Difference between revisions of "Part:BBa K2833014"
 
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<partinfo>BBa_K2833014 short</partinfo>
 
<partinfo>BBa_K2833014 short</partinfo>
  
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Ice nucleation protein(INP)is a secretory outer membrane protein from Pseudomomas syringae，P． flurorescens and several other Gram—negative bacteria．Using its characteristic of forming ice nucleation at relatively warm temperatures(一2～一4‘C)，INP is originally applied in biological refrigeration field．In the bacterial surface display technology，INP is widely used as a functional carrier protein．Compared with other carrier proteins，INP has advantages such as stably expressing foreign proteins and showing the larger molecular weight proteins．INP cell—sur— face display technology has been developed tO be a promising approach in many biotechn0109ical fields，such as whole cell bioeatalysts，whole cell bioadsorbence and biodegradation of environmental pollutants．
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<p>Previous research has found that expressing <i>Vitreoscilla</i> 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.<sup>[1]</sup> Follow-up studies have shown that expressing VHb in the periplasmic space could further improve that efficiency compared with intracellular expression.<sup>[2]</sup> 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.</p>
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<p>For surface display of VHb, we constructed this part to fuse the surface display protein INP(from <html><a href='https://parts.igem.org/Part:BBa_K523013'>BBa_K523013</a></html>) to the N-terminal of the VHb protein.(figure 1)
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Vitreoscilla haemoglobin (VHb) is a type of haemoglobin found in the Gram-negative aerobic bacterium, Vitreoscilla. It is the first haemoglobin discovered from bacteria, but unlike classic hemoglobin it is composed only of a single globin molecule. Sequence and Features
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[[File:T--BJRS China--014.jpg|thumbnail|center|800px|<b>Figure 1. The framework of BBa_K2833014</b>]]<br><br>
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<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.</p>
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[[File:T--BJRS China--demo3.jpg|thumbnail|center|800px|<b>Figure 2. The growth curve of INP-VHb expressed bacteria and empty vector transformed bacteria.
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</b>]]<br><br>
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===References===
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<p>1.Lei Zhang <i>et al.</i>. Recent developments and future prospects of <i>Vitreoscilla</i> hemoglobin application in metabolic engineering. <i>Biotechnology Advances</i> <b>25</b>(2007).</font></p>
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<p>2.Pengfei Ouyang <i>et al.</i>. Increasing oxygen availability for improving poly(3-hydroxybutyrate) production by <i>Halomonas</i>. <i>Metabolic Engineering</i> <b>45</b>(2018).</font></p>
  
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 10:42, 17 October 2018


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]