Proteolysis in accelerated ripened goat milk Jack cheese

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Pasteurized milk from Alpine goats was processed into control and accelerated ripened Jack cheeses. Mesophilic culture, Lactococcus lactis subsp lactis, was added to ferment cheese milk at the rate of 2% (v/v). The same culture was grown in 1 I batches of tryptic soy broth and bacterial cells were harvested by centrifugation. Harvested cells were washed with distilled water, disrupted, and the cellular extract was mixed with curd at 0.14 and 0.27 (g/100 g) to accelerate ripening of the treated cheeses. Control cheese did not contain any additional cellular extract. The treated cheeses had higher percentages of water soluble nitrogen when compared with the control. Similarly, the activity of endo- and exopeptidases was the lowest in the control during aging while the treatment with 0.14% extract had the second highest and the treatment with 0.27% extract had the highest level of enzymic activity. Electrophoretic analysis of the caseins in the cheese revealed that β-casein was the most abundant casein and was less susceptible to proteolysis while αs2 and κ-caseins were the second and the third major caseins in goat milk Jack cheese, respectively.

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