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Hydrolysate [id=LFB0003]

Producer Organism : Native Protein : Production Method :
Cow Lactoferrin (LF) Enzymatic hydrolysis
Activity : No activity detected
Target Organisms :

Unavailable data

Description :
Production method: Trypsin, papain, actinase AS (Streptomyces griseus), protease P (Aspergillus melleus), protease A (Aspergillus oryzae) or bioprase (Bacillus subtilis) hydrolysis.

Citation: 1

Potent antibacterial peptides generated by pepsin digestion of bovine lactoferrin

Cited Entries: LFB0002, LFB0003

Authors:Tomita, M., Bellamy, W., Takase, M., Yamauchi, K., Wakabayashi, H., Kawase, K.
Journal: Journal of Dairy Science 1991, 74(12).
CrossRef External Link
Abstract: The antibacterial properties of enzymatic hydrolysates of bovine lactoferrin were examined to determine whether active peptides are produced from this protein. Hydrolysates prepared by cleavage of lactoferrin with porcine pepsin, cod pepsin, or acid protease from Penicillium duponti showed strong activity against Escherichia coli O111, whereas hydrolysates produced by trypsin, papain, or other neutral proteases were much less active. Low molecular weight peptides generated by porcine pepsin cleavage of lactoferrin showed broad-spectrum antibacterial activity, inhibiting the growth of a number of Gram-negative and Gram-positive species, including strains that were resistant to native lactoferrin. The antibacterial potency of the hydrolysate was at least eightfold greater than that of undigested lactoferrin with all strains tested. The active peptides retained their activity in the presence of added iron, unlike native lactoferrin. The effect of the hydrolysate was bactericidal as indicated by a rapid loss of viability of E. coli O111. The lactoferrin hydrolysate described in the present study has commercial value as a natural preservative agent for use in foods and cosmetics, and as a functional component of new clinical foods for prevention or treatment of gastrointestinal disease.
Keywords: lactoferrin,antibacterial peptides,pepsin digestion

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