Skip to content

Factors That Lower the Heat Stability of Milk

5 min read

Over 90% of milk's heat stability is determined by the casein fraction of its proteins, making its composition a primary determinant of processing outcomes. Factors that lower the heat stability of milk can cause coagulation or gelling during high-temperature treatments like pasteurization or sterilization.

Quick Summary

An unstable dairy product can coagulate, curdle, or form sediment when heated due to changes in its protein and mineral balance. High-temperature processing, mineral imbalances, changes in pH, and elevated protein content are major contributors to this heat-induced destabilization.

Key Points

  • pH Level: The pH of milk is a crucial factor, with maximum heat stability occurring around pH 6.7-6.8; deviating from this range increases the likelihood of coagulation.

  • Mineral Balance: High levels of ionic calcium, in particular, can destabilize milk by promoting the aggregation of casein micelles during heating.

  • Protein Concentration: Increased protein concentration, especially in evaporated or reconstituted milk, heightens protein-protein interactions and aggregation at high temperatures, lowering stability.

  • Proteolytic Enzymes: Heat-resistant proteases from psychrotrophic bacteria or naturally occurring plasmin can degrade casein, leading to gelation and curdling, particularly in UHT milk.

  • Processing Conditions: Techniques such as homogenization and excessive preheating can alter the milk's protein structure and mineral balance, negatively impacting heat stability.

  • Seasonal Variations: Changes in cow's diet and environment throughout the year lead to seasonal variations in milk composition, which can affect its heat stability.

In This Article

The heat stability of milk refers to its capacity to withstand high temperatures without undergoing coagulation or gelation. This property is crucial for a wide range of dairy processes, especially those involving sterilization and ultra-high temperature (UHT) treatment. A delicate balance of milk's natural components, particularly proteins and minerals, dictates its resilience to heat. When this balance is disturbed by various intrinsic or extrinsic factors, the milk's stability is lowered, leading to adverse effects on product quality.

The Role of pH and Mineral Balance

One of the most influential factors governing milk's heat stability is its pH level, which is closely tied to the complex interplay of calcium and phosphate ions.

The Critical pH Range

Milk's heat stability exhibits a characteristic profile when plotted against pH. For bovine milk, a maximum stability is typically observed near its natural pH of 6.7–6.8. As the pH shifts away from this optimal range—either becoming more acidic (below 6.4) or more alkaline (above 7.0)—the stability decreases significantly, and the milk becomes more susceptible to coagulation. The destabilizing effect at lower pH is due to the proteins moving closer to their isoelectric point (around pH 4.6), where their net charge is zero, causing them to aggregate more readily. At higher pH values, the instability is linked to a different set of protein and mineral interactions.

The Dynamic Salt Balance: Calcium and Phosphate

Milk's stability is maintained by the colloidal calcium phosphate (CCP) that holds casein micelles together. During heating, the solubility of calcium phosphate decreases, causing some soluble calcium and phosphate to move into the colloidal phase. This shifts the mineral equilibrium, which in turn affects the net charge and structure of the casein micelles, potentially leading to aggregation. Excessive ionic calcium is a major destabilizing agent, and fortification with calcium salts can substantially reduce heat stability. In contrast, citrates and phosphates can act as stabilizing salts, improving heat stability by sequestering calcium and altering the mineral balance.

Seasonal Variations in Composition

Milk composition is known to vary with the seasons, which directly impacts its heat stability. Research shows that milk collected in autumn and winter often has better UHT stability than that collected during spring and summer. This is likely due to changes in feeding regimes, environmental temperatures, and the stage of lactation, which influence the milk's protein, fat, and mineral content.

Protein Interactions and Concentration

Milk proteins, particularly caseins and whey proteins, undergo complex changes when exposed to heat, and their concentration plays a significant role in determining stability.

Casein and Whey Protein Interactions

Casein micelles are naturally protected from aggregation by a 'hairy layer' of κ-casein. During heat treatment, whey proteins, especially β-lactoglobulin, denature and interact with this κ-casein layer through disulfide bonds. This disrupts the protective layer and can either stabilize or destabilize the micelles, depending on the pH and concentration. At low pH, denatured whey proteins help stabilize the micelles, while at higher pH in concentrated milk, their aggregation is a strong destabilizing factor.

Increased Protein Concentration

Concentrated milks are inherently less heat-stable than unconcentrated milk. The higher protein density, particularly the elevated levels of ionic calcium and increased viscosity, promotes greater protein-protein interactions and aggregation at high temperatures, leading to a significant drop in stability. For example, studies on milk protein concentrates (MPCs) have shown a substantial decline in heat stability when the protein content was increased from 4% to 8%.

Microbial Contamination and Processing Factors

Beyond milk's intrinsic composition, external factors such as microbial load and mechanical processing can also reduce heat stability.

Proteolytic Bacteria

Psychrotrophic bacteria, which can grow at cold storage temperatures, produce heat-resistant proteases that can degrade milk proteins. While pasteurization kills these bacteria, their enzymes can remain active and cause gelation during the storage of UHT milk. High somatic cell counts in milk, which are often correlated with heat stress in dairy cattle, can also increase plasmin activity, an endogenous heat-resistant protease that contributes to protein degradation and instability.

Effect of Homogenization and Preheating

Processing methods can significantly impact heat stability. Homogenization, especially at higher pressures, reduces the size of fat globules and causes more protein to adsorb onto their new surfaces, which can reduce stability. The severity of preheating can also alter stability. While mild preheating can improve stability by promoting beneficial whey protein-casein interactions, excessively severe preheating can have a detrimental effect by causing unwanted aggregation.

Factor How it Lowers Heat Stability Impact on Milk Components
Sub-Optimal pH Shifts away from the ideal pH range (6.7-6.8) disrupt the charge balance of casein micelles. At low pH, proteins approach their isoelectric point and aggregate. At high pH, denatured whey protein can promote aggregation.
High Ionic Calcium An excess of soluble calcium ions promotes protein aggregation by neutralizing the negative charges on casein micelles. Causes an increase in micellar calcium phosphate formation upon heating, destabilizing the casein structure.
Concentration Higher concentration of proteins and minerals leads to greater interactions and aggregation during heat treatment. Increases the viscosity and likelihood of protein-protein interactions, reducing heat coagulation time.
Proteolytic Enzymes Heat-resistant enzymes produced by bacteria or naturally occurring in milk degrade casein, leading to gelation over time. Hydrolyzes milk proteins, primarily caseins, which weakens the micelle structure.
Homogenization High-pressure homogenization increases the surface area of fat globules, leading to protein adsorption and destabilization. Casein and other proteins are redistributed to the new fat globule membrane, reducing their availability for colloidal stability.
Seasonal Changes Seasonal variations affect milk composition, including fat, protein, and mineral content, impacting stability. For example, milk in spring and summer may have a composition that is less conducive to heat stability than winter milk.

Conclusion

Maintaining the heat stability of milk is a complex challenge influenced by a multitude of interconnected factors. Shifts in pH, an imbalance of minerals—particularly calcium and phosphate—and elevated protein concentrations are key intrinsic destabilizing agents. Furthermore, external factors such as proteolytic enzyme activity from bacteria and the mechanical stress of processing techniques like homogenization and excessive preheating can contribute to instability. Understanding these intricate relationships is vital for the dairy industry to ensure high-quality and consistent dairy products, especially those requiring severe heat treatments. Proper management of milk composition and processing conditions is essential to mitigate these risks and prevent costly product failures.

Frequently Asked Questions

The primary cause of milk instability during heating is the aggregation of milk proteins, particularly caseins and denatured whey proteins, which are sensitive to changes in pH, mineral balance, and protein concentration.

Milk is most heat-stable at its natural pH of 6.7–6.8. A shift to a more acidic or alkaline pH causes the proteins to move closer to their aggregation point, thereby decreasing heat stability and increasing the risk of coagulation.

Yes, some psychrotrophic bacteria produce heat-resistant proteolytic enzymes that survive pasteurization. These enzymes can continue to degrade casein protein during storage, causing premature gelation and instability.

Adding calcium chloride increases the concentration of free ionic calcium in milk. This promotes the precipitation of colloidal calcium phosphate and the aggregation of casein micelles, which destabilizes the milk's protein structure and lowers its heat stability.

Stabilizing salts such as phosphates and citrates work by sequestering or binding to calcium ions. This helps to maintain the mineral equilibrium, preventing the heat-induced aggregation of casein micelles and improving overall stability.

Yes, high-pressure homogenization can reduce heat stability, especially in concentrated milk. It increases the fat globule surface area, causing milk proteins to adsorb onto these new surfaces, which alters the balance of proteins needed for colloidal stability.

Concentrated milk has a higher protein and mineral content, leading to a greater number of protein-protein interactions and increased viscosity during heat treatment. This higher concentration of interacting particles increases the likelihood of aggregation and reduces heat stability.

References

  1. 1
  2. 2
  3. 3

Medical Disclaimer

This content is for informational purposes only and should not replace professional medical advice.