Changes in Casein and Egg Albumin due to Reactions with Oxidizing Methyl Linoleate in Dehydrated Systems

Protein–lipid interactions during the incubation of whey proteins with autoxidizing lipids

“…Therefore, a more detailed analysis of the specific molecular changes on amino acid level was performed. Changes in amino acid composition of proteins as a result of their interaction with fatty acids or secondary oxidation products have been reported (Matoba et al, 1982;Sanchez-Vioque et al, 1999;Zamora & Hidalgo, 2003). Due to their structure, tryptophan, histidine, and proline, but also lysine, cysteine, methionine, and tyrosine are reported to be mostly prone to oxidation.…”

“…Most of the studies of interactions between oxidizing lipids and proteins have been carried out between a model lipid, mostly linoleic acid or its peroxides, and model proteins, usually lysozyme, casein or bovine serum albumin (Hidalgo & Kinsella, 1989;Kanner & Karel, 1976;Matoba, Yoshida, & Yonezawa, 1982;Zamora & Hidalgo, 2003). The objective of this study was to characterize changes induced in a more complex whey protein isolate (a mixture of primarily a-lactalbumin and b-lactoglobulin) through interaction with autoxidizing lipids.…”

Changes in Molecular Size and Chemical Properties of Gelatin Caused by the Reaction with Oxidizing Methyl Linoleate

“…However, we fouhd an insignificant decrease in the molecular size of casein and egg albumin after the reaction at RH 0%, although significant fragmentation of gelatin was detected. 5 ) There has been some information concerning the cross-linking (polymerization) and insolubilization of proteins caused by reaction with oxidizing lipids. In general, it is known that the polymerization increases with increasing water.…”