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Functional and Molecular Characterization of a Newly Discovered Bacteriocin‐like Substance
Author(s) -
Brock Susan R.,
Knadler Judith,
Triplet Meredith,
Baker Jason C.
Publication year - 2008
Publication title -
the faseb journal
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.709
H-Index - 277
eISSN - 1530-6860
pISSN - 0892-6638
DOI - 10.1096/fasebj.22.1_supplement.1061.9
Subject(s) - bacteriocin , antimicrobial , bacteria , biology , antimicrobial peptides , microbiology and biotechnology , antibiotics , bacillus amyloliquefaciens , plasmid , gene , biochemistry , genetics
Bacteriocins are antimicrobial peptides produced by bacteria while antibiotics are non‐proteinacous small organic antimicrobial molecules. They also differ from antibiotics in modes of action. Their wide range of molecular and functional characteristics include: molecular weight, structure, temperature/pH stability, and killing spectrums of susceptible species. Bacteriocins present potential for diverse applications as treatment/prevention of infectious diseases, food preservers, ect. In the spring of 2006, a bacteriocin‐like substance, currently referred to as Bacteriocin X (Bac. X), was discovered from a putative strain of Bacillus amyloliquefaciens. The objective of this study was to discern the functional and molecular characteristics of Bac. X. It demonstrated a wide spectrum of activity against an array of bacterial organisms (both Gram(+) and Gram(−)), including a variety of potential pathogens. It displayed stability under extreme temperature and pH conditions. It was not notably susceptible to Proteinase K or Trypsin; but its activity was destroyed by Pronase E. Bac. X was also able to destroy mammalian cells. This study is still pursuing the purification of Bac. X from cell filtrate or perhaps a plasmid isolation of its gene to facilitate sequencing and homology comparisons, looking for the identification of the bacteriocin or documentation of a new one. MWSU Summer Research Institute