PMID: 4990043Jun 1, 1967Paper

Purification and properties of a thermophilic bacteriophage lytic enzyme

Journal of Virology
N E Welker

Abstract

A phage lytic enzyme was isolated from lysates of Bacillus stearothermophilus (NCA 1503-4R). The enzyme was purified 1,998-fold with a 27% recovery of enzyme activity. By use of polyacrylamide gel electrophoresis and sucrose gradient centrifugation the enzyme was judged free from protein contaminants. The lytic enzyme was active over a pH range of 6.0 to 7.0, with a maximum at 6.3, and it was stable between pH 7.0 and 8.0 and at 5.0 and unstable between pH 5.5 and 6.5. The temperature coefficient (Q(10)) was 2.27 between 35 and 45 C, 2.01 between 45 and 55 C, and 2.00 between 50 and 60 C. Lytic enzyme in 0.1 m sodium phosphate was not inactivated after a 1-hr exposure to temperatures below 65.5 C, whereas a 1% inactivation was observed at 70.6 C. A 2-hr exposure at 60.1, 65.5, and 70.6 C resulted in an inactivation of 1.2, 9.6, and 12.0%, respectively. A sodium phosphate concentration of at least 0.1 m was necessary for the prolonged exposure of lytic enzyme at 55 C (pH 6.3), whereas 0.005 m was required for maximal lytic activity. Lytic activity was stimulated 169, 165, and 160% by 10(-4)m Mg(++), Ca(++), and Mn(++), respectively. Lytic activity was inhibited 75% by 10(-4)m ethylenediaminetetraacetic acid (EDTA). The EDTA inhi...Continue Reading

References

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