Discussion: The isolate studied was tested for innate antibiotic function on the following media: AC, LB, and 10% TSA. The ESKAPE relative strain that presented a response to the isolate was B.subtilis. In all cases except for that of LB, the isolate showed antibiotic qualities towards B.subtilis by presenting a zone of clearance on AC and 10% TSA media. This behavior is shown in Figures 4, 5, and 6.In the case with LB, B.subtilis inhibited the growth of the isolate as depicted by the empty patch containing the bacterium-inoculated streak pattern. Unlike its reaction toward B.subtilis, the isolate was neither inhibitory nor inhibited by the other ESKAPE relative strains: E.coli, S.epidermidis, P.putida and Enterobacter agglomerans. B.subtilis
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The forward and reverse primers aforementioned in the materials were specifically designed to attach to the 16s rRNA site for duplication. The buffer provides a medium for the increase of Mg2+ concentration derived from MgCl2. This concentration gradient influences the productivity and fidelity of the Taq DNA polymerase as it uses the deoxynucleotides (dNTPs) to create the 16s rRNA copy. After repetitive cycles of denaturation, annealing, and extension through optimal temperatures, copies of the 16s rRNA band were made and purified to later be assessed using agarose gel electrophoresis. Based on Figure 7, there was a clear indication of a band on 16s rRNA PCR with a basepair length of approximately 1450bp. By analyzing this band in terms of its specific nucleotide sequence and comparing it with the national database, the derived antibiotic-producing isolate was from the genus …show more content…
Studies have shown that the main mechanism of resistance to antibiotics such as Penicillin involve alterations in target site (penicillin-binding proteins), hydrolyzing enzyme activity, and limited access for penicillin molecules to target sites (Nakazawa, 1982). By studying the role of penicillin-binding proteins in penicillin-resistant Streptomyces cacaoi, the penicillin-binding proteins are slightly altered to prevent the binding of penicillin molecules to target sites (Nakazawa, 1982). This change in target site can drastically increase the levels of resistance to molecules found in penicillin and can be associated as a primary mechanism of intrinsic
The forward and reverse primers aforementioned in the materials were specifically designed to attach to the 16s rRNA site for duplication. The buffer provides a medium for the increase of Mg2+ concentration derived from MgCl2. This concentration gradient influences the productivity and fidelity of the Taq DNA polymerase as it uses the deoxynucleotides (dNTPs) to create the 16s rRNA copy. After repetitive cycles of denaturation, annealing, and extension through optimal temperatures, copies of the 16s rRNA band were made and purified to later be assessed using agarose gel electrophoresis. Based on Figure 7, there was a clear indication of a band on 16s rRNA PCR with a basepair length of approximately 1450bp. By analyzing this band in terms of its specific nucleotide sequence and comparing it with the national database, the derived antibiotic-producing isolate was from the genus …show more content…
Studies have shown that the main mechanism of resistance to antibiotics such as Penicillin involve alterations in target site (penicillin-binding proteins), hydrolyzing enzyme activity, and limited access for penicillin molecules to target sites (Nakazawa, 1982). By studying the role of penicillin-binding proteins in penicillin-resistant Streptomyces cacaoi, the penicillin-binding proteins are slightly altered to prevent the binding of penicillin molecules to target sites (Nakazawa, 1982). This change in target site can drastically increase the levels of resistance to molecules found in penicillin and can be associated as a primary mechanism of intrinsic