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Identification and characterization of a highly thermostable bacteriophage lysozyme

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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.
Keywords
phage infection, phage, lysozyme, recombinant expression, phi KMV, mass spectrometry, thermostable, T4 LYSOZYME, PURIFICATION, ENZYME, PROTEINS, INACTIVATION, INHIBITOR, AMIDASE, VIRIONS, GENOME, GENE

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MLA
Lavigne, R et al. “Identification and Characterization of a Highly Thermostable Bacteriophage Lysozyme.” CELLULAR AND MOLECULAR LIFE SCIENCES 61.21 (2004): 2753–2759. Print.
APA
Lavigne, R, Briers, Y., Hertveldt, K., Robben, J., & Volckaert, G. (2004). Identification and characterization of a highly thermostable bacteriophage lysozyme. CELLULAR AND MOLECULAR LIFE SCIENCES, 61(21), 2753–2759.
Chicago author-date
Lavigne, R, Yves Briers, K Hertveldt, J Robben, and G Volckaert. 2004. “Identification and Characterization of a Highly Thermostable Bacteriophage Lysozyme.” Cellular and Molecular Life Sciences 61 (21): 2753–2759.
Chicago author-date (all authors)
Lavigne, R, Yves Briers, K Hertveldt, J Robben, and G Volckaert. 2004. “Identification and Characterization of a Highly Thermostable Bacteriophage Lysozyme.” Cellular and Molecular Life Sciences 61 (21): 2753–2759.
Vancouver
1.
Lavigne R, Briers Y, Hertveldt K, Robben J, Volckaert G. Identification and characterization of a highly thermostable bacteriophage lysozyme. CELLULAR AND MOLECULAR LIFE SCIENCES. 2004;61(21):2753–9.
IEEE
[1]
R. Lavigne, Y. Briers, K. Hertveldt, J. Robben, and G. Volckaert, “Identification and characterization of a highly thermostable bacteriophage lysozyme,” CELLULAR AND MOLECULAR LIFE SCIENCES, vol. 61, no. 21, pp. 2753–2759, 2004.
@article{6846539,
  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.},
  author       = {Lavigne, R and Briers, Yves and Hertveldt, K and Robben, J and Volckaert, G},
  issn         = {1420-682X},
  journal      = {CELLULAR AND MOLECULAR LIFE SCIENCES},
  keywords     = {phage infection,phage,lysozyme,recombinant expression,phi KMV,mass spectrometry,thermostable,T4 LYSOZYME,PURIFICATION,ENZYME,PROTEINS,INACTIVATION,INHIBITOR,AMIDASE,VIRIONS,GENOME,GENE},
  language     = {eng},
  number       = {21},
  pages        = {2753--2759},
  title        = {Identification and characterization of a highly thermostable bacteriophage lysozyme},
  url          = {http://dx.doi.org/10.1007/s00018-004-4301-y},
  volume       = {61},
  year         = {2004},
}

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