クロストリジウム・HM3ファージの溶菌酵素の性質

概要

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A lytic enzyme (phage HM3-endolysin) was isolated from phage HM3-induced lysate of Clostridium saccharoperbutylacetonicum, by precipitation with ammonium sulfate, DEAE-Sephadex A-50, and Sephadex G-75. Optimum pH for the lytic activity was 6 to 6.5, and optimum temperature was 30°C. The lytic enzyme activity was stimulated about 130% by 10-3 M EDTA. Phage HM 3-endolysin lysed the living cells, but it had a narrow specificity which was restricted to a certain species of Clostridium such as C. saccharoperbutylacetonicum, C. botulinum, C. butyricum, C. sporogenes and C. thiaminolyticum. Digestion of the cell wall peptidoglycan of C. saccharoperbutylacetonicum by phage HM 3-endolysin was accompanied by the release of reducing groups without a concomitant release of amino groups. The reducing end was elucidated to be N-acetylmuramic acid by borohydride reaction. This result indicates that phage HM 3-endolysin is N-acetylmuramidase, which cleaves β-1, 4 bounds between N-acetylmuramic acid and N-acetylglucosamine.
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