How can the peptides produced from Emmental cheese give some insights on the structural features of the paracasein matrix?

Abstract

Proteolysis was considered as a typical biochemical parameter which allows cheese ripening and maturity to be characterised. Owing to methods for peptide sequencing, identification of peptides from cheese has been established as an efficient means to determine which proteolytic enzymes are active within cheese, their specificity, and casein molecular structure accessibility via cleavage site identification. This review is an attempt to determine whether these peptides produced in cheese can give information on the structure of paracasein matrix through the action of the inherent proteolysis (added coagulant, milk endogenous proteinases (plasmin, cathepsin) and proteinases and peptidases of bacterial origin). Some answers will be given with special reference to Emmental cheese of which some data on peptide characterisation are presented here.