Neutral Protease

Neutral Protease is a highly efficient proteolytic enzyme that hydrolyzes proteins into peptides and amino acids under neutral pH conditions. It is widely used in feed, and biotechnology industries for controlled protein degradation and hydrolysis applications. Neutral protease is valued for its mild reaction characteristics, high catalytic efficiency, and ability to function effectively without causing excessive damage to sensitive substrates. The enzyme operates optimally around neutral pH, making it suitable for applications requiring balanced processing conditions. Neutral Protease is a non-specific metalloprotease that catalyzes the hydrolysis of peptide bonds in proteins under neutral pH conditions. The enzyme exhibits broad substrate specificity and is particularly effective in degrading denatured and intercellular proteins containing exposed hydrophobic amino acid residues. Neutral protease hydrolyzes N-terminal peptide bonds of non-polar amino acid residues and demonstrates selective activity toward extracellular matrix proteins. It effectively cleaves: Fibronectin Collagen IV Partial activity against Collagen I However, it shows minimal or no hydrolytic activity toward: Collagen V Laminin The enzyme is believed to contain one zinc ion and four calcium ions per subunit, which contribute to its catalytic activity and structural stability.