Introduction: Chymotrypsin is a serine protease enzyme that catalyzes the hydrolysis of peptide bonds in proteins, particularly at aromatic amino acid residues such as phenylalanine, tyrosine, and tryptophan. It is an important digestive and proteolytic enzyme widely used in pharmaceutical. Chymotrypsin plays a significant role in protein digestion and controlled protein hydrolysis. Due to its selective proteolytic activity, it is commonly used in enzyme formulations, tissue dissociation, wound care preparations, and biochemical research applications.
Chymotrypsin is commonly obtained from the pancreas of healthy bovine origin under controlled extraction and purification processes. Recombinant production technologies may also be used for specialized applications. Bovine pancreas The enzyme is purified and standardized to ensure consistent enzymatic activity, purity, and product quality.
Hydrolyzes peptide bonds in proteins Cleaves proteins at aromatic amino acid residues Converts proteins into peptides and amino acids Cleavage Preference Phenylalanine Tyrosine Tryptophan
Customized activity available as per customer s requirement standard: FIP/USP/IP/BP/EP
Highly specific proteolytic activity Effective protein digestion capability Suitable for pharmaceutical and biotechnology applications Functions optimally under mild alkaline conditions
Chymotrypsin is available in 1 kg, 5 kg, and 25 kg packing options, with customized packaging available upon request for specific commercial requirements.
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