Part:BBa_K1291071

HORSERADISH PEROXIDASE TYPE C COMPOSITE PART

The enzyme horseradish peroxidase (HRP), found in the roots of plant horseradish, is used extensively in biochemistry applications primarily for its ability to amplify a weak signal and increase detectability of a target molecule. It is a metalloenzyme with many isoforms and the most studied type is C. This enzyme is primerly responsible for the degradation of industrial dyes such as Methylene Blue. The composite part starts off with the J23119 constitutive promoter, continues with the RBS which is followed by the Horseradish peroxidase coding region. The sequence ends with the terminators which come after the Histag region. There is the BamH1 enzyme restriction cite on the sequence before the RBS.

Sequence and Features

Assembly Compatibility:

• 10
  COMPATIBLE WITH RFC[10]
• 12
  INCOMPATIBLE WITH RFC[12]

  Illegal NheI site found at 7
  Illegal NheI site found at 30
  
• 21
  INCOMPATIBLE WITH RFC[21]

  Illegal BglII site found at 445
  
• 23
  COMPATIBLE WITH RFC[23]
• 25
  INCOMPATIBLE WITH RFC[25]

  Illegal NgoMIV site found at 565
  Illegal AgeI site found at 719
  Illegal AgeI site found at 1022
  
• 1000
  COMPATIBLE WITH RFC[1000]

Characterization and Improvement by REC-CHENNAI 2022

Part: BBa_K4509420

This existing part has a burden range of -0.6 ± 11.0% while the improved part with the promoter J23116 has a lesser burden range, thereby increasing cell growth.

The growth curve for the HRP plasmid with J23119, J23116, J23106 and J23100 is plotted in this graph. The burden on cells is indirectly proportional to cell viability. Looking at the growth curve it may be observed that the growth of J23116 is much more efficient than J23119. Thus the part has improved cell growth. J23100 and J23106 are used for comparison studies