Chemical interactions among caseins during rennet coagulation of milk.

Rennet milk curds were prepared under 4 different temperature and acidity conditions. The development of different types of inter-protein chemical bonds (disulfide, hydrophobic, electrostatic, hydrogen, and calcium bridges) was monitored for 60 min after curd cutting. Hydrophobic inter-protein interactions originally present in casein micelles in milk were substituted by electrostatic, hydrogen, and calcium bonds throughout the curd curing period. Disulfide bonds were not disturbed by the experimental conditions employed in the study, remaining at a constant level in all studied treatments. Acidification of curds increased the availability of soluble ionic calcium, increasing the relative proportion of calcium bridges at the expense of electrostatic-hydrogen bonds. Although pH defined the nature of the interactions established among proteins in curd, temperature modified the rate at which such bonds were formed.

Structure rearrangement during rennet coagulation of milk modifies curd density.

Milk curds are a semisolid structure resulting from the enzymatic coagulation of milk, consisting mainly of paracasein micelles, fat globules, and whey. This gel undergoes a series of changes in its composition and structure during setting and curing, affecting curd density. The present study investigated the composition and density of inoculated and noninoculated milk curds during a 60-min curing period conducted at 30, 35, and 40°C. The purpose of the study was to determine the density changes occurring in the protein phase of curds during curing under different conditions of temperature and pH to understand the nature of the structural changes happening in the paracasein matrix. Noninoculated curd density values oscillated between 1.0247 and 1.0294 g/cm3 after 60 min of curing, whereas inoculated treatments showed values between 1.0222 and 1.0321 g/cm3. This small difference in density between the studied samples was surprising because the whey content of samples differed greatly. Density of the protein phase reached values of 1.8002 and 1.4388 g/cm3 for noninoculated and inoculated curds, respectively, after 60 min of curing. Two independent mechanisms involved in the development of the protein-based structure of curds were identified upon comparison of the development of protein phase density in inoculated and noninoculated curds. Although the larger increase in protein phase density observed in noninoculated curds was probably due to the concurrent action of calcium-mediated electrostatic bonds and temperature-dependent hydrophobic bonds, inoculated curds showed a lower protein phase density caused by calcium solubilization and by a decrease in the net charge of paracasein micelles induced by pH reduction.