Difference between revisions of "Part:BBa K3051004"
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<partinfo>BBa_K3051004 short</partinfo> | <partinfo>BBa_K3051004 short</partinfo> | ||
− | https://2019.igem.org/wiki/images/archive/a/a1/20191020223854%21T--Warwick--CMLP_3D_structure.png | + | <p></p> |
+ | <h2>Comparative Enzyme Activity Assay</h2> | ||
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+ | <div align="center"><img height="50%" width="50%" src="https://2019.igem.org/wiki/images/8/83/T--Warwick--2019-EnzymeLipaseGraph.png"></img></div> | ||
+ | <p><b>Figure 1. Comparative Enzyme Activity Assay</b>Candida Antarctica Lipase A, Bacillus Subtilis Lipase and Serratia Marcescens Lipase enzyme activity were examined using p-Nitrophenol octanoate as a substrate.</p> | ||
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+ | The lipase parts were tested and characterized using a [https://2019.igem.org/Team:Warwick/Results p nitrophenol octanoate assay]. The enzyme activity was determined by measuring change in light absorbance at a wavelength of 400nm, which directly correlated to the concentration of p-Nitrophenol (pNP), caused by lipolysis of p-Nitrophenol octanoate (pNPO) substrate. The data from the pNPO lipolysis assay defined the enzyme activity. | ||
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+ | <p></p> | ||
+ | <h2>Structure and domains of Serratia Marcescens Lipase</h2> | ||
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+ | <html> | ||
+ | <div align="center"><img height="50%" width="50%" src="https://2019.igem.org/wiki/images/archive/a/a1/20191020223854%21T--Warwick--CMLP_3D_structure.png | ||
+ | "></img></div> | ||
+ | <p><b>Figure 2. Simulated 3D structure.</b>Structure of Serratia Marcescens Lipase simulated using Phyre 2 modelling.</p> | ||
+ | </html> | ||
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+ | <div> | ||
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Revision as of 23:55, 21 October 2019
Serratia Marcescens Lipase
Comparative Enzyme Activity Assay
![](https://2019.igem.org/wiki/images/8/83/T--Warwick--2019-EnzymeLipaseGraph.png)
Figure 1. Comparative Enzyme Activity AssayCandida Antarctica Lipase A, Bacillus Subtilis Lipase and Serratia Marcescens Lipase enzyme activity were examined using p-Nitrophenol octanoate as a substrate.
The lipase parts were tested and characterized using a p nitrophenol octanoate assay. The enzyme activity was determined by measuring change in light absorbance at a wavelength of 400nm, which directly correlated to the concentration of p-Nitrophenol (pNP), caused by lipolysis of p-Nitrophenol octanoate (pNPO) substrate. The data from the pNPO lipolysis assay defined the enzyme activity.
Structure and domains of Serratia Marcescens Lipase
![](https://2019.igem.org/wiki/images/archive/a/a1/20191020223854%21T--Warwick--CMLP_3D_structure.png
)
Figure 2. Simulated 3D structure.Structure of Serratia Marcescens Lipase simulated using Phyre 2 modelling.
Sequence and Features
- 10INCOMPATIBLE WITH RFC[10]Unknown
- 12INCOMPATIBLE WITH RFC[12]Unknown
- 21INCOMPATIBLE WITH RFC[21]Unknown
- 23INCOMPATIBLE WITH RFC[23]Unknown
- 25INCOMPATIBLE WITH RFC[25]Unknown
- 1000COMPATIBLE WITH RFC[1000]