Chymotrypsin Porcine

Alpha Chymotrypsin is a proteolytic enzyme that belongs to the serine protease family. It has a molecular mass of approximately 25 kDa and is composed of a single polypeptide chain. The enzyme’s active site contains a serine residue, which is essential for its catalytic activity. The enzyme cleaves peptide bonds selectively after large hydrophobic amino acids such as tryptophan, tyrosine, and phenylalanine .

Alpha Chymotrypsin is purified from the pancreas of pigs. The purification process involves several steps, including extraction, precipitation, and chromatography, to obtain a highly pure and active enzyme. The enzyme is typically available as a lyophilized (freeze-dried) powder, which can be reconstituted in aqueous solutions for various applications .

1. Biochemical Research: Alpha Chymotrypsin is extensively used in biochemical research to study protein structure and function. It serves as a model enzyme for understanding proteolytic mechanisms and substrate specificity.
2. Pharmaceutical Industry: The enzyme is used in the production of certain pharmaceuticals, including anti-inflammatory drugs and digestive aids.
3. Industrial Applications: Alpha Chymotrypsin is employed in the food industry for protein hydrolysis and in the leather industry for dehairing hides.

Lyophilized Alpha Chymotrypsin is stable at room temperature for up to three weeks. However, for long-term storage, it should be kept desiccated below -18°C. Upon reconstitution, the enzyme should be stored at 4°C for short-term use (2-7 days) and below -18°C for long-term use. It is recommended to add a carrier protein, such as 0.1% human serum albumin (HSA) or bovine serum albumin (BSA), to prevent freeze-thaw cycles .

Alpha Chymotrypsin is intended for laboratory research use only. It should not be used as a drug, agricultural or pesticidal product, food additive, or household chemical. Proper safety measures should be taken while handling the enzyme to avoid inhalation, ingestion, or contact with skin and eyes .