期刊
JOURNAL OF PROTEOME RESEARCH
卷 12, 期 12, 页码 5447-5462出版社
AMER CHEMICAL SOC
DOI: 10.1021/pr4003273
关键词
peptide profiling; bioactive peptides: milk; MALDI-TOF-MS; ESI-MS: caseins; OFFGEL fractionation; HPLC prefractionation; plasmin; cathepsin
资金
- Bavarian Research and Innovation Network
- European Regional Development Fund (ERFD, European Union and Free State Saxony)
- Federal Ministry of Education and Research (BMBF)
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 alpha(S1)-casein, followed by beta-casein, and alpha(S2)-casein. kappa-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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