Evidence map›Paper›PMID 23315725›Full record

ArticleApplied and environmental microbiology2013

Isolation of a bifidogenic peptide from the pepsin hydrolysate of bovine lactoferrin.

Hirotsugu Oda, Hiroyuki Wakabayashi, Koji Yamauchi, Takumi Sato, Jin-Zhong Xiao, Fumiaki Abe, Keiji Iwatsuki

Open access · bronzeAbstract read
In one paragraph

Article in Applied and environmental microbiology, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 22 papers.

0numbers the graph read from it
0cells of the map it votes in
22citing papers in PubMed
3.0field-weighted citation impact, top 9% of its field
1 · What the graph read from it

What it found

Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.

The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.

2 · The registry

The trial behind it

Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.

Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.

3 · Its place in the literature

Who cites it

22 citing papers in PubMed, 50 citations in OpenAlex.

  1. Trial
  2. Trial
  3. Review
  4. Lactoferrin: Properties and Potential Uses in the Food Industry.International journal of molecular sciences · 2025
    Review
  5. Review
  6. Lactoferrin and its digestive peptides induce interferon-α production and activate plasmacytoid dendritic cells ex vivo.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Article
  7. Clinical research review: usefulness of bovine lactoferrin in child health.Biometals : an international journal on the role of metal ions in biology, biochemistry, and medicine · 2023
    Review
  8. Article
  9. Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. The Impact of Lactoferrin on the Growth of Intestinal Inhabitant Bacteria.International journal of molecular sciences · 2019
    Review
  15. Milk Glycans and Their Interaction with the Infant-Gut Microbiota.Annual review of food science and technology · 2018
    Review
  16. Article
  17. Article
  18. Article
  19. Review
  20. The impact of the milk glycobiome on the neonate gut microbiota.Annual review of animal biosciences · 2015
    Review
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

7 authors.

Hirotsugu OdaFood Science and Technology Institute, Morinaga Milk Industry Company, Ltd., Zama City, Kanagawa Prefecture, Japan. h-oda@morinagamilk.co.jp
Hiroyuki Wakabayashi
Koji Yamauchi
Takumi Sato
Jin-Zhong Xiao
Fumiaki Abe
Keiji Iwatsuki

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lactoferrin is an iron-binding glycoprotein found in the milk of most mammals for which various biological functions have been reported, such as antimicrobial activity and bifidogenic activity. In this study, we compared the bifidogenic activity of bovine lactoferrin (bLF) and pepsin hydrolysate of bLF (bLFH), isolated bifidogenic peptide from bLFH, and investigated the bifidogenic spectra of bLF, bLFH, and its active peptide against 42 bifidobacterial strains comprising nine species. Against Bifidobacterium breve ATCC 15700(T), minimal effective concentrations of bLF and bLFH were 300 and 10 μg/ml. Against Bifidobacterium longum subsp. infantis ATCC 15697(T), the minimal effective concentration of bLFH was 30 μg/ml, and bLF did not show bifidogenic activity within 300 μg/ml. As an active peptide, a heterodimer of A(1)-W(16) and L(43)-A(48) linked by a disulfide bond was isolated. Previously, this peptide was identified as having antibacterial activity. An amino acid mixture with the same composition as this peptide showed no bifidogenic activity. The strains of each species whose growth was highly promoted (>150%) by this peptide at 3.75 μM were as follows: B. breve (7 out of 7 strains [7/7]), B. longum subsp. infantis (5/5), Bifidobacterium bifidum (2/5), B. longum subsp. longum (1/3), Bifidobacterium adolescentis (3/6), Bifidobacterium catenulatum (1/4), Bifidobacterium pseudocatenulatum (0/4), Bifidobacterium dentium (0/5), and Bifidobacterium angulatum (0/3). Growth of none of the strains was highly promoted by bLF at 3.75 μM. We demonstrated that bLFH showed stronger bifidogenic activity than natural bLF, especially against infant-representative species, B. breve and B. longum subsp. infantis; furthermore, we isolated its active peptide. This is the first report about a bifidogenic peptide derived from bLF.

Indexed as

AnimalsBifidobacteriumCattleGrowth InhibitorsHydrolysisIntercellular Signaling Peptides and ProteinsLactoferrinMicrobial Sensitivity TestsPepsin AGrowth InhibitorsIntercellular Signaling Peptides and ProteinsLactoferrinPepsin A

Identifiers

PMID23315725
PMCPMC3592234
OpenAlexW2154708032

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.