Main Article Content
Isolation and characterization of a bacteriocin produced by an isolated Bacillus subtilis LFB112 that exhibits antimicrobial activity against domestic animal pathogens
Abstract
The emergence of multidrug-resistant pathogens and the restriction on the use antibiotics as growth promoters in feed have drawn attention to the search for possible alternatives. Much interest has been focused on bacteriocins because they exhibit inhibitory activity against pathogens. In this study, an antibacterial substance produced by an isolated Bacillus subtilis strain LFB112 from Chinese herbs, was identified as bacteriocin. It was effective against both Gram-positive and Gram-negative bacteria
involved in domestic animal diseases, including Escherichia coli, Salmonella pullorum, Pseudomonas aeruginosa, Pasteurella multocida, Clostridium perfringens, Micrococcus luteus, Streptococcus bovis
and Staphylococcus aureus. Two multidrug-resistant clinical isolates and a phytopathogenic yeast strain were also inhibited. The antimicrobial substance was secreted at the middle of the exponential phase, whose activity was sensitive to proteinase K and pronase E but resistant to the proteolytic action of papain, trypsin and pepsin. The antimicrobial activity was relatively heat resistant and also active over a wide range of pH 3 - 10. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis
analysis revealed that the active peptide had an apparent molecular weight of about 6.3 kDa. It exhibited a bactericidal activity against S. aureus IVDC C56005. Such characteristics indicate that this bacteriocin may be a potential candidate for alternative agents to control important pathogens in domestic animal diseases.
involved in domestic animal diseases, including Escherichia coli, Salmonella pullorum, Pseudomonas aeruginosa, Pasteurella multocida, Clostridium perfringens, Micrococcus luteus, Streptococcus bovis
and Staphylococcus aureus. Two multidrug-resistant clinical isolates and a phytopathogenic yeast strain were also inhibited. The antimicrobial substance was secreted at the middle of the exponential phase, whose activity was sensitive to proteinase K and pronase E but resistant to the proteolytic action of papain, trypsin and pepsin. The antimicrobial activity was relatively heat resistant and also active over a wide range of pH 3 - 10. Sodium dodecyl sulfate-polyacrylamide gel electrophoresis
analysis revealed that the active peptide had an apparent molecular weight of about 6.3 kDa. It exhibited a bactericidal activity against S. aureus IVDC C56005. Such characteristics indicate that this bacteriocin may be a potential candidate for alternative agents to control important pathogens in domestic animal diseases.