Title: Identification and characterization of a highly thermostable bacteriophage lysozyme
Authors: Lavigne, Rob ×
Briers, Yves
Hertveldt, Kirsten
Robben, Johan
Volckaert, Guido #
Issue Date: Nov-2004
Publisher: Birkhauser verlag ag
Series Title: Cellular and molecular life sciences vol:61 issue:21 pages:2753-2759
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 100degreesC and 21% after autoclaving. This thermostability could prove an interesting characteristic for food conservation technology.
ISSN: 1420-682X
Publication status: published
KU Leuven publication type: IT
Appears in Collections:Division of Gene Technology (-)
Biochemistry, Molecular and Structural Biology Section
× corresponding author
# (joint) last author

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