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Cited by 92

The DOI matches its Crossref record; 61 of the 61 references it cites were found in a registry or an index.

Analysis of the Endogenous Peptide Profile of Milk: Identification of 248 Mainly Casein-Derived Peptides

Baum, Florian, Fedorova, Maria, Ebner, Jennifer, Hoffmann, Ralf, Pischetsrieder, Monika·2013·Journal of Proteome Research
DOI 10.1021/pr4003273
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Abstract

Milk is an excellent source of bioactive peptides. However, the composition of the native milk peptidome has only been partially elucidated. The present study applied matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) directly or after prefractionation of the milk peptides by reverse-phase high-performance liquid chromatography (RP-HPLC) or OFFGEL fractionation for the comprehensive analysis of the peptide profile of raw milk. The peptide sequences were determined by MALDI-TOF/TOF or nano-ultra-performance liquid chromatography-nanoelectrospray ionization-LTQ-Orbitrap-MS. Direct MALDI-TOF-MS analysis led to the assignment of 57 peptides. Prefractionation by both complementary methods led to the assignment of another 191 peptides. Most peptides originate from α(S1)-casein, followed by β-casein, and α(S2)-casein. κ-Casein and whey proteins seem to play only a minor role as peptide precursors. The formation of many, but not all, peptides could be explained by the activity of the endogenous peptidases, plasmin or cathepsin D, B, and G. Database searches revealed the presence of 22 peptides with established physiological function, including those with angiotensin-converting-enzyme (ACE) inhibitory, immunomodulating, or antimicrobial activity.

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Crossref · 10.1021/pr4003273

Cites

61 of 61 references verified0 citation errors · 0 not checkable

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Citations

Cites

Research works printed but not linked: 13

  1. Leszyk J. D., 2010, J. Biomol. Tech., 21, 81
  2. Kato H., 1980, J. Biochem., 88, 183
  3. Visser S., 1989, Milchwissenschaft, 44, 335
  4. Belitz H. D., 2009, Food Chem.
  5. Maruyama S., 1982, Agric. Biol. Chem., 46, 1393
  6. Shinoda I., 1985, Agric. Biol. Chem., 49, 2587
  7. Tamamura M., 1990, Agric. Biol. Chem., 54, 1401
  8. Sullivan J. J., 1971, Aust. J. Dairy Tech., 26, 111
  9. Visser S., 1975, Neth. Milk Dairy J., 29, 319
  10. Visser S., 1983, Neth. Milk Dairy J., 37, 250
  11. Visser S., 1983, Neth. Milk Dairy J., 37, 181
  12. Gupta A., 2010, Milchwissenschaft, 65, 396
  13. Matoba T., 1969, Agric. Biol. Chem., 33, 1662, 10.1080/00021369.1969.10859521 · doi:10.1080/00021369.1969.10859521

Cited by

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Metadata

Authors
Baum, F., Fedorova, M., Ebner, J., Hoffmann, R., & Pischetsrieder, M.
Affiliations
  • Department of Chemistry and Pharmacy, Food Chemistry, Emil Fischer Center, University of Erlangen-Nuremberg, Schuhstrasse 19, 91052 Erlangen, Germany
  • Center for Biotechnology and Biomedicine, Universität Leipzig, Deutscher Platz 5, 04103 Leipzig, Germany
Venue
Journal of Proteome Research
Publisher
American Chemical Society (ACS)
Published
2013-11-22
Volume
12
Issue
12
Pages
5447-5462
ISSN
  • 1535-3893
  • 1535-3907
DOI
10.1021/pr4003273
Cited by
92
References
61
Language
en

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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.