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
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]