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Neutral Protease is a type of protease that acts on the peptide bond of protein under neutral pH conditions, it can hydrolyze protein into amino acids, peptides and free amino acids.
| CAS Number | 9068-59-1 |
| Solubility (25°C) | Soluble in water |
| Storage | 2-8°C, protect from light, dry, sealed |
| Related Enzymes & Coenzymes Products |
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| Glucose isomerase
Glucose isomerase can catalyze the reversible isomerization of D-glucose and D-xylose into D-fructose and D-xylulose, respectively. |
| β-Galactosidase (from Aspergillus oryzae)
β-Galactosidase acts on the terminal β-D-galactosyl moieties of disaccharides, glycoconjugates, and polysaccharides. It is useful in mediating transglycosylation reactions such as the synthesis of galactooligosaccharides (GOS). β-Galactosidases might be used for glycobiological and biotechnological applications. β-galactosidase cleaves lactose into its monosaccharide components, glucose and galactose. It also catalyses the transglycosylation of glucose into allolactose, the inducer of β-galactosidase, in a feedback loop. |
| Butyryl Cholinesterase (Horse serum)
Butyryl Cholinesterase is a serine hydrolase that is structurally similar to acetylcholinesterase (AChE) but has different substrate specificity and inhibitor sensitivity. The enzyme is a tetrameric glycoprotein composed of four identical subunits (110 kDa each) and is also known as pseudocholinesterase. It is synthesised in the liver and distributed in blood, neuromuscular junction synapses, glial cells and white matter axons. |
| β-Glucosidase (from Almonds)
β-Glucosidase is the main component of glycoside hydrolases that hydrolyse Glucoside into glucose and other constituents. β-Glucosidase works by breaking down fibre-rich cell walls to release and utilise the nutrients such as proteins and starch contained therein, while at the same time degrading the fibre to reducing sugars that can be digested and assimilated by the body of the animal. |
| Diaphorase
Diaphorase has been used in a study to assess the protein-protein interactions in assembly of lipoic acid on the 2-oxoacid dehydrogenases of aerobic metabolism. |
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