Difference between revisions of "Part:BBa K2043008"

 
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bpuI-FBD1 codon optimized from Bacilus pumillus
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<h2>Description</h2>
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Laccases are commonly used enzymes for bleaching denim, as well as other textiles. They act in part by oxidizing phenolic compounds, offering a similar target to the phenol ring disrupting catalase enzymes also developed in this project (BBa_K2043001) (Reiss, 2011).<br>
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The <i>bpul</i> gene (<a href="https://parts.igem.org/Part:BBa_K2043007">Bba_K2043007</a>) codon optimized for <i>E. coli</i> was improved by addition of fabric binding domain 1 (FBD1) on the 3'-end of the sequence using Golden Gate assembly method. FBD1 is the first of 40 short peptides with affinity for cotton, linen, wool, polyester or silk identified in the <a href="http://2016.igem.org/Team:Paris_Bettencourt">Frank&Stain</a> project. It is positively charged (+1) and it is proline rich. We fused a fabric domain with <i>bpul</i> hoping to improve its function as stain removal. Unfortunately, this BioBrick was not tested for its activity due to a lack of time in iGEM competition. However, <a href="https://parts.igem.org/Part:BBa_K2043007">bpul</a> and <a href="https://parts.igem.org/Part:BBa_K2043008">FBD1</a> specifications can be found on their BioBrick pages
  
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<b>References</b><br>
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Reiss, R., Ihssen, J., & Thöny-Meyer, L. (2011). Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC biotechnology, 11(1), 1.
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===Usage and Biology===
 
===Usage and Biology===
 
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<span class='h3bb'>Sequence and Features</span>
 
<span class='h3bb'>Sequence and Features</span>
 
<partinfo>BBa_K2043008 SequenceAndFeatures</partinfo>
 
<partinfo>BBa_K2043008 SequenceAndFeatures</partinfo>
 
 
 
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===Functional Parameters===
 
===Functional Parameters===
 
<partinfo>BBa_K2043008 parameters</partinfo>
 
<partinfo>BBa_K2043008 parameters</partinfo>
 
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<h1>bpuI FBD1</h1>
 
 
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Latest revision as of 20:59, 27 October 2016

bpuI-FBD1 laccase codon optimized for E.coli

Description

Laccases are commonly used enzymes for bleaching denim, as well as other textiles. They act in part by oxidizing phenolic compounds, offering a similar target to the phenol ring disrupting catalase enzymes also developed in this project (BBa_K2043001) (Reiss, 2011).
The bpul gene (Bba_K2043007) codon optimized for E. coli was improved by addition of fabric binding domain 1 (FBD1) on the 3'-end of the sequence using Golden Gate assembly method. FBD1 is the first of 40 short peptides with affinity for cotton, linen, wool, polyester or silk identified in the Frank&Stain project. It is positively charged (+1) and it is proline rich. We fused a fabric domain with bpul hoping to improve its function as stain removal. Unfortunately, this BioBrick was not tested for its activity due to a lack of time in iGEM competition. However, bpul and FBD1 specifications can be found on their BioBrick pages

References
Reiss, R., Ihssen, J., & Thöny-Meyer, L. (2011). Bacillus pumilus laccase: a heat stable enzyme with a wide substrate spectrum. BMC biotechnology, 11(1), 1.


Sequence and Features


Assembly Compatibility:
  • 10
    COMPATIBLE WITH RFC[10]
  • 12
    COMPATIBLE WITH RFC[12]
  • 21
    INCOMPATIBLE WITH RFC[21]
    Illegal BglII site found at 699
  • 23
    COMPATIBLE WITH RFC[23]
  • 25
    COMPATIBLE WITH RFC[25]
  • 1000
    COMPATIBLE WITH RFC[1000]