Investigation of the antibiotic complex produced by Lactococcus lactis subsp. lactis 194, Variant K
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  • 作者:E. A. Ustyugova (1) ustyugova.katya@mail.ru
    G. B. Fedorova (2)
    G. S. Katrukha (2)
    L. G. Stoyanova (1) stoyanovamsu@mail.ru
  • 关键词:environmental strain L. lactis subsp. lactis 194 – ; phase variation – ; antibiotic complex – ; isolation – ; physicochemical properties – ; identification
  • 刊名:Microbiology
  • 出版年:2011
  • 出版时间:October 2011
  • 年:2011
  • 卷:80
  • 期:5
  • 页码:657-663
  • 全文大小:209.5 KB
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  • 作者单位:1. Biological Faculty, Moscow State University, Moscow, 119992 Russia2. Gause Institute of New Antibiotics, Russian Academy of Medical Sciences, ul. Bol鈥檚haya Pirogovskaya 11, Moscow, 119021 Russia
  • 刊物类别:Biomedical and Life Sciences
  • 刊物主题:Life Sciences
    Microbiology
    Medical Microbiology
    Russian Library of Science
  • 出版者:MAIK Nauka/Interperiodica distributed exclusively by Springer Science+Business Media LLC.
  • ISSN:1608-3237
文摘
Phase variation in the culture of the environmental strain Lactococcus lactis subsp. lactis 194 resulted in the formation of two types of colonies differing by 15% in antibiotic activity. The active variant 194-K produced an antibiotic complex with a broad spectrum of antibacterial and antifungal activity. Five components (194-A, B, C, D, and E) were isolated from the complex by solid-phase extraction and thin-layer chromatography. Components 194-A and 194-B were hydrophobic neutral compounds soluble in organic solvents. Component 194-A possessed fungicidal activity, whereas component 194-B exhibited only bactericidal activity. Physicochemical studies of the isolated components 194-A and 194-B revealed that they had no analogs in the Berdy database of biologically active substances (BNPD) and appeared to be novel antibiotics. Component 194-C was a hydrophilic polar compound inhibiting growth of gram-positive and gramnegative bacteria. Component 194-D belonged to peptide antibiotics; it inhibited growth of only gram-positive bacteria and was similar to nisin A in biological properties but differed in electrophoretic mobility and molecular mass.

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