New aspects of naturally occurring proteases in bovine milk.
The scientific literature on milk proteases, along with recent findings in the author's laboratory, are summarized and reviewed comprehensively. Emphasis is on detection of proteolytic enzymes and their activity, purification and kinetic characterization of the isolated enzymes, and technological problems associated with proteolytic enzymes in milk and milk products. Two serine proteinases isolated from milk are compared with plasmin of bovine blood serum. Results from these comparisons strongly suggest that milk proteinase I and plasmin are identical. Proteolysis studies with cold stored milk indicate a direct relationship between gamma-casein formation and milk proteinase association with casein micelles.
D015119:Aminocaproic Acid / Q000494:pharmacology; D000818:Animals; D002364:Caseins / Q000378:metabolism; D002417:Cattle; D010450:Endopeptidases / Q000378:metabolism; D004789:Enzyme Activation / Q000187:drug effects; D005341:Fibrinolysin / Q000378:metabolism; D005511:Food Handling; D007700:Kinetics; D008892:Milk / Q000201:enzymology*; D010447:Peptide Hydrolases / Q000032:analysis / Q000378:metabolism; D011480:Protease Inhibitors; D012697:Serine Endopeptidases; D013379:Substrate Specificity; D014568:Urokinase-Type Plasminogen Activator / Q000494:pharmacology
D002364:Caseins; D011480:Protease Inhibitors; D010450:Endopeptidases; D010447:Peptide Hydrolases; D012697:Serine Endopeptidases; D005341:Fibrinolysin; D014568:Urokinase-Type Plasminogen Activator; D015119:Aminocaproic Acid