Lytic activity of the recombinant staphylococcal bacteriophage ΦH5 endolysin active against Staphylococcus aureus in milk

International Journal of Food Microbiology

Volumn 128, Issue 2, 2008, Pages 212-218

  Obeso, José María ^a   Martínez, Beatriz ^a   Rodríguez, Ana ^a   García, Pilar ^a  

^a DEPARTMENT OF MICROBIOLOGY AND BIOCHEMISTRY OF DAIRY PRODUCTS   (Spain)

Author keywords

Biopreservation; Endolysin; Natural antimicrobials; Staphylococcus aureus

Indexed keywords

AMIDASE; BACTERIAL PROTEIN; ENDOLYSIN H5; HYDROLASE; PEPTIDASE; RECOMBINANT ENZYME; UNCLASSIFIED DRUG;

ANTIMICROBIAL ACTIVITY; ARTICLE; BACTERIAL GENOME; BACTERIAL GROWTH; BACTERIAL STRAIN; BACTERICIDAL ACTIVITY; BACTERIOPHAGE PHI H5; BACTERIUM CONTAMINATION; BACTERIUM DETECTION; BIOLOGICAL CONTROL AGENT; CONTROLLED STUDY; DAIRYING; ENZYME ACTIVITY; ENZYME PURIFICATION; ENZYME STABILITY; ESCHERICHIA COLI; FOOD CONTAMINATION; GENETIC CODE; INCUBATION TEMPERATURE; INCUBATION TIME; LYSIS; MILK; MOLECULAR CLONING; MOLECULAR PHYLOGENY; MOLECULAR WEIGHT; NONHUMAN; NUCLEOTIDE SEQUENCE; PH; PROTEIN DOMAIN; SEQUENCE ANALYSIS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS; STAPHYLOCOCCUS PHAGE; THERMOSTABILITY;

AMIDOHYDROLASES; ANIMALS; CATTLE; CLONING, MOLECULAR; ENDOPEPTIDASES; ESCHERICHIA COLI; FEMALE; GENE EXPRESSION REGULATION, ENZYMOLOGIC; GENE EXPRESSION REGULATION, VIRAL; HUMANS; HYDROGEN-ION CONCENTRATION; MEMBRANE PROTEINS; MILK; N-ACETYLMURAMOYL-L-ALANINE AMIDASE; PEPTIDE HYDROLASES; RECOMBINANT FUSION PROTEINS; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS PHAGES; TEMPERATURE; VIRAL PROTEINS;

BOVINAE; ESCHERICHIA COLI; STAPHYLOCOCCUS AUREUS; STAPHYLOCOCCUS EPIDERMIDIS;

EID: 55549119928     PISSN: 01681605     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ijfoodmicro.2008.08.010     Document Type: Article

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