4.6 Article

Lytic Activity of LysH5 Endolysin Secreted by Lactococcus lactis Using the Secretion Signal Sequence of Bacteriocin Lcn972

Journal

APPLIED AND ENVIRONMENTAL MICROBIOLOGY
Volume 78, Issue 9, Pages 3469-3472

Publisher

AMER SOC MICROBIOLOGY
DOI: 10.1128/AEM.00018-12

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Funding

  1. Ministry of Science and Innovation, Spain [AGL2009-13144-C02-01]
  2. Science, Technology and Innovation Programme, Principado de Asturias, Spain [IB08-052]
  3. CSIC, Spain [PIE200970I090]

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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 lactococcin 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.

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