Purification and Properties of Bacteriolytic Enzymes from Bacillus licheniformis YS-1005 against Streptococcus mutans

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概要

• 論文の詳細を見る

•   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.

• 社団法人日本農芸化学会の論文
• 1999-01-23

著者

• Kim Soyoung

  Department Of Food And Biotechnology And Bioproduct Research Center Yonsei University

• Bai Dong-Hoon

  Department of Food Engineering, Dankook University

• OHK SeungHo

  Department of Food and Biotechnology, and Bioproduct Research Center, Yonsei University

• BAI DongHoon

  Department of Food Engineering, Dankook University

• YU JuHyun

  Department of Food and Biotechnology, and Bioproduct Research Center, Yonsei University

• Yu Juhyun

  Department Of Food And Biotechnology And Bioproduct Research Center Yonsei University

• Ohk Seungho

  Department Of Food And Biotechnology And Bioproduct Research Center Yonsei University

• Bai Donghoon

  Department Of Food Engineering Dankook University

• Kim So-young

  Department Of Biochemistry And Molecular Biology Cancer Research Center Seoul National University Co

• Ohk Seung-Ho

  Department of Food and Biotechnology, and Bioproduct Research Center, Yonsei University

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