Enzymes of SPZ7 Phage: Isolation and Properties

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P. A. Levashov^1*, D. V. Popov², V. M. Popova², E. L. Zhilenkov², O. A. Morozova³, N. G. Belogurova¹, S. A. Sedov¹, I. A. Dyatlov², N. L. Klyachko¹, and A. V. Levashov¹

¹Faculty of Chemistry, Lomonosov Moscow State University, 119991 Moscow, Russia; fax: (495) 939-5417; E-mail: levashov@aport.ru

²State Research Center for Applied Microbiology and Biotechnology, 142279 Obolensk, Moscow Region, Russia; E-mail: popoviie@mail.ru

³Bacteriological Laboratory, Clinical Center, Sechenov Moscow Medical Academy, Bolshaya Pirogovskaya ul. 6, 119021 Moscow, Russia; E-mail: molgalex@yandex.ru

^* To whom correspondence should be addressed.

Received December 28, 2009; Revision received March 9, 2010

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Bacteriophage enzyme preparations exolysin and endolysin were studied. Exolysin (a phage-associated enzyme) was obtained from tail fraction and endolysin from phage-free cytoplasmic fraction of disintegrated Salmonella enteritidis cells. A new method for purification of these enzymes was developed, and their molecular masses were determined. The main catalytic properties of the studied enzymes (pH optimum and specificity to bacterial substrates) were found to be similar. Both enzymes lyse Escherichia coli cells like chicken egg lysozyme, but more efficiently lyse S. enteritidis cells and cannot lyse Micrococcus luteus, a good substrate for chicken egg lysozyme. Similar properties of exolysin and endolysin suggest that these enzymes are structurally similar or even identical.

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KEY WORDS: bacteriophage enzyme, lysis of bacteria, bacteriolytic activity

DOI: 10.1134/S0006297910090105

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