In this work, we studied the influence of the type of coagulant enzyme and the curd scalding temperature on the proteolysis and residual coagulant and plasmin activities of a cooked cheese, Reggianito, in the interest of reducing ripening time. A two-factor experimental design was applied in two levels: type of coagulant enzyme, bovine chymosin or camel chymosin, and curd scalding temperature, 50 or 56 °C. The experimental treatments were applied in Reggianito cheese making experiments, and the samples were ripened for 90 d at 12 °C. Scalding temperature influenced residual coagulant activity; the cheeses cooked at 50 °C had significantly higher activity than those treated at 56 °C. In contrast, scalding temperature did not modify plasmin activity. Proteolysis was primarily affected by curd cooking temperature because chymosin-mediated hydrolysis of αs1 casein was slower in cheeses treated at 56 °C. Additionally, the nitrogen content in the cheese soluble fractions was consistently lower in the cheeses scalded at 56 °C than those cooked at 50 °C. A significant influence of the type of coagulant enzyme was observed, especially in the nitrogen fractions and peptide profiles, which demonstrated that camel chymosin was slightly less proteolytic; however, these differences were lower than those caused by the scalding temperature.

The influence of high‐pressure homogenisation (HPH) at 100 MPa on Lacticaseibacillus paracasei 90 (L90) was studied in vitro and in situ (fermented milk and cheese). Lysis and injury signs were observed in cells treated with HPH, which were linked to the release of intracellular enzymes and changes in the metabolic activity of L90. HPH treatment led to a higher lactic acid content and lower pH and pyruvic acid levels in fermented milk. The microbiological and peptide profiles of cheeses were modified by using cells or cell‐free extracts of L90. Finally, this study suggests that L90 could release bioactive peptides.

No abstract