Enzima

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 > 6 months at 4-25°C can be guaranteed.
Key features are:

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.

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.

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.

A proteolytic enzyme; degrades protein contaminants in nucleic acid preparations

Peroxidase 12 recombinantly expressed in P. pastoria comes in a freeze-dried formulation. It has its pH optimum at 5-8 and temp. optimum at 20-40°C. 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. Peroxidase 12 was shown to act on styrene, veratryl alcohol, vanillyl alcohol, n-methyl anthranilate and thioanisole.

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.

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 %).

A catalase product which neutralizes hydrogen peroxide at much higher concentrations (>10 %) compared to pyruvate, which is only capable of completely neutralizing hydrogen peroxide at the lowest concentration tested (2 %). Catalase (EC 1.11.1.6) catalyzes the following reaction:2H2O2 → 2H2O + O21 unit of catalase will decompose 1.0 μmole of H2O2 per min at pH 7.0 and 25 °C.

Phospholipase D 040, concentrated (100 U/mg), spray-dried, recombinant, of prokaryotic origin, is an enzyme preparation designed for advanced biochemical applications. This enzyme is derived from a prokaryotic source through recombinant DNA technology, allowing for high purity and activity. Phospholipase D functions by catalyzing the hydrolysis of phospholipids to produce phosphatidic acid and free head groups, which is a crucial reaction in both lipid signaling and membrane dynamics.

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.

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.

ALPK1 Protein, Human, Recombinant (His & Myc) is expressed in Baculovirus.

The kit contains 8 different Glucosyltransferases (GTases), which are enzymes that transfer glucose to another organic molecule (aglycon), establishing glycosidic linkage. UDP-glucose dependent GTases are part of the enzyme family of glucosyltransferases, they are versatile tools in glucosylation reactions. Different GTases have different substrate specificities, as shown on Table 1. The kit is especially designed for screening and finding the most well-suited GTase for your specific process. All GTases in the kit are also available individually for bulk purchase.

Nitrile hydratase 21 recombinantly expressed in E. coli comes in a freeze-dried formulation. Nitrile hydratases can be utilized to convert nitriles into their corresponding amides, e.g. to produce acrylamide from acrylonitrile. Additional applications include the removal of nitriles from industrial wastewater. Our nitrile hydratases have been tested for hydrolysis of the following substrates:cyclohexanecarbonitrile, cinnamonitrile, benzonitrile, methacrylonitrile, pivalonitrile.

A pyridoxal phosphate-containing enzyme that converts L-methionine to α-ketobutyrate, ammonia and methyl mercaptan. Recombinant from e.coli source.  
EC 4.4.1.11

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. The Phospholipase D Kit contains 4 enzymes with a broad pH range for transphosphatidylation activity.

A protease enzyme from bacillus subtilis which catalyzed proteolysis, a process that breaks down proteins and peptides to small polypeptides or amino acids

E. coli recombinant α-2,6 sialyltransferase from Neisseria meningitidis. One unit is defined as the amount of enzyme that catalyses the formation of 1 μmol CMP-Neu5Ac from CTP and Neu5Ac per minute at 37 ºC.Activity: 100U/mg