Neutral Protease Dispase(R), Animal Origin Free

Neutral protease (Dispase(R)) is purified and one unit releases one micromole of Folin positive amino acids, measured as tyrosine, at 37°C, pH 7.5, using casein as the substrate. The enzyme is known to contain 1g-atom of zinc per g-mol of purified enzyme. If this zinc component is removed by chelating agents such as EDTA or EGTA, an inactive apoenzyme is obtained. Calcium has been detected in the purified protein and is believed to play a role in maintaining the structure and configuration, and preventing autolysis. Neutral protease is a non-specific metalloprotease. It cleaves fibronectin, collagen IV, and to a lesser extent collagen I, but it does not cleave collagen V or laminin. It hydrolyzes N-terminal peptide bonds of non-polar amino acid residues and may preferentially attack denatured and intercellular proteins with exposed hydrophobic amino acid residues. It is believed to bind one zinc ion and four calcium ions per subunit. Unlike other Bacillus species that produce neutral, alkaline, or a mixture of both proteases, Paenibacillus polymyxa is one of three species that produces only a neutral protease. Protein function: Involved in the generation of beta- and alpha-amylases from the large amylase precursor. [The UniProt Consortium]