Part:BBa_K2833014

J23104+B0032+INP+VHb+Ter

Previous research has found that expressing Vitreoscilla hemoglobin (VHb) inside the bacteria could leverage its property of combining and releasing oxygen to improve the efficiency of oxygen utilization and therefore enhance the efficiency of bacteria growth and production.^[1] Follow-up studies have shown that expressing VHb in the periplasmic space could further improve that efficiency compared with intracellular expression.^[2] Based on these, we proposed that expressing VHb outside the outer membrane using surface display system could further enhance the oxygen density surrounding the bacteria and improve oxygen utility in the system for further enhancement of the fermentation efficiency.

For surface display of VHb, we constructed this part to fuse the surface display protein INP(from BBa_K523013) to the N-terminal of the VHb protein.(figure 1)

Figure 1. The framework of BBa_K2833014

<p>We compared the growth curve of BBa_K2833014 transformed bacteria and empty vector transformed bacteria to see if the part works(figure 2).From this result we can see that the growth rate of INP-VHb transformed bacteria is higher than empty vector transformed bacteria.

Figure 2. The growth curve of INP-VHb expressed bacteria and empty vector transformed bacteria.

References

1.Lei Zhang et al.. Recent developments and future prospects of Vitreoscilla hemoglobin application in metabolic engineering. Biotechnology Advances 25(2007).</font>

2.Pengfei Ouyang et al.. Increasing oxygen availability for improving poly(3-hydroxybutyrate) production by Halomonas. Metabolic Engineering 45(2018).</font>

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal NheI site found at 7
  Illegal NheI site found at 30
  
• 21
  COMPATIBLE WITH RFC[21]
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 467
  
• 1000
  COMPATIBLE WITH RFC[1000]