title: Influence of chymosin type and curd scalding temperature on proteolysis of hard cooked cheeses.
abstract: 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.
authors: Instituto Nacional de Tecnología Agropecuaria (INTA),Estación Experimental Agropecuaria Rafaela,Ruta 34 km 227,2300,Rafaela.Santa Fe,Argentina.
authors: Luciana M
authors: LM
authors: Costabel
authors: Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina.
authors: Carina V
authors: CV
authors: Bergamini
authors: Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina.
authors: Leila
authors: L
authors: Pozza
authors: Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina.
authors: Facundo
authors: F
authors: Cuffia
authors: Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina.
authors: Mario C
authors: MC
authors: Candioti
authors: Instituto de Lactología Industrial,Universidad Nacional del Litoral - Consejo Nacional de Investigaciones Científicas y Técnicas,Santa Fe,Argentina.
authors: Erica
authors: E
authors: Hynes
mesh_terms: D000818:Animals; D001118:Argentina; D002162:Camelus; D002364:Caseins / Q000378:metabolism; D002417:Cattle; D002611:Cheese / Q000032:analysis*; D012085:Chymosin / Q000378:metabolism*; D005341:Fibrinolysin / Q000378:metabolism*; D005511:Food Handling / Q000379:methods*; D006358:Hot Temperature; D006863:Hydrogen-Ion Concentration; D009584:Nitrogen / Q000032:analysis; D010455:Peptides / Q000032:analysis; D059748:Proteolysis
chemical_list: D002364:Caseins; D010455:Peptides; D005341:Fibrinolysin; D012085:Chymosin; D009584:Nitrogen
keywords: Camel chymosin; bovine chymosin; proteolysis; residual coagulant activity; scalding temperature