Date of Award:


Document Type:


Degree Name:

Doctor of Philosophy (PhD)


Nutrition, Dietetics, and Food Sciences

Committee Chair(s)

Rodney J. Brown


Rodney J. Brown


Donald J. McMahon


Gary H. Richardson


C. Anthon Ernstrom


Donald V. Sisson


Betty Boeker


Milk coagulation consists of four overlapping phases: enzymic hydrolysis, micelle aggregation, gelation and syneresis. The objectives of this study were to determine the effects of added CaCl2 on milk coagulation and the relationship between enzymic hydrolysis and micelle aggregation with substrate at different concentrations.

Addition of CaCl2 to milk is widely practiced in industry and in laboratories. This changes calcium concentration, pH and ionic strength. It is impossible to separate these three variables and investigate each one independently.

Addition of low levels of CaCl2 shortens coagulation time and increases curd firming rate. Low levels of CaCl2 also accelerate the enzymic hydrolysis process. Calcium ions increase hydrolysis rate, but this effect is much smaller than that of lowered pH. Increase of ionic strength due to addition of CaCl2 has an adverse effect on enzymic hydrolysis. This dominates at high CaCl2 concentration, and the overall coagulation process slows down. Adding CaCl2 also promotes micelle aggregation. However, aggregation is retarded by high levels of added CaCl2.

Results of this study show that about 90% of the κ-casein is hydrolyzed for diluted milk (1/3) to coagulate. Samples at normal concentration (12 g NDM/100 ml solution) require only 60% conversion of κ-casein to para-κ-casein. Addition of CaCl2 significantly decreases this percentage. This suggests a different aggregation and gelation process in samples containing added CaCl2

When pepstatin A is used to stop enzymic hydrolysis at different times, different degrees of κ-casein conversion are obtained. Micelles aggregate even at very low percentages of hydrolysis. Previous reports have stated that a micelle cannot participate in aggregation until almost all of its κ-caseins have been hydrolyzed.



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