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Heat-Induced Redistribution of Disulfide Bonds in Milk Proteins. 1. Bovine beta-Lactoglobulin

By Lawrence K Creamer, Annie Bienvenue, Hanna Nilsson, Marie Paulsson, Miriam van Wanroij, Edwin K Lowe, Skelte G Anema, Michael J Boland and Rafael Jiménez-Flores

Abstract

Changes in the structure and chemistry of -lactoglobulin (-LG) play an important role in the processing and functionality of milk products. In model -LG systems, there is evidence that the aggregates of heated -LG are held together by a mixture of intermolecular non-covalent association and heat-induced non-native disulfide bonds. Although a number of non-native disulfide bonds have been identified, little is known about the initial inter- and intramolecular disulfide bond rearrangements that occur as a result of heating. These interchange reactions were explored by examining the products of heat treatment to determine the novel disulfide bonds that form in the heated -LG aggregates. The native protein and heat-induced aggregates were hydrolyzed by trypsin, and the resulting peptides, before and after reduction with dithiothreitol, were separated by high-performance liquid chromatography and their identities confirmed by electrospray ionization mass spectrometry. Comparisons of these peptide patterns showed that some of the Cys160 was in the reduced form in heated -LG aggregates, indicating that the Cys160-Cys66 disulfide bond had been broken during heating. This finding suggests that disulfide bond interchange reactions between -LG non-native monomers, or polymers, and other proteins could occur largely via Cys160

Topics: Agricultural Science, Forestry and Fisheries
Publisher: 'American Chemical Society (ACS)'
Year: 2004
DOI identifier: 10.1021/jf049388y
OAI identifier: oai:lup.lub.lu.se:fb53450d-a255-4fc0-98f7-0f0b4b10b190
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