Journal
LWT-FOOD SCIENCE AND TECHNOLOGY
Volume 112, Issue -, Pages -Publisher
ELSEVIER
DOI: 10.1016/j.lwt.2019.05.117
Keywords
Lactobacillus curvatus; Fish; Multiple bacteriocins; Bacteriocin structure/function; In vitro safety
Categories
Funding
- Ministerio de Ciencia, Innovacion y Universidades [RTI2018-094907-B-I00]
- Universidad Complutense de Madrid [FEI16/54]
- Santander/UCM [PR75/18]
- company Innaves S. A. (Vigo, Spain)
- UCM, Spain
- UCM [FEI16/54]
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The antimicrobial activity of Lactobacillus curvatus BCS35 is due to the production of, at least, two class Ha bacteriocins: sakacin P-H12Y (SakP-H12Y), which is a sakacin P (SakP) variant with tyrosine (Tyr) instead of histidine (His) at position 12, and sakacin X (SakX). Moreover, DNA sequence analysis revealed the presence of the genes encoding the two-peptide bacteriocin sakacin T. In order to compare the specific antimicrobial activities of SakP-H12Y and SakX with other class Ha bacteriocins (SakP from Lactobacillus sakei LTH673 and pediocin PA-1 (PedPA-1) from Pediococcus acidilactici 347), and to determine if the substitution His12/Tyr12 in SakP-H12Y/SakP exerts any effect on the bacteriocin potency and/or specificity, these four bacteriocins were purified and challenged against different indicator strains. Our results showed that (i) PedPA-1 was, in general, the most active peptide, and (ii) SakP-H12Y, which contains one less positively charged residue in the N-terminal half (His12/Tyr12), has a reduced antimicrobial potency against most of the tested indicators compared to Sale, confirming the importance of the N-terminal cationic patch of SakP-H12Y/SakP in target-cell binding, potency and specificity. The in vitro safety of Lb. curvatus BCS35 was established by antibiotic susceptibility testing concluding that it may be considered as a safe strain.
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