Influence of ß-casein genotype on physicochemical properties and functionality of bovine milk.

Several studies have been focused on the effect of milk protein genetic variants on milk physicochemical properties and functionality in recent years. ß-casein, an important protein related to milk processibility, has been reported to have 2 main genetic variants A1 and A2, for which cows may be homozygous or heterozygous. In this study, several physicochemical properties of milk with ß-casein variants A1A1, A1A2, and A2A2 from 3 collection occasions were analyzed. Higher manganese content and lower pH were found to be associated with the A1A1 variant compared with the other 2 genotypes. Better rennet and acid coagulation were found in A1A1 milk compared with A1A2 and A2A2 milk (although P > 0.05), whereas A2A2 milk was more stable to creaming compared with the other 2 genotypes, which may be linked to its smaller fat globule size. Thus, milk from cows with A1A1 genotype could be preferable for cheese making, while that with A2A2 variant can be used in formulations requiring good stability against creaming, and for example, yogurt making, where the softer yogurt texture may be easier to digest.

The contribution of lactococcal starter proteinases to proteolysis in cheddar cheese.

The contribution of the lactococcal proteinase to proteolysis and flavor development in Cheddar cheese was investigated using the starter strains Lactococcus lactis ssp. lactis UC317, its proteinase-negative derivative FH041, and variants of UC317 modified in proteinase production, location, and specificity. Lactococcus lactis ssp. lactis FH041 was transformed by electroporation with plasmids pCI3601, pCI3602, or pNZ521. Plasmids pCI3601 and pCI3602 harbor the cloned proteinase genes of L. lactis ssp. lactis UC317 on a high copy number vector and, as such, encode an increased concentration of cell wall-associated and secreted enzymes, respectively. Plasmid pNZ521 contains the cloned proteinase genes from Lactococcus lactis ssp. cremoris SK11. Assessment of proteolysis and flavor development in Cheddar cheese made with these strains revealed that starter proteinases are required for the accumulation of small peptides and free amino acids in Cheddar cheese. Proteolysis was not enhanced by an approximately threefold increase in concentration of the lactococcal proteinase. The strain in which the proteinase remained attached to the cell wall appeared to contribute more to proteolysis than the strain that secreted the enzyme. Water-soluble peptides unique to Lactococcus lactis ssp. cremoris SK11 and L. lactis ssp. lactis UC317 were detected by PAGE and HPLC, respectively. Sensory evaluation showed that the flavors of all cheeses made with proteinase-positive starters were similar, but cheeses made with proteinase-negative starters lacked flavor.