like cysteine protease, requires homodimerisation for proteolytic activity, cleaves the viral polyproteins in 11 distinct sites, exclusively after a glutamine residue. A fluorogenic substrate for Mpro assays is Ac-Abu-Tle-Leu-Gln-AMC.The protein amount or better its concentration in solution is quantified using either A280 (absorption at 280 nm with its specific absorption coefficient) or using the Bradford assay (uses the dye Coomassie Brilliant Blue). Both of these methods quantify the total amount of protein in a sample, no matter what the oligomerization state is.</p>

<p>PAIRED PRODUCTS AVAILABLE:</p>

<p>Alpha Amylase, powder, is an enzyme preparation that acts as a catalyst for the hydrolysis of starch, breaking it down into simpler sugars like maltose and glucose. This enzyme is derived from microbial or fungal sources, commonly via fermentation processes using strains of bacteria or fungi specifically optimized for enzyme production.</p>

<p>Lipase 04 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-7 and temp. optimum at 60-70°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 04 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (68 %), laurate (2 %), palmitate (2 %), stearate (2 %), arachidate (2 %) and behenate (2 %).</p>

<p>Lipase CR 03 is an industrial-grade enzyme product that is derived from microbial sources, specifically engineered for robust and efficient catalytic activity. The enzyme is extracted utilizing advanced fermentation techniques that capitalize on the prolific nature of specific strains known for lipase production. Its mode of action involves the hydrolysis of ester bonds in triglycerides, converting them into free fatty acids and glycerol. This catalytic process is critical in various biochemical pathways and industrial reactions.</p>

<p>ApStar Taq DNA Polymerase is a thermostable DNA polymerase, originally derived from the thermophilic bacterium Thermus aquaticus. It operates by synthesizing new strands of DNA through the extension of primers in the 5' to 3' direction, utilizing a DNA template. This enzyme is specifically engineered to withstand high temperatures, making it ideal for the denaturation phases of PCR.</p>

<p>Alpha Amylase (Amylase, α-Amylase, 1,4-α-D-glucan glucanohydrolase, glycogenase, PPA; systematic name 4-α-D-glucan glucanohydrolase; EC 3.2.1.1, CAS Number [9000-90-2]) is an enzyme that catalyzes hydrolysis of large polysaccharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. One unit of Alpha Amylase will catalyze the hydrolysis of 1.0 μmol of 2-chloro-4-nitrophenyl-α-D-maltotrioside to yield 2-chloro-4-nitrophenol per minute at 37°C. Porcine pancreatic Alpha Amylase is supplied as lyophilized, off-white to white powder, lyophilized from tris chloride and mannitol, pH 7.2. Activity is ≥70U/mL, specific activity ≥100 U/mg protein. Store at -20°C on arrival.</p>

<p>Lipase immo Kit 01 is an advanced biochemical tool designed for the immobilization of lipase, an enzyme commonly sourced from microorganisms. This innovative kit utilizes a sophisticated immobilization matrix to enhance enzyme stability and reusability. By binding the enzyme to a solid support, the kit facilitates repeated and continuous use in various reactions without significant loss of activity.</p>

<p>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</p>

<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>Peroxidase 013 belongs to the class of the heme-family peroxidases and can be utilized for catalyzing oxidation/epoxidation of unsaturated C-C bonds, N- or S-oxidation, ether cleavage and alcohol/aldehyde oxidation reactions. The Peroxidase 12 has a temperature optimum in the 20 - 40 °C range and pH optimum between pH 5 and 8.</p>

<p>Xanthine oxidase is an enzyme that catalyzes the hydroxylation of hypoxanthine to xanthine and xanthine to uric acid</p>

<p>Sialic acid aldolase - crystalline is a purified enzyme product, which is typically derived from microbial sources, such as certain bacteria, that have evolved to metabolize sialic acids. This enzyme catalyzes a reversible aldol reaction between sialic acid and pyruvate, facilitating the cleavage or formation of sialic acid from N-acetylmannosamine and pyruvate. By breaking the carbon-carbon bond in sialic acid, sialic acid aldolase plays a critical role in the degradation and biosynthesis pathways of sialic acid, which are key factors in numerous biological processes.</p>

<p>Creatinine amidohydrolase (also sometimes reffered as creatininase, EC 3.5.2.10) is an enzyme that catalyses the following reaction: creatinine + H2O ⇌ creatine  One unit of creatinine amidohydrolase will produce 1.0 µmole of creatine at pH 7.5 and 37 °C.</p>

<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>

<p>Lipase 56 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 8 and temp. optimum at 40-50°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 56 was shown to hydrolyze p-Nitrophenyl esters of butyrate (79 % activity compared to octanoate), octanoate (100 %), laurate (51 %), palmitate (29 %), stearate (15 %), arachidate (0.2 %) and behenate (0.1 %).</p>

<p>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>

<p>β-Glucosidase (β-D-glucosidase, systematic name β-D-glucoside glucohydrolase; EC 3.2.1.21) is an enzyme that catalyzes the release the terminal glucose monomers from cellulose and the other oligo- and poly saccharides with β-1,4-linked glucosyl residues. One Unit of β-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic p-nitrophenyl β-glucoside per minute under optimum conditions.</p>

<p>Glucosyltransferases (GTases) can be utilized as enzymes to transfer glucose to another organic molecule (aglycon) establishing glycosidic linkages. UDP-glucose dependent GTases are part of the enzyme family of glycosyltransferases, they are versatile tools in glucosylation reactions. Our kit contains 8 lyophilized enzymes, which cover a wide range of different aglycons for the synthesis of glucosides: aliphatic, terpene, aromatic and heterocyclic glucosides.Overall the process of glycosylation is highly beneficial to both the pharma and cosmetic industries. Particularly the ability of GTases to transfer glucose to organic molecules (aglycon), is a sought-after activity for water-soluble formulations in the cosmetic industry. This is because the addition of a sugar moiety can result in a more hydrophilic product. Not only this but glucosyltransferase can be utilized to synthesize aliphatic, terpene, aromatic and heterocyclic glucosides, used in flavour or fragrance applications. In the pharma industry, glycosylating active pharmaceutical ingredients can improve the solubility of active ingredients, allowing the possibility for patient to take medication in a liquid form. This would be more accessible to those patients who find taking tablets difficult.Contact our enzyme experts for custom glucoside synthesis services, based on our full library of glycosyltransferases.</p>

<p>Isoamylase (also known as debranching enzyme, systemic name glycogen α-1,6-glucanohydrolase; EC 3.2.1.68) is an enzyme from the family of carbohydrolases acting specifically on α-1,6-glucosidic branch linkages in polysaccharides such as amylopectin or glycogen, but rarely hydrolyzes such bonds in pullulan. Isoamylase has been obtained from P. amyloderamosa and has a temperature optimum in the 30 – 40 °C range and pH optimum between pH 3 and 4.</p>

<p>Lipase 06 recombinantly expressed in E. coli comes in a freeze-dried formulation. It has its pH optimum at 7 and temp. optimum at 30-45°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 06 was shown to hydrolyze p-Nitrophenyl esters of butyrate (91 % activity compared to octanoate), octanoate (100 %), laurate (13 %), palmitate (1 %), stearate (2 %), arachidate (0.3 %) and behenate (1 %).</p>

<p>KPC-1 (β-Lactamase) is a specialized enzyme, which is produced by certain Gram-negative bacteria, notably Klebsiella pneumoniae. It functions by hydrolyzing the β-lactam ring found in a wide range of β-lactam antibiotics, such as penicillins and cephalosporins. This enzymatic action effectively neutralizes the antibiotic's antimicrobial properties, rendering the drugs ineffective against bacteria that produce KPC-1.</p>

<p>SPM-1 (β-Lactamase) is a metallo-β-lactamase enzyme, which is derived from certain Gram-negative bacteria, such as Pseudomonas aeruginosa. This enzyme is characterized by its ability to hydrolyze a broad spectrum of β-lactam antibiotics, including penicillins, cephalosporins, and carbapenems, due to the presence of a zinc ion in its active site. The zinc ion plays a crucial role in the catalytic mechanism by facilitating the cleavage of the β-lactam ring, rendering the antibiotic ineffective against bacterial cell wall synthesis.</p>

<p>beta lactamase I activity - min. 600.0 IU/mg</p>

<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>

<p>VIM-15 (β-Lactamase) is an enzyme product, specifically a metallo-beta-lactamase, which is sourced from certain resistant bacterial strains. This enzyme functions by hydrolyzing the beta-lactam ring of antibiotics, rendering them ineffective. The primary mode of action involves the coordination of zinc ions at its active site, enabling the breakdown of a broad spectrum of beta-lactam antibiotics including penicillins, cephalosporins, and carbapenems. This enzymatic activity significantly contributes to antibiotic resistance, posing a challenge in the treatment of bacterial infections. Its prevalence is noted in healthcare settings, where multidrug-resistant organisms are a concern. VIM-15 is of particular interest in clinical microbiology research and antimicrobial resistance studies, where understanding its structure and function can aid in the development of new inhibitors, potentially restoring the efficacy of beta-lactam antibiotics against resistant strains. Its characterization and study are critical for developing strategies to combat antibiotic-resistant infections effectively.</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>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>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>Glucosyltransferase211-freeze dried is an enzyme preparation which is derived from microbial fermentation. This enzyme functions by catalyzing the transfer of glucosyl groups from activated donor molecules to specific acceptor substrates. Its mechanism of action involves the formation of glycosidic bonds, facilitating the synthesis of various oligosaccharides and polysaccharides.</p>

<p>α-Glucosidase (EC 3.2.1.20) is a glycoside hydrolase enzyme that hydrolyzes α-1,4-linked D-glucose residues (e.g. in starch or oligosaccharides)  to produce α-D-glucose. One unit of α-Glucosidase will release 1.0 µmole of p-nitrophenol from the chromogenic substrate mimic 4-nitrophenyl α-D-glucopyranoside per minute at pH 6.8 and 37 °C.</p>

<p>Glucosyltransferase204-freeze dried is an enzyme preparation, derived from specific strains of Streptococcus bacteria, which plays a crucial role in catalyzing the transfer of glucosyl units from donor molecules to acceptor carbohydrates, predominantly in the formation of glucans. This enzymatic activity results in complex carbohydrate structures essential for various biological processes.</p>

<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>

<p>o-Glycosidase (O-Glycanase, endo-a-acetylgalactosaminidase, endo-a-N-acetylgalactosaminidase; EC 3.2.1.97) is an enzyme that specifically removes N-acetylgalactosamine disaccharides, that were attached to serine's or threonine's side-chain oxygen (hence o-Glycosidase). One unit of o-Glycosidase will hydrolyze 1.0 mmole of of substrate per minute at 37 °C and pH 5.0.</p>

<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>

<p>Lysozyme, lyophilized powder, min 45000 FIP U/mg, is an enzymatic product derived primarily from egg white. It is a versatile and potent enzyme known for its ability to hydrolyze the β(1-4) glycosidic bonds in the peptidoglycan layer of bacterial cell walls. This mechanism of action is particularly effective against Gram-positive bacteria due to the accessibility of their peptidoglycan layer.</p>

<p>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.</p>

<p>Lipase 32 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 7 and temp. optimum at 50-70°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 32 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (88 %), laurate (11 %), palmitate (0.3 %) and stearate (0.1 %).</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>Phospholipase A2, liquid, food-grade, is an enzymatic product derived from natural sources, typically microbial or animal tissues, utilized in various lipid modification processes. This enzyme specifically targets phospholipids, catalyzing the hydrolysis of the sn-2 ester bond, which releases free fatty acids and lysophospholipids. Its precise and efficient mode of action allows for targeted alterations in the lipid structure, offering potential benefits in modifying texture, flavor, and stability of food products.</p>

<p>Lipase, powder, food-grade, broad spectrum is an enzyme product, which is derived from microbial sources such as fungi and bacteria through a fermentation process. This enzyme operates by catalyzing the hydrolysis of fats into free fatty acids and glycerol, facilitating the breakdown of complex lipid molecules.</p>

<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>

<p>Aldehyde dehydrogenase (EC 1.2.1.3) is the enzyme that catalyzes oxidation of aldehydes to carboxilic acids, using NAD+ as a cofactor in the following reaction: R-CHO + NAD+ + H2O → R-COOH + NADH + H+    One enzyme unit will oxidize 1.0 μmole of acetaldehyde to acetic acid per min at 25 °C at pH 8.0 in the presence of β-NAD+, potassium and thiols.</p>

<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.</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>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>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>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.</p>

<p>Sucrose phosphorylase (sucrose glucosyltransferase, disaccharide glucosyltransferase, systemic name Sucrose:orthophosphate α-D-glucosytransferase; EC 2.4.1.7) is an enzyme that catalyzes the following reaction:sucrose + Pi ⇌ D-fructose + α-D-glucose-1-phosphateOne unit of Sucrose phosphorylase will produce 1.0 μmole of D-fructose per minute in the presence of sucrose and phosphate under optimum conditions.</p>

<p>Lipase 70 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at 35-45°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 70 was shown to hydrolyze p-Nitrophenyl esters of butyrate (100 % activity), octanoate (62 %), laurate (15 %), palmitate (4 %), stearate (3 %), arachidate (2 %) and behenate (0.2 %).</p>

<p>The improved, thermostable X-ShiningTM Luciferase is suitable for any luciferin-luciferase-based assay using D-luciferin (dLuc) or synthetic pro-luciferins (caged luciferins). Examples of its typical applications include ATP tests in hygiene monitoring, ATP tests in drug screenings and bacteria identification in microbial assays. The thermostable luciferase X-ShiningTM has been optimised by genetic engineering for strongly increased thermostability and storage stability. In temperature stress tests, the enzyme survives temperatures of 60 °C for over an hour, whereas a wild type luciferase from firefly is inactivated after only a few minutes. The extraordinary stability makes it user-friendly and eliminates some of the main disadvantages and limitations of the commonly used wild type luciferase. X-ShiningTM Luciferase is supplied as aqueous solution with glycerol or as a lyophilisate (L-8095), and it may be stored for months at room temperature without significant loss of function. Find out more about our innovative X-Shining range here X-Shining | Innovation | Cymit Quimica Carbosynth.</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. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</p>

<p>5′-Nucleotidase (EC 3.1.3.5) is an enzyme that catalyzes hydrolysis of 5' nucleotides, removing the phosphate group:  AMP + H2O ⇌ adenosine + Pi  One unit of 5′-Nucleotidase will generate 1.0 μmole of phosphate ions per minute in the presence of AMP under optimal reaction conditions.</p>

<p>Phospholipases D belong to the family of esterases and act on phosphatidylcholine in the plasma membrane to release phosphatidic acid (PA) and choline. Phospholipases D can be used as versatile tools in hydrolysis and transphosphatidylation reactions for industrial, chemical and food applications.Spray dried version of EPLD840.6_R</p>

<p>Pyroglutamate aminopeptidase from Pyrococcus furiosus, recombinant from E. coli, is an enzymatic product that specifically targets N-terminal pyroglutamyl residues in peptide chains. This enzyme is derived from the hyperthermophilic archaeon Pyrococcus furiosus, which allows it to exhibit high thermal stability and activity across a broad range of temperatures. Being produced recombinantly in E. coli ensures consistent availability and purity suitable for scientific applications.</p>

<p>Please enquire for more information about Nicotinamide phosphoribosyltransferase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</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. The immobilized Lipase 070 has a temperature optimum at 45 °C and pH optimum between pH 5 and 8, and is covalently immobilized on a polymer resin. Immobilized lipases can be utilized in various reaction types, and are optimal for all reactions in organic solvents or solvent-free systems.</p>

<p>Chloramphenicol acetyltransferase from escherichia coli (EC 2.3.1.28) detoxfies the antibiotic Chloramphenicol by attaching aceryl group. This renders chroramphenicol inactive, as it looses its ability to bind and inactivate ribosomes. One unit of Chloramphenicol acetyltransferase will convert 1 nmol of chloramphenicol and acetyl-CoA to chloramphenicol 3-acetate and CoA per min at pH 7.8 and 25 °C.</p>

<p>This product shows beta-lactamase 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.</p>

<p>Please enquire for more information about Ribokinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Please enquire for more information about Hypoxanthine phosphoribosyltransferase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Please enquire for more information about Sucrose phosphorylase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Please enquire for more information about Dextran dextrinase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Please enquire for more information about Phosphoribosyl pyrophosphate synthase, liquid including the price, delivery time and more detailed product information at the technical inquiry form on this page</p>

<p>Porcine liver esterase (EC 3.1.1.1) is an enzyme that catalyses ester hydrolysis, producing a fatty acid and an alcohol. One unit of esterase will hydrolyze 1.0 μmole of ethyl butyrate to butyric acid and ethanol per min at pH 8.0 and 25 °C. Ethyl butyrate is available here.</p>

<p>Amidase is a hydrolase acting on carbon-nitrogen bonds in linear amides, and can be used in hydrolysis of amides to acids. Amidase 01 is of bacterial origin (P. aeruginosa) and has been produced in E.coli.</p>

<p>Alpha Amylase is an enzyme that catalyses hydrolysis of large polysacharides into smaller fragments. Alpha amylase targets alpha bonds of 1→4 glycosidic linkages of poly- and oligosaccharides with three or more D-glucose units. Systematic name of alpha-amylase is 4-α-D-glucan glucanohydrolase, EC 3.2.1.1. One unit of Alpha Amylase will produce 1.0 mg of maltose from starch in 1 minute at pH 4.9 and 40 °C.</p>