Difference between revisions of "Part:BBa K3051004"
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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>
 
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<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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<p><b>Figure 1. Relative Comparatison 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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Revision as of 23:59, 21 October 2019


Serratia Marcescens Lipase

Comparative Enzyme Activity Assay

Figure 1. Relative Comparatison 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.

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]