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Please use this identifier to cite or link to this item: http://hdl.handle.net/1942/2377

Title: Identification and characterization of a highly thermostable bacteriophage lysozyme
Authors: Lavigne, R
Briers, Y
Hertveldt, K
Volckaert, G
Issue Date: 2004
Citation: CELLULAR AND MOLECULAR LIFE SCIENCES, 61(21). p. 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.
Notes: Katholieke Univ Leuven, Lab Gene Technol, B-3001 Louvain, Belgium. Limburgs Univ Ctr, Biomed Res Inst, B-3590 Diepenbeek, Belgium. Transnatl Univ Limburg, Sch Life Sci, B-3590 Diepenbeek, Belgium.Volckaert, G, Katholieke Univ Leuven, Lab Gene Technol, Kasteelpk Arenberg 21, B-3001 Louvain, Belgium.guido.volckaert@agr.kuleuven.ac.be
URI: http://hdl.handle.net/1942/2377
DOI: 10.1007/s00018-004-4301-y
ISI #: 000225046500012
ISSN: 1420-682X
Category: A1
Type: Journal Contribution
Validation: ecoom, 2005
Appears in Collections: Research publications

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