Enzyme

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.

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

Penicillin G acylase, 10mg/ml aqueous solution, is a biocatalytic enzyme used in pharmaceutical research and production. This enzyme is typically sourced from various microbial species, predominantly bacteria, through fermentation processes. Its primary mode of action involves the hydrolysis of penicillin G, catalyzing the cleavage of the side chain amide bond to produce 6-aminopenicillanic acid (6-APA), a core building block for the synthesis of a variety of semi-synthetic penicillins.

Hydrolytic enzyme; biocatalyst in production of beta-lactam antibiotics

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.

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.

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.

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 %).

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 %).

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.

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.

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.

Elastase is a proteolytic enzyme that breaks down elastin

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.

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 %).

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.

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.