### Stability of whey protein derived peptides upon severe protein glycation

Tatiana Cucu UGent, Bruno De Meulenaer UGent, Barbara Kerkaert UGent, Isabel Vandenberghe UGent and Bart Devreese UGent (2010) p.47-47
abstract
Cow’s milk and dairy products are major nutrients in the human diet, especially during infancy. Though at one time whey proteins were considered as by-product of the cheese making process, nowadays, due to their wide ranging nutritional, biological, and functional properties, whey proteins are often used in food technology as low-cost protein ingredients. However, whey-protein fractions, such as β-lactoglobulin (β-LG) and α-lactalbumin (α-LA) represent the major allergens in cow’s milk. Therefore, the use of whey proteins in food might pose a serious threat to the milk allergic consumers. It is well reported that food processing may modify the allergenicity and detectability of proteins. This can be due to hydrolysis or chemical reactions with other food components (carbohydrates, fatty acids etc), leading to modification or destruction of the allergen’s structure. Therefore, the objective of this study was in the first stage to investigate the influence of glycation on the molecular changes induced in whey proteins. This was done with a special focus on the modifications induced on the lysine residues, free amino groups, the formation of protein bound carbonyls, formation of fluorescent compounds and brown polymers and on the protein aggregation. Matrix-assisted laser desorption/ionization - time of flight mass spectrometry (MALDI-TOF MS) was used to get a better insight into the molecular changes that took place on the protein level. Unexpectedly, this study led to the identification of protein segments in the epitope region that remained unmodified during the experiments that mimic typical food processing conditions. The 57Val – Lys76 and 31Val – Arg56 from β–LG, remained unchanged disregarding the severe heating treatment in the presence of glucose and bulk proteins and they could be identified by either direct MALDI-TOF MS and MS/MS or after a more tedious separation using reversed phase chromatography. It is proposed that these peptide segments can be used as analytical targets for the development of more robust methods for the assessment of the presence of whey proteins in processed foodstuffs. Moreover, MALDI-TOF MS and MS/MS holds potential to be used as a screening tool for the identification of such stable peptides.
author
organization
year
type
conference
publication status
published
subject
keyword
Maillard reaction, MALDI-TOF MS and MS/MS, stable peptides, food allergens, whey proteins
in
Exchange : open innovation for feed, food and health, where industry and academia meet
pages
47 - 47
publisher
Food2Know ; Ghent BC
conference name
Exchange : open innovation for feed, food and health, where industry and academia meet
conference location
Ghent, Belgium
conference start
2010-09-28
conference end
2010-09-28
language
English
UGent publication?
yes
classification
C3
I have retained and own the full copyright for this publication
id
1175825
handle
http://hdl.handle.net/1854/LU-1175825
date created
2011-02-28 14:28:48
date last changed
2011-04-06 10:03:51
@inproceedings{1175825,
abstract     = {Cow{\textquoteright}s milk and dairy products are major nutrients in the human diet, especially during infancy. Though at one time whey proteins were considered as by-product of the cheese making process, nowadays, due to their wide ranging nutritional, biological, and functional properties, whey proteins are often used in food technology as low-cost protein ingredients. However, whey-protein fractions, such as \ensuremath{\beta}-lactoglobulin (\ensuremath{\beta}-LG) and \ensuremath{\alpha}-lactalbumin (\ensuremath{\alpha}-LA) represent the major allergens in cow{\textquoteright}s milk. Therefore, the use of whey proteins in food might pose a serious threat to the milk allergic consumers. It is well reported that food processing may modify the allergenicity and detectability of proteins. This can be due to hydrolysis or chemical reactions with other food components (carbohydrates, fatty acids etc), leading to modification or destruction of the allergen{\textquoteright}s structure. Therefore, the objective of this study was in the first stage to investigate the influence of glycation on the molecular changes induced in whey proteins. This was done with a special focus on the modifications induced on the lysine residues, free amino groups, the formation of protein bound carbonyls, formation of fluorescent compounds and brown polymers and on the protein aggregation. Matrix-assisted laser desorption/ionization - time of flight mass spectrometry (MALDI-TOF MS) was used to get a better insight into the molecular changes that took place on the protein level. Unexpectedly, this study led to the identification of protein segments in the epitope region that remained unmodified during the experiments that mimic typical food processing conditions. The 57Val -- Lys76 and 31Val -- Arg56 from \ensuremath{\beta}--LG, remained unchanged disregarding the severe heating treatment in the presence of glucose and bulk proteins and they could be  identified by either direct MALDI-TOF MS and MS/MS or after a more tedious separation using reversed phase chromatography. It is proposed that these peptide segments can be used as analytical targets for the development of more robust methods for the assessment of the presence of whey proteins in processed foodstuffs. Moreover, MALDI-TOF MS and MS/MS holds potential to be used as a screening tool for the identification of such stable peptides.},
author       = {Cucu, Tatiana and De Meulenaer, Bruno and Kerkaert, Barbara and Vandenberghe, Isabel and Devreese, Bart},
booktitle    = {Exchange : open innovation for feed, food and health, where industry and academia meet},
keyword      = {Maillard reaction,MALDI-TOF MS and MS/MS,stable peptides,food allergens,whey proteins},
language     = {eng},
location     = {Ghent, Belgium},
pages        = {47--47},
publisher    = {Food2Know ; Ghent BC},
title        = {Stability of whey protein derived peptides upon severe protein glycation},
year         = {2010},
}


Chicago
Cucu, Tatiana, Bruno De Meulenaer, Barbara Kerkaert, Isabel Vandenberghe, and Bart Devreese. 2010. “Stability of Whey Protein Derived Peptides Upon Severe Protein Glycation.” In Exchange : Open Innovation for Feed, Food and Health, Where Industry and Academia Meet, 47–47. Food2Know ; Ghent BC.
APA
Cucu, T., De Meulenaer, B., Kerkaert, B., Vandenberghe, I., & Devreese, B. (2010). Stability of whey protein derived peptides upon severe protein glycation. Exchange : open innovation for feed, food and health, where industry and academia meet (pp. 47–47). Presented at the Exchange : open innovation for feed, food and health, where industry and academia meet, Food2Know ; Ghent BC.
Vancouver
1.
Cucu T, De Meulenaer B, Kerkaert B, Vandenberghe I, Devreese B. Stability of whey protein derived peptides upon severe protein glycation. Exchange : open innovation for feed, food and health, where industry and academia meet. Food2Know ; Ghent BC; 2010. p. 47–47.
MLA
Cucu, Tatiana, Bruno De Meulenaer, Barbara Kerkaert, et al. “Stability of Whey Protein Derived Peptides Upon Severe Protein Glycation.” Exchange : Open Innovation for Feed, Food and Health, Where Industry and Academia Meet. Food2Know ; Ghent BC, 2010. 47–47. Print.