Natural Association of Lysozyme and Casein Micelles in Human Milk

Research output: Contribution to journalResearch articleContributedpeer-review

Contributors

  • Mathias Jaeser - , TUD Dresden University of Technology (Author)
  • Ulrike Moeckel - , TUD Dresden University of Technology (Author)
  • Kati Weigel - , TUD Dresden University of Technology (Author)
  • Thomas Henle - , Chair of Food Chemistry, TUD Dresden University of Technology (Author)

Abstract

Using reversed phase high-performance liquid chromatography with ultraviolet (UV) detection and electrospray ionization (ESI)-quadrupole time-of-flight mass spectrometry (RP-HPLC-UV-ESI-Q-TOF), the lysozyme content in the milk of 10 volunteering mothers was quantified, ranging from 29 to 96 μg/mL. Following ultracentifugation, it was found that the lysozyme in human milk, unlike other whey proteins, is mainly bound to casein micelles (ca. 75%). The enzymatic activity of human lysozyme, measured as lytic activity against cell walls of Micrococcus lysodeikticus, was similar for the micelle-bound and free protein, indicating that the micellar structure should not affect the antibacterial activity of lysozyme. The results indicate that lysozyme is an integral component of casein micelles in human milk.

Details

Original languageEnglish
Pages (from-to)1652-1658
Number of pages7
JournalJournal of agricultural and food chemistry
Volume70
Issue number5
Publication statusPublished - 9 Feb 2022
Peer-reviewedYes

External IDs

Scopus 85124437378
Mendeley 47af1ed9-2208-3315-aede-d0873d631a19

Keywords

Keywords

  • lysozyme, lysozyme activity, casein, casein micelle, human milk, nanoparticle tracking analysis, BETA-CASEIN, ALPHA-LACTALBUMIN, BREAST-MILK, LACTOFERRIN, PROTEINS, QUANTIFICATION, DISSOCIATION, PH