scispace - formally typeset
Journal ArticleDOI

Antibacterial spectrum of lactoferricin B, a potent bactericidal peptide derived from the N-terminal region of bovine lactoferrin

TLDR
Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested, and Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.
Abstract
A physiologically diverse range of Gram-positive and Gram-negative bacteria was found to be susceptible to inhibition and inactivation by lactoferricin B, a peptide produced by gastric pepsin digestion of bovine lactoferrin. The list of susceptible organisms includes Escherichia coli, Salmonella enteritidis, Klebsiella pneumoniae, Proteus vulgaris, Yersinia enterocolitica, Pseudomonas aeruginosa, Campylobacter jejuni, Staphylococcus aureus, Streptococcus mutans, Corynebacterium diphtheriae, Listeria monocytogenes and Clostridium perfringens. Concentrations of lactoferricin B required to cause complete inhibition of growth varied within the range of 0.3 to 150 micrograms/ml, depending on the strain and the culture medium used. The peptide showed activity against E. coli O111 over the range of pH 5.5 to 7.5 and was most effective under slightly alkaline conditions. Its antibacterial effectiveness was reduced in the presence of Na+, K+, Mg2+ or Ca2+ ions, or in the presence of various buffer salts. Lactoferricin B was lethal, causing a rapid loss of colony-forming capability in most of the species tested. Pseudomonas fluorescens, Enterococcus faecalis and Bifidobacterium bifidum strains were highly resistant to this peptide.

read more

Citations
More filters
Journal ArticleDOI

Physico-chemical characteristics of goat and sheep milk

TL;DR: In this article, the main forms of caprine and ovine caseino-macropeptides (CMP), which are the soluble C-terminal derivatives from the action of chymosin on β-casein during the milk clotting process of cheesemaking, have been identified and are a good source of antithrombotic peptides.
Journal ArticleDOI

Tryptophan- and arginine-rich antimicrobial peptides: structures and mechanisms of action.

TL;DR: In this review, the structures of a number of different Trp- and Arg-rich antimicrobial peptides are examined and some of the major mechanistic studies are presented.
Journal ArticleDOI

Bioactive Milk Peptides: A Prospectus

TL;DR: This work reviews the scientific literature and attempts to stimulate consideration of the continued use of bioactive peptides and their expanded development as a commercial product.
Journal ArticleDOI

Lactoferrin--a multifunctional protein with antimicrobial properties.

TL;DR: Its extensive antimicrobial activities were originally attributed to its ability to sequester essential iron, however, it is now established that it possesses bactericidal activities as a result of a direct interaction between the protein or lactoferrin-derived peptides.
Journal ArticleDOI

Lactoferrin: a general review

TL;DR: A wide spectrum of functions are ascribed to lactoferrin, which range from a role in the control of iron availability to immune modulation, and more research is necessary to obtain clarity with regard to the exact mechanism of action.
References
More filters
Related Papers (5)