Abstract:
:Holder pasteurization (62.5 °C, 30 min) of human milk denatures beneficial proteins. The present paper aimed to assess whether this can affect the kinetics of peptide release during digestion at the preterm stage. Raw (RHM) or pasteurized (PHM) human milk were digested in triplicates using an in vitro dynamic system. Mass spectrometry and multivariate statistics were conducted. Pre-proteolysis occurred mostly on β-casein, for which cumulative peptide abundance was significantly greater in PHM over 28% of the hydrolysed sequence. Eight clusters resumed the kinetics of peptide release during digestion, which differed on seven clusters (69% of the 1134 peptides). Clusters associated to the heat-denaturated proteins, lactoferrin and bile salt-stimulated lipase, presented different kinetics of release during digestion, unlike that for β-casein. Some bioactive peptides from β-casein presented significant different abundances between PHM and RHM before digestion (1-18, 185-211) or in during intestinal digestion (154-160, 161-166). Further physiological consequences should be investigated.
journal_name
Food Chemjournal_title
Food chemistryauthors
Deglaire A,Oliveira S,Jardin J,Briard-Bion V,Kroell F,Emily M,Ménard O,Bourlieu C,Dupont Ddoi
10.1016/j.foodchem.2018.12.086subject
Has Abstractpub_date
2019-05-30 00:00:00pages
294-303eissn
0308-8146issn
1873-7072pii
S0308-8146(18)32190-3journal_volume
281pub_type
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