Abstract
Plasmid-specified traits like lactose metabolism and L-asparginase production could be eliminated from Streptomyces longsporesflavns culture during production of fermented product (Microbial succession). In this study we mainly focus on plasmid profiling and plasmid characterization from S. longsporesflavns isolated from marine soil. Then we observe the efficacy of plasmid curing agent on S. longsporesflavns. Plasmid-free strains and cured derivatives harboring only a single plasmid (6.2 Kbp) were also obtained. Treatment of S. longsporesflavns with novobiocin at concentrations of 2.4 µg/ml could produce a large number of chloramphenicol‑ variants at a very high frequency (4.6%). These curing data confirmed the novobiocine act as an effective curing agent for S. longsporesflavns. Key words: Antibiotic resistance, curing agent, Streptomyces longsporesflavns, plasmid profile, plasmid curing.
Highlights
Streptomyces sp is a commercially important actinomycets variety of wide applications, both in food industry and as a probiotic agent for the improvement of human health, antileukaemia agent by secreting Lasparginase (Cebeci and Gürakan, 2003)
This study focused primarily on these three antibiotics, because they serve as selective markers in transformation studies of actinomycets (Kok et al, 1984)
These antibiotics have been listed as antibiotics which are authorized for veterinary medicine in Europe for the treatment of food- producing animals, including avian, bovine, prscine and porcine species (Charteris et al, 1998)
Summary
Streptomyces sp is a commercially important actinomycets variety of wide applications, both in food industry and as a probiotic agent for the improvement of human health, antileukaemia agent by secreting Lasparginase (Cebeci and Gürakan, 2003). To improve the strain characteristic in food industries, genetic modification of Streptomyces strains are normally targeted toward the improvement or augmentation of specific strain characteristics, such as bacteriocin and L-asparginase. L-asparaginase belongs to an amidase group that catalyses the conversion of L-asparagine to L-aspartic acid and ammonium. Asparagine is an amino acid required by cells for the production of protein. Asparagine is not an essential amino acid in normal cells and they synthesize this amino acid by the catalytic activity of asparagines synthetase from aspartic acid and glutamine.
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