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The effect of milk preacidification on cheese manufacturing, chemical properties, and functional properties of low fat Mozzarella cheese was determined. Four vats of cheese were made in 1 d using no preacidification (control), preacidification to pH 6.0 and pH 5.8 with acetic acid, and preacidification to pH 5.8 with citric acid. This process was replicated four times. Modifications in the typical Mozzarella manufacturing procedures were necessary to accommodate milk preacidification. The chemical composition of the cheeses was similar among the treatments, except the calcium content and calcium as a percentage of protein were lower in the preacidified treatments. During refrigerated storage, the chemical and functional properties of low fat Mozzarella were affected the most by milk preacidification to pH 5.8 with citric acid. The amount of expressible serum, unmelted cheese whiteness, initial unmelted hardness, and initial apparent viscosity were lower with preacidification. The reduction in initial unmelted cheese hardness and initial apparent viscosity in the pH 5.8 citric treatments represents an improvement in the quality of low fat Mozzarella cheese that allows the cheese to have better pizza bake characteristics with shorter time of refrigerated storage.

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SUMMARYThe type and relative amounts of plasminogen activator (PA) in different fractions of bovine milk obtained from 15 Holstein cows were examined. Raw milk was centrifuged to separate skim milk and a somatic cell pellet. PA was mainly localized within the casein fraction, being 42 times that in the serum, and in association with somatic cells. The predominant form of PA in milk casein was isolated from SDS-PAGE gel extracts and had a molecular mass of ∽75 kDa. Its activity was increased 41-fold (P < 0·01) in the presence of fibrin but was unaffected by the presence of amiloride, indicating that it was due to tissue-PA. The predominant forms of PA associated with milk somatic cells were isolated from SDS-PAGE gel extracts and had molecular masses of ∽ 30 and ∽ 50 kDa. The activity of both proteins was unaffected by the presence of fibrin but was dramatically reduced by the presence of amiloride, indicating that they represented urokinase-PA.

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