Lytic Activity of LysH5 endolysin secreted by Lactococcus lactis using the secretion signal sequence of bacteriocin Lcn972

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Abstract

Bacteriophage endolysins have an interesting potential as antimicrobials. The endolysin LysH5, encoded by Staphylococcus aureus phage vB_SauS-phi-IPLA88, was expressed and secreted in Lactococcus lactis using the signal peptide of bacteriocin lacto-coccin 972 and lactococcal constitutive and inducible promoters. Up to 80 U/mg of extracellular active endolysin was detected in culture supernatants, but most of the protein (up to 323 U/mg) remained in the cell extracts. © 2012, American Society for Microbiology.

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Rodríguez-Rubio, L., Gutiérrez, D., Martínez, B., Rodríguez, A., & García, P. (2012). Lytic Activity of LysH5 endolysin secreted by Lactococcus lactis using the secretion signal sequence of bacteriocin Lcn972. Applied and Environmental Microbiology, 78(9), 3469–3472. https://doi.org/10.1128/AEM.00018-12

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