Figure 1.
Purification diagram and SDS analysis of RAcc-royalisin.
(A) The diagram of RAcc-royalisin purified at UV A280 nm from the recombinant E. coli. 1–2 (indicated by arrows): The outflow peak of the first injection samples; 3–4 : The outflow peak of the second injection samples; 5–10 : The elution peak of RAcc-royalisin. (B) The SDS-PAGE pattern of the purified RAcc-royalisin. Lane M: Protein marker; Lane 1–5: The elution peak products; Lane 6: The outflow peak products.
Figure 2.
RAcc-royalisin inhibition plate against Gram-positive bacteria.
B. subtilis (plate A) and M. flavus (plate B) were treated by RAcc-royalisin , nisin
and blank control
, respectively.
Figure 3.
Correlation between RAcc-royalisin concentration and antibacterial activity against Gram-positive bacterial strains.
Correlation between RAcc-royalisin concentration and antibacterial activity against B. subtilis (A) and M. flavus (B).
Table 1.
The ΔOD600 (mean ± SD) value of RAcc-royalisn and nisin against three Gram-positive bacterial strains at different concentrations.
Table 2.
Minimum inhibition concentrations (µg/ml; MICa) at 24 h for RAcc-royalisin and nisin on different microorganism strains.
Figure 4.
The effects of temperature on the antibacterial activity of RAcc-royalisin against B. subtilis.
Figure 5.
Determination of cell surface hydrophobicity as measured by cell adhesion.
Figure 6.
The effect of RAcc-royalisin on the cell membrane of Gram-positive bacteria.
The UV absorbance of B. subtilis (A) and M. flavus (B) at 0, 15, 30, 45 and 60 minutes of treatment with RAcc-royalisin, nisin and blank control, respectively.
Figure 7.
Transmission electron photomicrographs (at 50000× magnification) of B. subtilis treated with RAcc-royalisin.
(A) Untreated B. subtilis. (B) B. subtilis treated with RAcc-royalisin at 37°C for 48 hours. Bar represents 0.2 µm.