Purification, Bacteriolytic Activity, and Specificity of β-Lytic Protease from Lysobacter sp. IB-9374(ENZYMOLOGY, PROTEIN ENGINEERING, AND ENZYME TECHNOLOGY)

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Lysobacter sp. IB-9374, which was isolated from soil as a high lysyl endopeptidase-producing strain (Chohnan et al., FEMS Microbiol. Lett., 213, 13-20, 2002), was found to produce a β-lytic protease capable of lysing gram-positive bacteria such as Staphylococcus aureus, Microccocus luteus, and Bacillus subtilis. The Lysobacter strain secreted the β-Lytic protease into the culture medium at a 2.4-fold higher level than Achromobacter lyticus. The enzyme was highly purified through a series of six steps with a high yield. The enzyme was strongly inhibited by tetraethylenepentamine and 1,10-phenanthroline. The purified enzyme lysed more efficiently almost all the gram-positive bacteria tested than lysozyme, lysostaphin, and mutanolysin. The enzyme was very similar to Achromobacterβ-lytic protease containing one zinc atom in terms of amino acid composition and N-terminal sequence. The nucleotide sequence revealed that the mature enzyme was composed of 179 amino acid residues with additional 198 amino acids at the amino-terminal end of the enzyme. The deduced amino acid sequence of the mature enzyme coincided with that of the Achromobacter enzyme, although the prepro-region showed a 41% sequence identity with the counterpart. These results indicate that Lysobacter sp. is a useful strain for an efficient large-scale preparation of β-lytic protease capable of lysing bacteria.
社団法人日本生物工学会の論文
2003-01-25