Difference between revisions of "Part:BBa K2043009"
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<h2>Description</h2> | <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 (<a href="https://parts.igem.org/Part: | + | 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 (<a href="https://parts.igem.org/Part:BBa_K2043001">Bba_K2043001</a>) (Reiss, 2011).<br> |
The bpul 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 10 (FBD1) on the 3'-end of the sequence using Golden Gate assembly method. FBD10 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. FBD10 is reported to have binding affinity for cotton (Goldstein 1993). 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 | The bpul 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 10 (FBD1) on the 3'-end of the sequence using Golden Gate assembly method. FBD10 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. FBD10 is reported to have binding affinity for cotton (Goldstein 1993). 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 | ||
Revision as of 20:57, 27 October 2016
bpuI-FBD10 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 10 (FBD1) on the 3'-end of the sequence using Golden Gate assembly method. FBD10 is the first of 40 short peptides with affinity for cotton, linen, wool, polyester or silk identified in the Frank&Stain project. FBD10 is reported to have binding affinity for cotton (Goldstein 1993). 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
Reference
Goldstein, MARC A., et al. "Characterization of the cellulose-binding domain of the Clostridium cellulovorans cellulose-binding protein A." Journal of bacteriology 175.18 (1993): 5762-5768.
Sequence and Features
- 10COMPATIBLE WITH RFC[10]
- 12COMPATIBLE WITH RFC[12]
- 21COMPATIBLE WITH RFC[21]
- 23COMPATIBLE WITH RFC[23]
- 25COMPATIBLE WITH RFC[25]
- 1000COMPATIBLE WITH RFC[1000]