Heat induced crosslinks in milk proteins and consequences for the milk system.
The protein system of milk is rather unusual, there are nearly no interchain crosslinks found. Even intrachain crosslinks, especially disulfide bridges, are present only in about every fourth protein molecule. Heating causes dramatic changes in the structure of milk proteins, resulting in the formation of polymeric networks. The contribution of individual milk proteins, namely the beta-lactoglobulins, alpha-lactalbumin and chi-casein, to the formation of crosslinks is studied with respect to heating temperature and time, pH and atmosphere. Measured are changes in molecular weights and in the SH/SS-levels as well as the formation of dehydroalanine, lysinoalanine, lanthionine and isopeptide bonds. Some practical aspects of crosslinking in milk proteins are discussed.
D000818:Animals; D002364:Caseins; D002417:Cattle; D005033:Ethylmaleimide; D005260:Female; D006020:Glycopeptides; D006358:Hot Temperature; D007768:Lactalbumin; D007782:Lactoglobulins; D008894:Milk Proteins
D002364:Caseins; D006020:Glycopeptides; D007782:Lactoglobulins; D008894:Milk Proteins; D007768:Lactalbumin; D005033:Ethylmaleimide