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Figure 4 | BMC Microbiology

Figure 4

From: Biotechnical paving of recombinant enterocin A as the candidate of anti-Listeriaagent

Figure 4

Effects of pH, temperature and proteolytic enzymes on the rEntA activity. A, pH stability of rEntA. Purified rEntA was incubated in buffers with a pH range from 2 to 10 at 37°C for 12 h. The initial activity of the sample in a buffer with a pH of 6 was described as 100% activity. B, Thermal stability of EntA. Purified rEntA was incubated in buffers with a pH range from 2 to 10 at temperatures of 37, 60, 80, and 100°C for 1 h. The initial activity of the sample in a buffer with a pH of 6 was described as 100% activity. C, Proteolysis resistance of rEntA. Purified rEntA was incubated with pepsin, papain and trypsin at 37°C for 4 h. The residual antimicrobial activity of samples was tested after the pH was readjusted to pH 6.0 with sodium phosphate buffer.

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