Purification and Properties of Bacteriolytic Enzymes from<i>Bacillus licheniformis</i>YS-1005 against<i>Streptococcus mutans</i>

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  • KIM So-Young
    Department of Food and Biotechnology, and Bioproduct Research Center, Yonsei University
  • OHK Seung-Ho
    Department of Food and Biotechnology, and Bioproduct Research Center, Yonsei University
  • BAI Dong-Hoon
    Department of Food Engineering, Dankook University
  • YU Ju-Hyun
    Department of Food and Biotechnology, and Bioproduct Research Center, Yonsei University

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  • Purification and Properties of Bacteriolytic Enzymes from Bacillus licheniformis YS-1005 against Streptococcus mutans.
  • Purification and properties of bacteriolytic enzymes from Bacillus licheniformis YS-1005 against Streptomyces mutans

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  To find a novel lytic enzyme against cariogenic Streptococci, strains showing strong lytic activity have been screened from soil using Streptococcus mutans. A strain identified as Bacillus licheniformis secreted two kinds of lytic enzymes, which were purified by methanol precipitation, CM-cellulose chromatography, gel filtration, and hydroxyapatite chromatography. The molecular weights of these two enzymes, L27 and L45, were 27,000 and 45,000, respectively. Optimum pH and temperature of both enzymes for lytic activity were pH 8 and 37°C. L27 and L45 digest the peptide linkage between L-Ala and D-Glu in peptidoglycan of Streptococcus mutans. The lytic activity was highly specific for Streptococcus mutans, suggesting their potential use as a dental care product.<br>

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