Difference between revisions of "Part:BBa K3039001"
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| − | The enzymes PETase and MHETase were first discovered in <i>Ideonella sakaiensis</i> in 2016 by a group of researchers in Japan. These enzymes were found to degrade polyethylene terephthalate (PET) into its monomers, terephthalic acid (TPA) and ethylene glycol (EG). PETase degrades PET into Mono-(2-hydroxyethyl)terephthalic acid (MHET), Bis(2-Hydroxyethyl) terephthalate (BHET) and TPA, the main product being MHET. MHET is further degraded by MHETase into TPA and EG. We are aiming to use mutants of these enzymes to degrade the microfibres that are coming off clothing during washing cycles. The enzymes would be secreted into a filter that captures the microfibres. Different mutations that have been reported in past papers to increase the activity of PETase have been combined into a novel mutant, in order to test if this would result in an overly active mutant. This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the novel mutant of PETase, with an attached His tag. The His tag was attached in order to more easily identify the enzymes. | + | The enzymes PETase and MHETase were first discovered in <i>Ideonella sakaiensis</i> in 2016 by a group of researchers in Japan. These enzymes were found to degrade polyethylene terephthalate (PET) into its monomers, terephthalic acid (TPA) and ethylene glycol (EG). PETase degrades PET into Mono-(2-hydroxyethyl)terephthalic acid (MHET), Bis(2-Hydroxyethyl) terephthalate (BHET) and TPA, the main product being MHET. MHET is further degraded by MHETase into TPA and EG. We are aiming to use mutants of these enzymes to degrade the microfibres that are coming off clothing during washing cycles. The enzymes would be secreted into a filter that captures the microfibres. Different mutations that have been reported in past papers to increase the activity of PETase have been combined into a novel mutant, in order to test if this would result in an overly active mutant. This sequence is the <i>Escherichia coli</i> K12 (<i>E. coli</i> K12) codon optimized DNA of the novel mutant of PETase, with an attached His tag. The His tag was attached in order to more easily identify the enzymes. |
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Revision as of 11:23, 2 September 2019
PETase T88A_S121E_D186H_R280A
The enzymes PETase and MHETase were first discovered in Ideonella sakaiensis in 2016 by a group of researchers in Japan. These enzymes were found to degrade polyethylene terephthalate (PET) into its monomers, terephthalic acid (TPA) and ethylene glycol (EG). PETase degrades PET into Mono-(2-hydroxyethyl)terephthalic acid (MHET), Bis(2-Hydroxyethyl) terephthalate (BHET) and TPA, the main product being MHET. MHET is further degraded by MHETase into TPA and EG. We are aiming to use mutants of these enzymes to degrade the microfibres that are coming off clothing during washing cycles. The enzymes would be secreted into a filter that captures the microfibres. Different mutations that have been reported in past papers to increase the activity of PETase have been combined into a novel mutant, in order to test if this would result in an overly active mutant. This sequence is the Escherichia coli K12 (E. coli K12) codon optimized DNA of the novel mutant of PETase, with an attached His tag. The His tag was attached in order to more easily identify the enzymes.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal XhoI site found at 667
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]