Difference between revisions of "Part:BBa K3051004"
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− | Figure 1 compares enzyme activity of Candida Antarctica Lipase A <bbpart>BBa_K3051001</bbpart>, Bacillus Subtilis Lipase <bbpart>BBa_K3051005</bbpart> and Serratia Marcescens Lipase <bbpart>BBa_K3051004</bbpart>. | + | Figure 1 compares enzyme activity of Candida Antarctica Lipase A <bbpart>BBa_K3051001</bbpart>, Bacillus Subtilis Lipase <bbpart>BBa_K3051005</bbpart> and Serratia Marcescens Lipase <bbpart>BBa_K3051004</bbpart>. 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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− | 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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Latest revision as of 00:05, 22 October 2019
Serratia Marcescens Lipase
Comparative Enzyme Activity Assay
![](https://2019.igem.org/wiki/images/8/83/T--Warwick--2019-EnzymeLipaseGraph.png)
Figure 1. Relative Comparaison Lipase Activity Assay. Candida Antarctica Lipase A, Bacillus Subtilis Lipase and Serratia Marcescens Lipase enzyme activity were examined using p-Nitrophenol octanoate as a substrate.
Figure 1 compares enzyme activity of Candida Antarctica Lipase A BBa_K3051001, Bacillus Subtilis Lipase BBa_K3051005 and Serratia Marcescens Lipase BBa_K3051004. 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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]