Part:BBa_K2043008
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]
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