title: Identification and characterization of a highly thermostable bacteriophage lysozyme.
abstract: Pseudomonas aeruginosa bacteriophage phiKMV is a T7-like lytic phage. Liquid chromatography-mass spectrometry of the structural proteins revealed gene product 36 (gp36) as part of the phiKMV phage particle. The presence of a lysozyme domain in the C terminal of this protein (gp36C) was verified by turbidimetric assays on chloroform-treated P. aeruginosa PAO1 and Escherichia coli WK6 cells. The molecular mass (20,884 Da) and pI (6.4) of recombinant gp36C were determined, as were the optimal enzymatic conditions (pH 6.0 in 16.7 mM phosphate buffer) and activity (4800 U/mg). Recombinant gp36C is a highly thermostable lysozyme, retaining 26% of its activity after 2 h at 100 degrees C and 21% after autoclaving. This thermostability could prove an interesting characteristic for food conservation technology.
authors.affiliation: Laboratory of Gene Technology, Katholieke Universiteit Leuven, Kasteelpark Arenberg 21, 3001 Leuven, Belgium.
authors.forename: R
authors.initials: R
authors.lastname: Lavigne
authors.forename: Y
authors.initials: Y
authors.lastname: Briers
authors.forename: K
authors.initials: K
authors.lastname: Hertveldt
authors.forename: J
authors.initials: J
authors.lastname: Robben
authors.forename: G
authors.initials: G
authors.lastname: Volckaert
mesh_terms: D000595:Amino Acid Sequence; D001435:Bacteriophages / Q000201:enzymology*; D004795:Enzyme Stability; D006863:Hydrogen-Ion Concentration; D008969:Molecular Sequence Data; D008970:Molecular Weight; D009113:Muramidase / Q000737:chemistry* / Q000302:isolation & purification / Q000378:metabolism*; D017434:Protein Structure, Tertiary; D016415:Sequence Alignment; D013696:Temperature
chemical_list: D009113:Muramidase