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

Creamer, Lawrence K; Bienvenue, Annie; Nilsson, Hanna; Paulsson, Marie LU ; van Wanroij, Miriam; Lowe, Edwin K; Anema, Skelte G; Boland, Michael J and Jiménez-Flores, Rafael (2004) In Journal of Agricultural and Food Chemistry 52(25). p.7660-7668
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... (More)
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. (Less)
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author
organization
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type
Contribution to journal
publication status
published
subject
in
Journal of Agricultural and Food Chemistry
volume
52
issue
25
pages
7660 - 7668
publisher
The American Chemical Society
external identifiers
  • wos:000225742500034
  • pmid:15675818
  • scopus:10644243447
ISSN
0021-8561
DOI
10.1021/jf049388y
language
English
LU publication?
yes
id
fb53450d-a255-4fc0-98f7-0f0b4b10b190 (old id 141705)
date added to LUP
2007-07-18 13:35:47
date last changed
2017-10-22 03:51:51
@article{fb53450d-a255-4fc0-98f7-0f0b4b10b190,
  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.},
  author       = {Creamer, Lawrence K and Bienvenue, Annie and Nilsson, Hanna and Paulsson, Marie and van Wanroij, Miriam and Lowe, Edwin K and Anema, Skelte G and Boland, Michael J and Jiménez-Flores, Rafael},
  issn         = {0021-8561},
  language     = {eng},
  number       = {25},
  pages        = {7660--7668},
  publisher    = {The American Chemical Society},
  series       = {Journal of Agricultural and Food Chemistry},
  title        = {Heat-Induced Redistribution of Disulfide Bonds in Milk Proteins. 1. Bovine beta-Lactoglobulin},
  url          = {http://dx.doi.org/10.1021/jf049388y},
  volume       = {52},
  year         = {2004},
}