Bioscience, Biotechnology, and Biochemistry
Online ISSN : 1347-6947
Print ISSN : 0916-8451
Biochemistry & Molecular Biology Regular Papers
Purification and Properties of Bacteriolytic Enzymes from Bacillus licheniformis YS-1005 against Streptococcus mutans
So-Young KIMSeung-Ho OHKDong-Hoon BAIJu-Hyun YU
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JOURNAL FREE ACCESS

1999 Volume 63 Issue 1 Pages 73-77

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Abstract

  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.

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© 1999 by Japan Society for Bioscience, Biotechnology, and Agrochemistry
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