Difference between revisions of "Part:BBa K5291003"
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<i>vgb</i> encodes VHb. VHb, the first discovered bacterial hemoglobin, is a soluble heme-binding protein with a faster rate of oxygen dissociation. It can enhance cell growth, product synthesis and stress tolerance. Especially under oxygen-limited conditions, VHb can interact with terminal oxidase to deliver enough oxygen to improve the degradation ability of CYPY96F on PE. | <i>vgb</i> encodes VHb. VHb, the first discovered bacterial hemoglobin, is a soluble heme-binding protein with a faster rate of oxygen dissociation. It can enhance cell growth, product synthesis and stress tolerance. Especially under oxygen-limited conditions, VHb can interact with terminal oxidase to deliver enough oxygen to improve the degradation ability of CYPY96F on PE. | ||
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===Usage and Biology=== | ===Usage and Biology=== | ||
| − | In degradation module we constructed pAB1-CYPY96F- | + | In degradation module we constructed pAB1-CYPY96F-VHb to accelerate the degradation rate by improving the absorbing and hydroxylation of PE monomer.<br> |
| − | <html><img width = " | + | <html><img width = "600" src="https://static.igem.wiki/teams/5291/images/part-wyn/pab1-cypy96f-vhb-plasmid.png" /></html><br> |
| − | <b>Fig.1 The map of plasmid pAB1-CYPY96F-VHB.</b><br><br> | + | <b>Fig.1 The map of plasmid pAB1-CYPY96F-VHb.</b><br><br> |
| − | Moreover, | + | |
| − | <html><img width = "500" src="https://static.igem.wiki/teams/5291/images/part-wyn/sds- | + | We transferred the constructed plasmid into <i>Escherichia coli</i> DH5α strain, conducted colony PCR and obtained the correct result. |
| − | <b>Fig. | + | <html><img width = "300" src="https://static.igem.wiki/teams/5291/images/part-wyn/gel-vhb-white.png" /></html><br> |
| − | Since we set CYPY96F and | + | <b>Fig.2 P.aeryginosa PAO1 colony PCR results of CYPY96F-VHB.</b><br><br> |
| + | |||
| + | Moreover,VHb proteins was successfully expressed in the strains. SDS-PAGE was performed and the following results were obtained.<br> | ||
| + | <html><img width = "500" src="https://static.igem.wiki/teams/5291/images/part-wyn/sds-vhb-white.png" /></html><br> | ||
| + | <b>Fig.3 The SDS-PAGE result of VHb.</b><br><br> | ||
| + | Since we set CYPY96F and VHb as a whole, the overall functions need moving to the part BBa_K5291034.<br> | ||
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Latest revision as of 05:06, 2 October 2024
vgb: Vitreoscilla hemoglobin
vgb encodes VHb. VHb, the first discovered bacterial hemoglobin, is a soluble heme-binding protein with a faster rate of oxygen dissociation. It can enhance cell growth, product synthesis and stress tolerance. Especially under oxygen-limited conditions, VHb can interact with terminal oxidase to deliver enough oxygen to improve the degradation ability of CYPY96F on PE.
Usage and Biology
In degradation module we constructed pAB1-CYPY96F-VHb to accelerate the degradation rate by improving the absorbing and hydroxylation of PE monomer.
Fig.1 The map of plasmid pAB1-CYPY96F-VHb.
We transferred the constructed plasmid into Escherichia coli DH5α strain, conducted colony PCR and obtained the correct result.
Fig.2 P.aeryginosa PAO1 colony PCR results of CYPY96F-VHB.
Moreover,VHb proteins was successfully expressed in the strains. SDS-PAGE was performed and the following results were obtained.
Fig.3 The SDS-PAGE result of VHb.
Since we set CYPY96F and VHb as a whole, the overall functions need moving to the part BBa_K5291034.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]