The rheological characterization of stirred yogurt with added milk fat, Na caseinate (or micellar casein) and gelatin (4 Bloom strengths), starch or a xanthan gum/LBG 50:50 mixture was carried out. Dynamic and shear values were measured at 8°C and syneresis at 4°C. Consistency (k* and k) and syneresis were more frequently influenced by the composition variables than the power law factors n* and n and the critical strain ␥ c . The k* ranged from 15.8 to 576 Pa s n* , n* from 0.038 to 0.220,␥ c from 1.6 to 49.0 ∞ 10 -3 , k from 0.37 to 32.47 Pa s n , n from 0.005 to 0.587, and syneresis from 0.0 to 49.2%.

Two sets of Cheddar cheese were made in which the milk protein level (%, wt/wt) was increased from 3.3 (Control A, CA) to 3.6 (set A) or from 3.3 (control B, CB) to 4.0 (set B) by the addition of phosphocasein (PC), milk protein concentrate (MPC), or freshly prepared ultrafiltered milk retentate (UFR). The cheeses were denoted CA, PCA, MPCA, and UFRA from set A, and CB, PCB, MPCB, and UFRB, from set B, respectively. The level of cheese moisture decreased significantly on increasing milk protein level from 3.3 to 3.6 or 4.0% (wt/wt), but was not affected significantly by the method of protein standardization. The percentage milk fat recovered to cheese increased significantly on increasing the level of milk protein from 3.3 to 3.6% (wt/wt) with PC, and from 3.3 to 4.0% (wt/wt) with PC, MPC, and UFR. Increasing milk protein level from 3.3 to 4.0% (wt/wt) with PC significantly increased the percentage of milk protein recovered to cheese. Actual cheese yield increased significantly with milk protein level. The yield of cheese per 100 kg of milk normalized to reference levels of fat (3.4%, wt/wt) and casein (2.53%, wt/wt) indicated no significant effects of protein content or standardization treatment on yield. However, the moisture-adjusted yield per 100 kg of milk with reference levels of fat and casein increased significantly on increasing the protein content from 3.3 to 3.6% (wt/wt) with MPC and from 3.3 to 4.0% (wt/wt) with PC, MPC, and UFR.

The role of the free sulfhydryl group of beta-lactoglobulin in the formation of a stable non-native monomer during heat-treatment of beta-lactoglobulin solutions was investigated. Two concomitant events occurred at the earlier stage of heating: unfolding of native globular monomer and intramolecular sulfhydryl/disulfide exchange reaction. Thus, two denatured monomeric species were formed: a non-native monomer with exposed Cys-121 (Mcys121) which became reversible after cooling, and a stable non-native monomer with exposed Cys-119 (Mcys119) which exhibited both a larger hydrodynamic conformation than native monomer and low solubility at pH 4.7. The results also show that the formation of these monomeric species throughout heat-induced denaturation of native beta-lg monomers is faster than their subsequent aggregation. A mechanism describing the behavior of beta-lg denaturation/aggregation during heat-treatment under selected conditions (5.8 mg/ml, low ionic strength, pH 6.6, 85 degrees C) is presented.

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