Difference between revisions of "Part:BBa K1921001"

Line 17: Line 17:
 
<!-- -->
 
<!-- -->
 
===Usage===
 
===Usage===
PETase is dedicated to the role of PET degradation. Our subject of the competition for this year is to modify PETase and developing cell surface display. <br>
+
MHET is dedicated to the role of PET degradation. <br>
  
 
===Biology===
 
===Biology===
PETase was found from a kind of microorganism(Ideonella sakaiensis 201-F6) living on PET as the main carbon source. It can degrade macromolecular polymers into monomers.PETase is the only enzyme found in bacteria which can degrade PET. Compare to the other enzyme found in fungi like LCC, TfH, FsC, PETase is much more active under low temperature environment, which means its reaction conditions is feasible in practical application than the others'.Additionally, PETase has been shown to have a degrading efficiency 120 times greater than alternative enzymes.
+
Like PETase, MHETase is also discovered from Ideonella sakaiensis 201-F6, it is a enzyme which can hydrolyze MHET, which is the main product of PETase when hydrolyzing PET.
  
 
===Reference===
 
===Reference===
 +
[1] Kohei Oda, Shosuke Yoshida, et al. A bacterium that degrades and assimilates poly(ethylene terephthalate)[J]. Science. Vol 351. MARCH 2016: 1196-1199

Revision as of 17:05, 1 October 2016

MHETase


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
    INCOMPATIBLE WITH RFC[25]
    Illegal NgoMIV site found at 1027
    Illegal AgeI site found at 247
    Illegal AgeI site found at 364
  • 1000
    COMPATIBLE WITH RFC[1000]


Usage

MHET is dedicated to the role of PET degradation.

Biology

Like PETase, MHETase is also discovered from Ideonella sakaiensis 201-F6, it is a enzyme which can hydrolyze MHET, which is the main product of PETase when hydrolyzing PET.

Reference

[1] Kohei Oda, Shosuke Yoshida, et al. A bacterium that degrades and assimilates poly(ethylene terephthalate)[J]. Science. Vol 351. MARCH 2016: 1196-1199