| Autor: |
Costabel LM; Instituto Nacional de Tecnología Agropecuaria (INTA),Estación Experimental Agropecuaria Rafaela,Ruta 34 km 227,2300,Rafaela.Santa Fe,Argentina., Bergamini CV; Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina., Pozza L; Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina., Cuffia F; Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina., Candioti MC; Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina., Hynes E; Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina. |
| Abstrakt: |
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. |
