Coding

Part:BBa_K5171000

Designed by: Anna Filindri   Group: iGEM24_Anatolia-College   (2024-10-02)


IsPETase-HiCutinase Fusion Enzyme

The IsPETase-HiCutinase Fusion Enzyme is a fusion enzyme in which PETase and cutinase are connected via the (GGGGS)3 flexible peptide linker. The enzyme PETase is derived from the bacterium Ideonella Sakaiensis and has the ability of biodegrading the plastic PET. The enzyme cutinase is derived from the fungus Humicola Insolens and has very similar abilities and optimum operating conditions to PETase and can also break down other aliphatic polyesters such as polylactic acid and polycaprolactone. The fusion enzyme we designed exhibits enhanced effectiveness in biodegradation through several key mechanisms: Firstly, the synergistic action of the two enzymes increases the biodegradation speed. Secondly the enzymes target different parts of PET molecules, increasing the efficiency of biodegradation as PETase can initially cleave PET into intermediates such as MHET, which can be further degraded by cutinase, facilitating faster degradation. Finally, PETase and cutinase can work sequentially, with PETase initiating degradation and cutinase accelerating the breakdown of intermediates, leading to faster overall degradation.

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
    INCOMPATIBLE WITH RFC[1000]
    Illegal SapI site found at 426


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