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Characterization of a lysin from deep-sea thermophilic bacteriophage GVE2

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Abstract

Thermostable enzymes from thermophiles have attracted extensive studies. However, little is known about thermophilic lysin of bacteriophage obtained from deep-sea hydrothermal vent. In this study, a lysin from deep-sea thermophilic bacteriophage Geobacillus virus E2 (GVE2) was characterized for the first time. It was found that the GVE2 lysin was highly homologous with N-acetylmuramoyl-L-alanine amidases. After expression in Escherichia coli, the recombinant GVE2 lysin was purified. The recombinant lysin was active over a range of temperature from 40 °C to 80 °C, with an optimum at 60 °C. Its optimal pH was 6.0, and it was stable over a wide range of pH from 4.0 to 10.0. The lysin was highly active when some enzyme inhibitors or detergents (phenylmethylsulfonyl fluoride, Tween 20, Triton X-100, and chaps) were used. However, it was strongly inhibited by sodium dodecyl sulfate and ethylene diamine tetraacetic acid. Its enzymatic activity could be slightly stimulated in the presence of Na+ and Li+. But the metal ions Mg2+, Ba2+, Zn2+, Fe3+, Ca2+, and Mn2+ at concentrations of 1 or 10 mM showed inhibitions to the lysin activity. Our study demonstrated the first characterization of lysin from deep-sea thermophilic bacteriophage.

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Acknowledgements

This work was financially supported by National Natural Science Foundation of China (40576076), China Ocean Mineral Resources R & D Association (DYXM-115–02–2–15) and Hi-Tech Research and Development Program of China (863 program of China; 2007AA091407).

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  1. Key Laboratory of Marine Biogenetic Resources, Third Institute of Oceanography, State Oceanic Administration, **amen, 361005, People’s Republic of China

    Ting Ye & **aobo Zhang

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  1. Ting Ye
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  2. **aobo Zhang
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Correspondence to **aobo Zhang.

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Ye, T., Zhang, X. Characterization of a lysin from deep-sea thermophilic bacteriophage GVE2. Appl Microbiol Biotechnol 78, 635–641 (2008). https://doi.org/10.1007/s00253-008-1353-1

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