2022
DOI: 10.1021/acs.jafc.1c07192
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Natural Association of Lysozyme and Casein Micelles in Human Milk

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 activi… Show more

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Cited by 7 publications
(4 citation statements)
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“…As shown in Supplementary Table 1 , lysozyme (P61626), the main whey protein, was also detected in the casein fraction. As indicated in a recent study, approximately 75% of lysozyme in human milk is naturally bound to casein, and this association does not affect the antibacterial activity of lysozyme ( 7 ).…”
Section: Resultsmentioning
confidence: 85%
See 1 more Smart Citation
“…As shown in Supplementary Table 1 , lysozyme (P61626), the main whey protein, was also detected in the casein fraction. As indicated in a recent study, approximately 75% of lysozyme in human milk is naturally bound to casein, and this association does not affect the antibacterial activity of lysozyme ( 7 ).…”
Section: Resultsmentioning
confidence: 85%
“…Casein content in milk depends on the lactation period—it is approximately 20% in the early stage and 45% in the late phase ( 6 ). Caseins in milk mainly exist in the form of micelles with an average size of 40–100 nm ( 7 ). Caseins have been shown to have multiple biological functions in newborn babies, especially in transporting calcium phosphate from the mother to the infants.…”
Section: Introductionmentioning
confidence: 99%
“…The most abundant soluble or whey proteins in human milk are alpha-lactalbumin (~3.3 g/L), lactoferrin (~2.0 g/L), sIgA (~1.0 g/L), lysozyme (29 to 96 µg/ml; Jaeser et al, 2022 ), bile salt stimulated lipase, and serum albumin (0.4 g/L). There are many others most of whose functions in milk are not currently clear ( Smilowitz et al, 2023 ).…”
Section: Properties Of Human Milkmentioning
confidence: 99%
“…β-casein is highly phosphorylated and about half the molecular weight of human casein is due to its heavy glycosylation ~50% vs. 10% in the bovine ( Lonnerdal and Atkinson, 1995 ). The casein micelle binds about 75% of the lysozyme in human milk ( Jaeser et al, 2022 ); however, the activity of the bound lysozyme was not different from that of the free lysozyme.…”
Section: Properties Of Human Milkmentioning
confidence: 99%