Natural Association of Lysozyme and Casein Micelles in Human Milk.
Mathias JaeserUlrike MoeckelKati WeigelThomas HenlePublished in: Journal of agricultural and food chemistry (2022)
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.
Keyphrases
- human milk
- high performance liquid chromatography
- ms ms
- low birth weight
- mass spectrometry
- drug delivery
- tandem mass spectrometry
- simultaneous determination
- preterm infants
- solid phase extraction
- cancer therapy
- drug release
- endothelial cells
- preterm birth
- single cell
- hyaluronic acid
- gas chromatography
- stem cells
- hydrogen peroxide
- loop mediated isothermal amplification