Difference between revisions of "Part:BBa K3051004"
 
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<partinfo>BBa_K3051004 short</partinfo>
 
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<h2>Comparative Enzyme Activity Assay</h2>
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<div align="center"><img height="85%" width="85%" src="https://2019.igem.org/wiki/images/8/83/T--Warwick--2019-EnzymeLipaseGraph.png"></img></div>
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<p><b>Figure 1. Relative Comparaison Lipase 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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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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<h2>Structure and domains of Serratia Marcescens Lipase</h2>
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<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
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<p><b>Figure 2. Simulated 3D structure.</b>Structure of Serratia Marcescens Lipase simulated using Phyre 2 modelling.</p>
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<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here

Latest revision as of 00:05, 22 October 2019


Serratia Marcescens Lipase

Comparative Enzyme Activity Assay

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

Figure 2. Simulated 3D structure.Structure of Serratia Marcescens Lipase simulated using Phyre 2 modelling.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    COMPATIBLE WITH RFC[21]
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]