RESUMEN
Thermally induced changes in milk proteins and minerals, particularly interactions among caseins and denatured whey proteins, influence important properties of dairy products in both positive and negative ways. Whereas the extensive protein connectivity and increased water-holding capacity resulting from such heat-induced protein modification account for the much desired firmness of acid gels of yogurt, thermal processing, on the other hand, severely impairs clotting and adversely affects the cheesemaking properties of rennet-coagulated cheeses. In technological terms, the principal ongoing challenge in the cheese industry is to take advantage of the water-holding capacity of thermally aggregated whey proteins without compromising the rennetability of cheese milk or the textural and functional attributes of cheese. Including some recent data from the authors' laboratory, this paper will discuss important aspects and current literature on the use of thermally processed milk in the production of rennet-coagulated cheeses and also some of the potential alternatives available for inclusion of whey proteins in cheese, such as the addition of microparticulated whey proteins to cheese milk.
Asunto(s)
Queso/análisis , Quimosina/química , Manipulación de Alimentos/métodos , Leche/química , Animales , TemperaturaRESUMEN
Casein micelles were separated from unheated reconstituted skim milk powder (RSMP) and were resuspended in the serum of RSMP that had been heated, with and without dialysis of this serum against unheated RSMP. Using size-exclusion chromatography, it was found that the soluble complexes of whey protein (WP) with κ-casein in the serum of the heated milk bind progressively to unheated casein micelles during renneting, even prior to the onset of clotting. Similar trends were noted when casein micelles from RSMP heated at pH values of 6.7, 7.1, or 6.3, each with different amounts of WP coating the micelles, were renneted in the presence of soluble WP/κ-casein complexes. No matter what was the initial load of micelle-bound WP complexes, all micelle types were capable of binding additional serum protein complexes during renneting. However, it is not clear that this binding of WP/κ-casein complexes to the micellar surface is a direct cause of the impaired rennet clotting of the RSMP.