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Zinc binding in bovine milk.

H Singh¹, A Flynn, P F Fox

¹Department of Food Chemistry, University College, Cork, Irish Republic.

The Journal of Dairy Research

|May 1, 1989

Summary

Zinc in bovine skim milk primarily binds to casein micelles and colloidal calcium phosphate (CCP). Understanding this zinc binding is crucial for improving the nutritional bioavailability of zinc in dairy products.

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Area of Science:

Dairy Science
Biochemistry
Nutritional Science

Background:

Zinc is an essential mineral with varying bioavailability in different milk sources.
Understanding the interaction of zinc with milk components is key to improving its nutritional value.

Purpose of the Study:

To investigate the binding forms and locations of zinc within bovine skim milk.
To elucidate the relationship between zinc, casein micelles, and colloidal calcium phosphate (CCP).

Main Methods:

Ultracentrifugation to separate sedimentable and non-sedimentable zinc fractions.
Dialysis and EDTA treatments to assess zinc solubility and binding.
pH manipulation to study the stability of zinc-protein and zinc-mineral complexes.

Main Results:

Approximately 90% of zinc in skim milk is associated with sedimentable fractions, primarily casein micelles and CCP.
Zinc binding to casein micelles is concentration-dependent, leading to micelle coagulation at higher concentrations.
Approximately 32% of zinc is directly bound to caseins, while about 63% is associated with CCP.

Conclusions:

Bovine skim milk contains distinct zinc fractions bound to casein micelles and CCP.
The binding of zinc to CCP is more stable than its binding to caseins.
These binding characteristics may contribute to the lower nutritional bioavailability of zinc in bovine milk compared to human milk.

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