Gouda cheese proteinases

The gross proteolysis of casein is probably due solely to rennet and plasmin activity (O Keeffe et al. 1978). Bacterial proteases and peptides are responsible for subsequent breakdown of the large peptides produced by rennet and plasmin into successively smaller peptides and finally amino acids (O Keeffe et al. 1978). If the relative rate of proteinase activity by rennet, plasmin, and bacterial proteases exceeds that of the bacterial peptidase system, bitterness in the cheese could result. Bitter peptides can be produced from a,-,- or /3-casein by the action of rennet or the activity of bacterial proteinase on /3-casein (Visser et al. 1983). The proteolytic breakdown of /3-casein and the subsequent development of bitterness are strongly retarded by the presence of salt (Fox and Walley 1971 Stadhouders et al. 1983). The principal source of bitter peptides in Gouda cheese is 3-casein, and more particularly the C-terminal region, i.e., 3(193-209) and 3(193-207) (Visser et al. 1983). In model systems, bitter peptides are completely debittered by a peptidases system of S. cremoris (Visser et al. 1983). 

Dozens of different peptides have been identified in cheeses. Most of them arise from and -caseins and a few are from aj2-and K-caseins. The proteinases involved in hydrolysis of aj -casein are mainly cathepsin D originating from milk and cell-envelope proteinase from thermophilic starters, while P- and aj2-caseins are mainly hydrolysed by plasmin. Moreover, peptidases from starters are also active throughout the ripening process, presumably similar to those from non-starter lactic acid bacteria. For example, the bitterness of mature Gouda cheese is caused by calcium and magnesium chlorides, some bitter-tasting free amino acids and is modified by peptides, which arise from the hydrolysis of fS-casein (such as decapeptide Tyr-Pro-Phe-Pro-Gly-Pro-Ile-His-Asn-Ser and derived nonanpeptide without the terminal serine) and casein (tetrapeptide Leu-Pro-Gln-Glu). 

Hydrolysis of the casein micelle-stabilizing K-casein by the action of selected acid proteinases (rennets), and the resultant slow quiescent aggregation of the destabilized micelles in the presence of calcium ions ( 3 mM) at 30-36°C (e.g., for most rennet-curd cheeses such as Cheddar, Mozzarella and Gouda)... 

Kaminogawa, S., Yan T. R., Azuma, N., and Yamauchi, K. (1986). Identification of low molecular weight peptides in Gouda-type cheese and evidence for the formation of these peptides from 23 N-terminal residues of a,i-casein by proteinases of Streptococcus cremoris H61. J. Food Sci 51, 1253-1256. 

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