Difference between revisions of "Part:BBa K2043009"

Revision as of 20:58, 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.
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