Heat-Induced Redistribution of Disulfide Bonds in Milk Proteins. 1. Bovine beta-Lactoglobulin
(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)
Please use this url to cite or link to this publication:
https://lup.lub.lu.se/record/141705
- author
- 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
- organization
- publishing date
- 2004
- 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 (ACS)
- 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
- 2016-04-01 12:22:20
- date last changed
- 2023-11-11 22:27:13
@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 (ACS)}},
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}},
doi = {{10.1021/jf049388y}},
volume = {{52}},
year = {{2004}},
}