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Antioxidants (Basel)
2023 Jun 07;126:. doi: 10.3390/antiox12061227.
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Characterization of a Novel Superoxide Dismutase from a Deep-sea Sea Cucumber (Psychoropotes verruciaudatus).
Li Y
,
Chen Z
,
Zhang P
,
Gao F
,
Wang J
,
Lin L
,
Zhang H
.
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At present, deep-sea enzymes are a research hotspot. In this study, a novel copper-zinc superoxide dismutase (CuZnSOD) was successfully cloned and characterized from a new species of sea cucumber Psychropotes verruciaudatus (PVCuZnSOD). The relative molecular weight of the PVCuZnSOD monomer is 15 kDa. The optimum temperature of PVCuZnSOD is 20 °C, and it maintains high activity in the range of 0-60 °C. It also has high thermal stability when incubated at 37 °C. PVCuZnSOD has a maximum activity of more than 50% in the pH range of 4-11 and a high activity at pH 11. In addition, PVCuZnSOD has strong tolerance to Ni2+, Mg2+, Ba2+, and Ca2+, and it can withstand chemical reagents, such as Tween20, TritonX-100, ethanol, glycerol, isopropanol, DMSO, urea, and GuHCl. PVCuZnSOD also shows great stability to gastrointestinal fluid compared with bovine SOD. These characteristics show that PVCuZnSOD has great application potential in medicine, food, and other products.
42006115 National Natural Science Foundation of China, 2020A1515110826 Guangdong Province Basic and Applied Basic Research Fund Project, LMM2021-5 Guangdong Key Laboratory of Marine Materia Medica, FEEL-2021-10 Fund of Guangdong Provincial Key Laboratory of Fishery Ecology and Environment
Figure 2. Multiple alignment of PVCuZnSOD with other SODs. The colors of shadow from dark to light represent the conservation of amino acid residues from high to low. Gaps are indicated by dashes to improve the alignment. The GenBank accession numbers are shown in Table 1. ‘*’ represents the terminator of the amino acid sequence. ‘$’ represents metal binding sites, the blue (PS00087) and red (PS00332) box represent motifs. ’#’ represents the two conserved cysteines.
Figure 1. Nucleotide and deduced amino acid sequences of PVCuZnSOD. The green underlines represent β sheets. The shaded part from Leu9 to Ile147 represents the predicted domain area.
Figure 3. Phylogenetic trees for PVCuZnSOD constructed by the neighbor-joining method based on the sequences from different animals. The PVCuZnSOD was highlight by the red box. The numbers before the branches (only display >50%) in the figure represent confidence. The Genbank accession numbers are shown in Table 1.
Figure 4. The three-dimensional model of the PVCuZnSOD. The yellow part is the metal binding site, and the red (PS00332) and blue (PS00087) part is the location of the motif. (A) 3D structure of PVCuZnSOD using the Swiss model. (B) Close-up of the active sites.
Figure 5. Expression and purification of PVCnZnSOD. (A) SDS-PAGE analysis of PVCuZnSOD. Lane M: marker. Lane 1: total protein of E. coli pCold II/BL21 containing recombinant plasmid before IPTG induction. Lane 2: total protein of E. coli pCold II/BL21 containing recombinant plasmid after IPTG induction. Lane 3: supernatant after ultrasonic treatment. Lane 4: purified recombinant protein. (B) Western blot analysis of PVCuZnSOD. Lane M: marker. Lane 1: purified recombinant protein.
Figure 6. Effect of temperature on activity of PVCuZnSOD. (A) Effect of temperature on activity of PVCuZnSOD. The dotted line represents the temperature at which the enzyme activity is highest. (B) Effect of temperature on stability of PVCuZnSOD.
Figure 7. Effect of pH on activity of PVCuZnSOD. The dotted line represents the pH corresponding to the highest enzymatic activity.
Figure 8. Effect of various treatments on the activity of PVCuZnSOD. * p < 0.05, ** p < 0.01 compared with the control group.
Figure 9. The effect of surfactants (A) and organic solvents (B). * p < 0.05, ** p < 0.01 compared with the control group.
Figure 10. The effect of urea and GuHCl. * p < 0.05, ** p < 0.01 compared with the control group.
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