Difference between revisions of "Part:BBa K2010999"
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This graph demonstrates PETase activity as a function of pH. PETase is most active at a pH of 9.0. | This graph demonstrates PETase activity as a function of pH. PETase is most active at a pH of 9.0. | ||
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Revision as of 00:42, 22 October 2019
PETase (PET-degrading enzyme, origin I. sakaiensis)
PETase is a poly(ethylene terehphthalate)-degrading enzyme first identified in Ideonella sakaiensis. BBa_K2010999 is the sequence for the E. coli K12 optimized DNA sequence for PETase. The catalytic activity of IsPETase can be characterized using a p-nitrophenol butyrate (pNPB) assay, in which PETase cleaves the ester bond of pNPB to release p-nitrophenolate. The absorbance of this compound can be measured at 405 nm to reflect IsPETase activity.
An SDS-PAGE gel demonstrates successful protein purification of PETase, which has a molecular weight of approximately 30 kDa.
This graph demonstrates PETase activity with various substrate concentrations at a pH of 7.0.
This graph demonstrates PETase activity with various substrate concentrations at a pH of 8.0.
This graph demonstrates PETase activity with various substrate concentrations at a pH of 9.0.
This graph demonstrates PETase activity as a function of pH. PETase is most active at a pH of 9.0.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12INCOMPATIBLE WITH RFC[12]Illegal NotI site found at 67
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]