Difference between revisions of "Part:BBa K2043008"
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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> | ||
| + | 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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<partinfo>BBa_K2043008 parameters</partinfo> | <partinfo>BBa_K2043008 parameters</partinfo> | ||
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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
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
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21INCOMPATIBLE WITH RFC[21]Illegal BglII site found at 699
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]