Recombinant chymotrypsin is a serine endopeptidase that is expressed in E. coli expression system and purified by HPLC. Its amino acid sequence is the same as that of human chymotrypsin. Recombinant chymotrypsin can selectively hydrolyze the peptide bonds formed by the C-terminus of aromatic amino acids such as tyrosine, phenylalanine and tryptophan. It can also hydrolyze the peptide bonds formed by leucine and methionine at a slower rate. , Can also act on esters formed by sensitive amino acids. The optimum pH of chymotrypsin is 7.0--9.0. Recombinant production, no foreign virus contamination, such as swine flu virus, porcine parvovirus, etc. No contamination by other miscellaneous enzymes: No other side reactions in the digestion reaction. Freeze-dried powder, easy to store and transport; mass production, stable product quality. Used alone, or together with other proteases to digest protein, or other special purposes, such as organic synthesis, etc.
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