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Peptidomic profiling of human milk with LC–MS/MS reveals pH-specific proteolysis of milk proteins
- Source :
- Food Chemistry. 274:766-774
- Publication Year :
- 2019
- Publisher :
- Elsevier BV, 2019.
-
Abstract
- Human milk is a dynamic protein-protease system that delivers bioactive peptides to infants. The pH of milk changes from the mother’s mammary gland to the infant’s digestive tract. Although the release of human milk peptides has been studied during in vivo or in vitro digestion, these models did not explicitly vary nor observe the effect of pH. The objective of this research was to determine the effect of pH on the proteolysis of human milk. Using high-resolution accurate-mass Orbitrap mass spectrometry, profiles of endogenous human milk peptides before and after incubation at various pH levels have been mapped. Over 5000 peptides were identified. Comparative analyses classified 74 peptides that were consistently found independent of pH alterations, and 8 peptides that were released only at pH 4 or 5 (typical infant gastric pH). Results documented that the proteolysis of milk proteins, particularly β-casein, polymeric immunoglobulin receptor, and α-lactalbumin, is pH-dependent.
- Subjects :
- Proteomics
Protein digestion
Proteolysis
Mammary gland
Endogeny
Orbitrap
01 natural sciences
Article
Analytical Chemistry
law.invention
0404 agricultural biotechnology
Tandem Mass Spectrometry
law
In vivo
medicine
Animals
Humans
Incubation
Milk, Human
medicine.diagnostic_test
Chemistry
010401 analytical chemistry
food and beverages
04 agricultural and veterinary sciences
General Medicine
Hydrogen-Ion Concentration
Milk Proteins
040401 food science
0104 chemical sciences
medicine.anatomical_structure
Biochemistry
Female
Polymeric immunoglobulin receptor
Chromatography, Liquid
Food Science
Subjects
Details
- ISSN :
- 03088146
- Volume :
- 274
- Database :
- OpenAIRE
- Journal :
- Food Chemistry
- Accession number :
- edsair.doi.dedup.....7bf0c425f7cf7c7e36628378dfc14ed1