Open AccessHuman milk provides peptides highly stimulating the growth of bifidobacteria
Author(s) -
Liepke Cornelia,
Adermann Knut,
Raida Manfred,
Mägert HansJürgen,
Forssmann WolfGeorg,
Zucht HansDieter
Publication year - 2002
Publication title -
european journal of biochemistry
Language(s) - English
Resource type - Journals
eISSN - 1432-1033
pISSN - 0014-2956
DOI - 10.1046/j.0014-2956.2001.02712.x
Subject(s) - lactoferrin , pepsin , chymotrypsin , trypsin , peptide , proteases , biochemistry , bifidobacterium , biology , prebiotic , antimicrobial peptides , chemistry , microbiology and biotechnology , enzyme , lactobacillus , fermentation
The large intestine of breast‐fed infants is colonized predominantly by bifidobacteria, which have a protective effect against acute diarrhea. In this study we report for the first time the identification of human milk peptides that selectively stimulate the growth of bifidobacteria. Several bifidogenic peptides were purified chromatographically from pepsin‐treated human milk and identified as proteolytically generated fragments from the secretory component of the soluble polyimmunoglobulin receptor and lactoferrin; both of these proteins exhibit antimicrobial effects. Hydrolysis of the identified peptides with the gastrointestinal proteases pepsin, trypsin and chymotrypsin did not lead to the loss of bifidogenic activity, indicating their potential function in vivo . Sequential comparison revealed a similar structural motif within the identified peptides. A correspondingly designed small peptide (prebiotic lactoferrin‐derived peptide‐I, PRELP‐I) was found to stimulate the growth of bifidobacteria as effectively as the native peptides. The combination of antimicrobial and bifidobacterial growth stimulatory activity in human milk proteins leads to highly specific compounds capable of regulating the microbial composition of infants' large intestine.