Enzima

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>In a single vial and in a single step, the X-ShiningTM all-in-one ATP Assay provides an optimized reaction solution for the specific bioluminescent detection of ATP.  Simply reconstitute, and the X-ShiningTM all-in-one ATP Assay solution can be directly applied to samples for ATP measurement in a 1:1 ratio for an immediate bioluminescent read-out. The measurement of ATP levels is crucial to study cell cultures, cell viability, cell response, biochemical processes, to monitor environmental sample activity levels, to assess water quality, to test for biological contamination and to assess biocide efficacy. The X-ShiningTM all-in-one ATP Assay provides sufficient reagent solution to perform 50-to-100 measurements in a 96-well plate and can be easily adapted to measurements in tubes. Find out more about our innovative X-ShiningTM range here X-Shining | Innovation | Cymit Quimica .</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>Dextranase (alternative names dextran hydrolase, endo-dextranase, endodextranase, dextranase DL 2, α-D-1,6-glucan-6-glucanohydrolase, 1,6-α-D-glucan 6-glucanohydrolase, EC 3.2.1.11) is dextran-degrading enzyme that hydrolyzes the α(1→6) glycosidic linkage of dextran, cutting it into progressively shorter fragments, ultimaly producing isomaltose (a disaccharide) and glucose. One unit of dextranase will cleave dextrane to yield 1.0 μmole of isomaltose per min at pH 6.0 and 37 °C.</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>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>

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

A trypsin product which can be used as a standard in proteomics procedures such as mass spectrometry. 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>Pyruvate oxidase is a phosphorylating oxidoreductase which uses FAD as a cofactor to convert pyruvate into acetate and CO2. Pyruvate oxidase (PoxB) is used in metabolism studies in bacteria and in clinical assays for pyruvate, and requires thiamine pyrophosphate (TPP) and magnesium alongside FAD for optimum activity.</p>

<p>Aspartate Aminotransferase (AST), Recombinant is a purified enzyme product utilized extensively in biochemical research and clinical diagnostics. Derived from a recombinant source, this enzyme mirrors the naturally occurring AST found in human tissues, ensuring consistency and reliability in experimental setups.</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 (L-8093), 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>

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.

Phosphorylase is an enzyme that plays a crucial role in carbohydrate metabolism, primarily sourced from various biological organisms, including humans, plants, and bacteria. Its mode of action involves catalyzing the breakdown of glycogen into glucose-1-phosphate by adding an inorganic phosphate group. This process is critical in regulating energy release and storage within cells.

<p>Cholesterol dehydrogenase (EC 1.1.1.840) is NADP+-dependant oxidoreductase, that catalyses the following reaction:cholesterol + NADP+ + H2O → cholest-4-en-3-one + NADPH + H+This is achieved by oxidizing alcohol hydroxy-group into ketone. One unit of cholesterol dehydrogenase will produce 1.0 μmole of cholest-4-en-3-one per minute at pH 8.5 and 25 °C.</p>

<p>Enolase (phosphopyruvate hydratase, EC 4.2.1.11) is an enzyme that catalyses the following reaction:  2-phospho-D-glycerate ⇌ phosphoenolpyruvate + H2O  One unit of enolase will convert 1.0 μmole of 2-phosphoglycerate to phosphoenolpyruvate per minute.</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.

Enzyme involved in the reduction of hydrogen peroxide to water and oxygen. This is a highly important reaction as it protects the cell from oxidative damage.

<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>LacBuster®-L is a novel liquid and ready-to-use sterile beta-lactamase formulation with a broad substrate range against beta-lactam antibiotics including carbapenems, cephalosporins up to 5th generation and penicillins. LacBuster®-L is especially well suited for the direct innoculation method and membrane filtration tests according to US Pharmacopeia (USP &lt;71&gt;) and European Pharmacopeia (EP &lt;2.6.1&gt;). 1 Piece contains 10 vials.</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>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>

Lipase 38 recombinantly expressed in E. coli comes in a spray-dried formulation. It has its pH optimum at 6-8 and temp. optimum at >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 38 was shown to hydrolyze p-Nitrophenyl esters of acetate (27 % activity compared to butyrate), butyrate (100 %), octanoate (9 %) and caprate (5 %).

<p>Endopeptidase, liquid, food grade, broad spectrum is an enzymatic product used in the food industry. It is derived from microbial sources, specifically engineered strains capable of producing high yields of proteolytic enzymes. This endopeptidase functions by hydrolyzing peptide bonds within proteins, targeting internal sites to break down long protein chains into smaller peptides and amino acids.</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>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>

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>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>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>

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.

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>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>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>

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.

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.

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>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>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>

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>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>

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.

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>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>

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.

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.