Lactoferricin: A Broad-Spectrum Antimicrobial Peptide From Milk That Works Better in Acid
Lactoferricin B showed broad-spectrum bactericidal activity at low concentrations, enhanced at lower pH and against actively growing bacteria.
Quick Facts
What This Study Found
Lactoferricin B showed broad-spectrum bactericidal activity at low concentrations, with enhanced effectiveness at lower pH and against actively growing bacteria.
Key Numbers
How They Did This
Researchers determined minimum inhibitory and bactericidal concentrations of purified lactoferricin B against multiple bacterial species. They tested effects of growth phase, inoculum size, pH, and ionic strength.
Why This Research Matters
With antibiotic resistance growing, natural antimicrobial peptides from food sources like milk offer promising alternatives. Lactoferricin B is especially interesting because it comes from a common dietary protein.
The Bigger Picture
With antibiotic resistance growing globally, natural antimicrobial peptides from common food sources offer a promising alternative. Lactoferricin's acid-enhanced activity makes it particularly suited for gut and food safety applications.
What This Study Doesn't Tell Us
In vitro study only. Antibacterial activity in a test tube may not translate to effectiveness inside the body, where pH, salt levels, and other proteins can interfere.
Questions This Raises
- ?Could lactoferricin be used as a food preservative in acidic products?
- ?Does oral lactoferricin provide gut antimicrobial protection?
Trust & Context
- Key Stat:
- Broad-spectrum + acid-enhanced Lactoferricin B killed many bacterial species and worked even better at lower pH — ideal for stomach and food environments
- Evidence Grade:
- Moderate — comprehensive in vitro antimicrobial spectrum study. Multiple species tested under varying conditions.
- Study Age:
- Published in 1994 (32 years ago). Lactoferricin is now well-characterized and recognized as a potent natural antimicrobial.
- Original Title:
- Lactoferricin, a new antimicrobial peptide.
- Published In:
- The Journal of applied bacteriology, 77(2), 208-14 (1994)
- Authors:
- Jones, E M, Smart, A, Bloomberg, G, Burgess, L, Millar, M R
- Database ID:
- RPEP-00297
Evidence Hierarchy
Frequently Asked Questions
Where does lactoferricin come from?
Lactoferricin B is produced when stomach acid and the enzyme pepsin digest lactoferrin, a protein naturally present in cow's milk. It's essentially a natural antibiotic that forms when you digest milk.
Why does it work better in acid?
Many antimicrobial peptides are more active at lower pH because the acidic environment enhances their ability to interact with and disrupt bacterial membranes. This makes lactoferricin well-suited for the stomach environment.
Read More on RethinkPeptides
Cite This Study
https://rethinkpeptides.com/research/RPEP-00297APA
Jones, E M; Smart, A; Bloomberg, G; Burgess, L; Millar, M R. (1994). Lactoferricin, a new antimicrobial peptide.. The Journal of applied bacteriology, 77(2), 208-14.
MLA
Jones, E M, et al. "Lactoferricin, a new antimicrobial peptide.." The Journal of applied bacteriology, 1994.
RethinkPeptides
RethinkPeptides Research Database. "Lactoferricin, a new antimicrobial peptide." RPEP-00297. Retrieved from https://rethinkpeptides.com/research/jones-1994-lactoferricin-a-new-antimicrobial
Access the Original Study
Study data sourced from PubMed, a service of the U.S. National Library of Medicine, National Institutes of Health.
This study breakdown was produced by the RethinkPeptides research team. We analyze and report published research findings without making health recommendations. All interpretations are based solely on the published abstract and study data.