Peptidomic profiling of human milk with LC-MS/MS reveals pH-specific proteolysis of milk proteins.

Autor: Gan J; Department of Food Science and Technology, University of California Davis, USA. Electronic address: jagan@ucdavis.edu., Robinson RC; Department of Food Science and Technology, University of California Davis, USA. Electronic address: rcrobinson@ucdavis.edu., Wang J; Department of Food Science and Technology, University of California Davis, USA. Electronic address: jqqwang@ucdavis.edu., Krishnakumar N; Department of Food Science and Technology, University of California Davis, USA. Electronic address: nkumar@ucdavis.edu., Manning CJ; Department of Chemistry, University of California Davis, USA. Electronic address: cjmanning@ucdavis.edu., Lor Y; College of Biological Sciences, University of California Davis, USA. Electronic address: yijlor@ucdavis.edu., Breck M; Department of Food Science and Technology, University of California Davis, USA; Foods for Health Institute, University of California Davis, USA. Electronic address: mabreck@ucdavis.edu., Barile D; Department of Food Science and Technology, University of California Davis, USA; Foods for Health Institute, University of California Davis, USA. Electronic address: dbarile@ucdavis.edu., German JB; Department of Food Science and Technology, University of California Davis, USA; Foods for Health Institute, University of California Davis, USA. Electronic address: jbgerman@ucdavis.edu.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2019 Feb 15; Vol. 274, pp. 766-774. Date of Electronic Publication: 2018 Sep 10.
DOI: 10.1016/j.foodchem.2018.09.051
Abstrakt: 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.
(Copyright © 2018 Elsevier Ltd. All rights reserved.)
Databáze: MEDLINE
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