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Milk proteins: molecular, colloidal and functional properties

Published online by Cambridge University Press:  01 June 2009

Patrick F. Fox  and
Daniel M. Mulvihill
Patrick F. Fox
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic
Daniel M. Mulvihill
Affiliation:
Department of Dairy and Food Chemistry, University College, Cork, Irish Republic
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Summary

The proteins of bovine milk are the best-characterized food-protein system. Lactoproteins, which have high biological value, contribute ∼25% of dietary protein in North West Europe, North America and Oceania. However, in protein-rich western diets, milk proteins are frequently more highly valued for their functional properties than for their nutritional qualities. The remarkably high heat stability of the caseinate system permits the manufacture of a range of sterilized, concentrated and dehydrated products while its gelation on very limited proteolysis is the basis of cheese manufacture. Skim-milk powders, caseinates and whey protein concentrates are the most flexible and widely used functional proteins in food processing.

This communication reviews recent studies on milk proteins with respect to molecular and colloidal properties; coagulation by Ca2+, heat and ethanol; and functional properties and their chemical and enzymic modification.

Type
Short Communication
Information
Journal of Dairy Research , Volume 49 , Issue 4 , November 1982 , pp. 679 - 693
Copyright
Copyright © Proprietors of Journal of Dairy Research 1982

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