Enzyme

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.

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 %).

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.

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.

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.

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.

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.

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 %).

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.

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.

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.
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)

Freeze-dried powder with 3300 IU beta-lactamase I activity per vial against all relevant penicillins.  Our penase (penicillinase) posesses a specific substrate range solely against all relevant penicillins.

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.

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.

A proteolytic enzyme; degrades protein contaminants in nucleic acid preparations

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

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