Chymosin
Definition:
EC Tree > 3 Hydrolases > 3.4 Acting on peptide bonds (peptidases) > 3.4.23 Aspartic endopeptidases > 3.4.23.4 chymosin
Chymosin is a neonatal gastric aspartic endopeptidase formed from prochymosin, with high milk-clotting and weak general proteolytic activity, found among mammals that absorb immunoglobulins after birth. It belongs to peptidase family A1. Its broad specificity resembles pepsin A; it clots milk by cleaving a single Ser-Phe105-/-Met-Ala bond in the kappa-chain of casein. In the suckling stomach it curdles milk for digestion while sparing casein micelles. It features a pepsin-like aspartic-protease fold widely used in cheese making.
Chymosin is a neonatal gastric aspartic endopeptidase formed from prochymosin, with high milk-clotting and weak general proteolytic activity, found among mammals that absorb immunoglobulins after birth. It belongs to peptidase family A1. Its broad specificity resembles pepsin A; it clots milk by cleaving a single Ser-Phe105-/-Met-Ala bond in the kappa-chain of casein. In the suckling stomach it curdles milk for digestion while sparing casein micelles. It features a pepsin-like aspartic-protease fold widely used in cheese making.
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