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The impact of photo-induced molecular changes of dairy proteins on their ACE-inhibitory peptides and activity

Barbara Kerkaert UGent, Frédéric Mestdagh UGent, Tatiana Cucu UGent, Kshitij Shrestha UGent, John Van Camp UGent and Bruno De Meulenaer UGent (2012) AMINO ACIDS. 43(2). p.951-962
abstract
Among all dietary proteins, dairy proteins are the most important source of bio-active peptides which can, however, be affected by modifications upon processing and storage. Since it is still unknown to which extent the biological activity of dairy proteins is altered by chemical reactions, this study focuses on the effect of photo-induced molecular changes on the angiotensin I converting enzyme (ACE) inhibitory activity. Milk proteins were dissolved in phosphate buffer containing riboflavin and stored under light at 4A degrees C for one month during which the molecular changes and the ACE-inhibitory activity were analysed. An increase in the total protein carbonyls and the N-formylkynurenine content was observed, besides a decrease in the free thiol, tryptophan, tyrosine and histidine content. These changes were more severe in caseins compared with whey proteins and resulted moreover in the aggregation of caseins. Due to these photo-induced molecular changes, a significant loss of the ACE-inhibitory activity was observed for casein peptides. A peptide analysis moreover illustrated that the decreased activity was not attributed to a reduced digestibility but to losses of specific ACE-inhibitory peptides. The observed molecular changes, more specifically the degradation of specific amino acids and the casein aggregation, could be assigned as the cause of the altered peptide pattern and as such of the loss in ACE-inhibitory activity.
Please use this url to cite or link to this publication:
author
organization
year
type
journalArticle (original)
publication status
published
subject
keyword
ACE-inhibitory peptides, MILK-PROTEINS, LC–TOF–MS, ACE-inhibitory activity, Photo-oxidation, Milk proteins, BETA-LACTOGLOBULIN, ENZYME, PHOTOOXIDATION, RIBOFLAVIN, HYDROLYSIS, TRYPTOPHAN, DIGESTION, OXIDATION, FOODS
journal title
AMINO ACIDS
Amino Acids
volume
43
issue
2
pages
951 - 962
Web of Science type
Article
Web of Science id
000306365500040
JCR category
BIOCHEMISTRY & MOLECULAR BIOLOGY
JCR impact factor
3.914 (2012)
JCR rank
86/288 (2012)
JCR quartile
2 (2012)
ISSN
0939-4451
DOI
10.1007/s00726-011-1157-y
language
English
UGent publication?
yes
classification
A1
copyright statement
I have transferred the copyright for this publication to the publisher
id
1992304
handle
http://hdl.handle.net/1854/LU-1992304
date created
2012-01-18 11:00:49
date last changed
2012-09-26 16:47:19
@article{1992304,
  abstract     = {Among all dietary proteins, dairy proteins are the most important source of bio-active peptides which can, however, be affected by modifications upon processing and storage. Since it is still unknown to which extent the biological activity of dairy proteins is altered by chemical reactions, this study focuses on the effect of photo-induced molecular changes on the angiotensin I converting enzyme (ACE) inhibitory activity. Milk proteins were dissolved in phosphate buffer containing riboflavin and stored under light at 4A degrees C for one month during which the molecular changes and the ACE-inhibitory activity were analysed. An increase in the total protein carbonyls and the N-formylkynurenine content was observed, besides a decrease in the free thiol, tryptophan, tyrosine and histidine content. These changes were more severe in caseins compared with whey proteins and resulted moreover in the aggregation of caseins. Due to these photo-induced molecular changes, a significant loss of the ACE-inhibitory activity was observed for casein peptides. A peptide analysis moreover illustrated that the decreased activity was not attributed to a reduced digestibility but to losses of specific ACE-inhibitory peptides. The observed molecular changes, more specifically the degradation of specific amino acids and the casein aggregation, could be assigned as the cause of the altered peptide pattern and as such of the loss in ACE-inhibitory activity.},
  author       = {Kerkaert, Barbara and Mestdagh, Fr{\'e}d{\'e}ric and Cucu, Tatiana and Shrestha, Kshitij and Van Camp, John and De Meulenaer, Bruno},
  issn         = {0939-4451},
  journal      = {AMINO ACIDS},
  keyword      = {ACE-inhibitory peptides,MILK-PROTEINS,LC--TOF--MS,ACE-inhibitory activity,Photo-oxidation,Milk proteins,BETA-LACTOGLOBULIN,ENZYME,PHOTOOXIDATION,RIBOFLAVIN,HYDROLYSIS,TRYPTOPHAN,DIGESTION,OXIDATION,FOODS},
  language     = {eng},
  number       = {2},
  pages        = {951--962},
  title        = {The impact of photo-induced molecular changes of dairy proteins on their ACE-inhibitory peptides and activity},
  url          = {http://dx.doi.org/10.1007/s00726-011-1157-y},
  volume       = {43},
  year         = {2012},
}

Chicago
Kerkaert, Barbara, Frédéric Mestdagh, Tatiana Cucu, Kshitij Shrestha, John Van Camp, and Bruno De Meulenaer. 2012. “The Impact of Photo-induced Molecular Changes of Dairy Proteins on Their ACE-inhibitory Peptides and Activity.” Amino Acids 43 (2): 951–962.
APA
Kerkaert, B., Mestdagh, F., Cucu, T., Shrestha, K., Van Camp, J., & De Meulenaer, B. (2012). The impact of photo-induced molecular changes of dairy proteins on their ACE-inhibitory peptides and activity. AMINO ACIDS, 43(2), 951–962.
Vancouver
1.
Kerkaert B, Mestdagh F, Cucu T, Shrestha K, Van Camp J, De Meulenaer B. The impact of photo-induced molecular changes of dairy proteins on their ACE-inhibitory peptides and activity. AMINO ACIDS. 2012;43(2):951–62.
MLA
Kerkaert, Barbara, Frédéric Mestdagh, Tatiana Cucu, et al. “The Impact of Photo-induced Molecular Changes of Dairy Proteins on Their ACE-inhibitory Peptides and Activity.” AMINO ACIDS 43.2 (2012): 951–962. Print.