Difference between revisions of "Part:BBa K3759019"
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===Usage===
 
===Usage===
  
 +
It has been well known that the surface of PET film is hydrophobic, and the surface of mLCC is hydrophilic. By constructing the mLCC-linker-BsLA fusion protein, the PET degradation efficiency will be enhanced enormously, due to the unique properties of amphiphilicity and self-assembly of hydrophobin BslA. Also, as BslA was extracted from bacteria and was a bacterial hydrophobin, it shows a better fusion with mLCC, which help the increment of the PET degradation efficiency of mLCC-linker-BslA.
  
 +
===Biology===
  
−
 
+
LCC is a leaf-branch compost cutinase[1] and a kinetically robust protein[2]. A research published on Nature came up with a mutant enzyme, mLCC[1] that hydrolyzes 90% of PET in plastic bottles in just 10 hours. This is more efficient than any previous PET hydrolase, and more importantly, the resulting monomers- ethylene glycol and terephthalic acid have the same properties as the monomers found in petrochemical materials.
 
<!-- Add more about the biology of this part here
 
<!-- Add more about the biology of this part here
 
===Usage and Biology===
 
===Usage and Biology===

Revision as of 03:35, 18 October 2021


mLCC-linker-BsLA

Sequence and Features


Assembly Compatibility:
  • 10
    INCOMPATIBLE WITH RFC[10]
    Illegal EcoRI site found at 261
    Illegal EcoRI site found at 1079
  • 12
    INCOMPATIBLE WITH RFC[12]
    Illegal EcoRI site found at 261
    Illegal EcoRI site found at 1079
    Illegal NheI site found at 193
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal EcoRI site found at 261
    Illegal EcoRI site found at 1079
  • 23
    INCOMPATIBLE WITH RFC[23]
    Illegal EcoRI site found at 261
    Illegal EcoRI site found at 1079
  • 25
    INCOMPATIBLE WITH RFC[25]
    Illegal EcoRI site found at 261
    Illegal EcoRI site found at 1079
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage

It has been well known that the surface of PET film is hydrophobic, and the surface of mLCC is hydrophilic. By constructing the mLCC-linker-BsLA fusion protein, the PET degradation efficiency will be enhanced enormously, due to the unique properties of amphiphilicity and self-assembly of hydrophobin BslA. Also, as BslA was extracted from bacteria and was a bacterial hydrophobin, it shows a better fusion with mLCC, which help the increment of the PET degradation efficiency of mLCC-linker-BslA.

Biology

LCC is a leaf-branch compost cutinase[1] and a kinetically robust protein[2]. A research published on Nature came up with a mutant enzyme, mLCC[1] that hydrolyzes 90% of PET in plastic bottles in just 10 hours. This is more efficient than any previous PET hydrolase, and more importantly, the resulting monomers- ethylene glycol and terephthalic acid have the same properties as the monomers found in petrochemical materials.