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 ROBBEN, Johan Volckaert, G |
Issue Date: | 2004 | Publisher: | BIRKHAUSER VERLAG AG | Source: | 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 | Keywords: | phage; phage infection; lysozyme; recombinant expression; phi KMV; mass spectrometry; thermostable | Document URI: | http://hdl.handle.net/1942/2377 | ISSN: | 1420-682X | e-ISSN: | 1420-9071 | DOI: | 10.1007/s00018-004-4301-y | ISI #: | 000225046500012 | Category: | A1 | Type: | Journal Contribution | Validations: | ecoom 2005 |
Appears in Collections: | Research publications |
Show full item record
SCOPUSTM
Citations
64
checked on Sep 2, 2020
WEB OF SCIENCETM
Citations
86
checked on Oct 12, 2024
Page view(s)
52
checked on Jun 28, 2023
Google ScholarTM
Check
Altmetric
Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.