TL;DR: In this article, the main forms of caprine and ovine caseino-macropeptides (CMP), which are the soluble C-terminal derivatives from the action of chymosin on β-casein during the milk clotting process of cheesemaking, have been identified and are a good source of antithrombotic peptides.
TL;DR: Proteolysis in cheese has been the subject of active research in the last decade; there have been developments in the analytical techniques used to monitor proteolysis and patterns of proteolyisation in many cheese varieties have now been investigated as mentioned in this paper.
TL;DR: The texture of a cheese is determined primarily by its pH and the ratio of intact casein to moisture, which is controlled largely by the proportion of residual rennet and plasmin in the cheese, salt to moisture ratio, and storage temperature.
TL;DR: In this paper, a number of Cheddar cheese samples of different ages, pH and moisture content have been examined rheologically and electrophoretically to determine whether the progressive changes in cheese texture were related to casein proteolysis.
Abstract: A number of Cheddar cheese samples of different age, pH and moisture content have been examined rheologically and electrophoretically to determine whether the progressive changes in cheese texture were related to casein proteolysis. The force-compression curves obtained by crushing cubes of cheese between small flat plates at constant speed were different for the different cheese samples and were affected by the moisture content, pH and extent of αsl-casein proteolysis that had taken place in the cheese. These results support a model of cheese micro structure in which an extensive network involving αsl- casein molecules traverses the cheese and as the cheese ripens, chymosin cleavage of αsl-casein weakens the protein network. Such a model explains the rapid decrease in Cheddar cheese yield-force that occurs during the early stages of ripening.
TL;DR: Proteolysis in cheese during ripening is catalyzed by proteinases and peptidases from six sources: (1) the coagulant, the enzymes involved depend on the type of coagula used.
Abstract: This chapter discusses proteolysis process in cheese during ripening. Proteolysis contributes to: (1) The development of cheese texture: via hydrolysis of the protein matrix of cheese; via a decrease in aw through changes to water binding by the new carboxylic acid and amino groups liberated on hydrolysis of peptide bonds. These groups are ionized at the pH of cheese and thus bind water; indirectly via an increase in pH caused by the liberation of ammonia from amino acids produced by proteolysis. (2) Flavor and perhaps the off-flavor of cheese, directly by the production of short peptides and amino acids, some of which have flavors; indirectly by the liberation of amino acids, which act as substrates for a range of catabolic reactions, which generate important volatile flavor compounds; by facilitating the release of sapid compounds from the cheese matrix during mastication. Proteolysis in cheese during ripening is catalyzed by proteinases and peptidases from six sources: (1) the coagulant—the enzymes involved depend on the type of coagulant used. (2) the milk—a number of indigenous proteinases are present in milk, the most important of which is plasmin, which is produced from an inactive precursor, plasminogen. (3) starter lactic acid bacteria (LAB) contain a cell envelope-associated proteinase, which contributes to ripening principally by hydrolyzing intermediate-sized and short peptides produced from the caseins by the action of chymosin or plasmin. The other three sources are nonstarter lactic acid bacteria (NSEAB), secondary starter ( Propionibacterium freudenreichii subsp, shermanii in Swiss-type cheese), and exogenous proteinases and peptidases.