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: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 (FBD10) on the 5'-end of the sequence using Golden Gate assembly method. FBD10 is the positive control obtained from literature with affinity for cellulose. This 7 amino acid sequence was obtained by the phage display technique. They screened for small peptide ligands that selectively bind to the Cellulose nano whiskers. These peptides were selected on the target by bio-panning, by which a pool of randomized peptides were screened based on the binding affinity to cellulose. After three round of bio-panning, a consensus peptide sequence of “WHWRAWY” was found to efficiently bind to cellulose. | ||
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<br><br> | <br><br> | ||
| − | + | <b>References</b><br> | |
| − | 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. | + | 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.<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.<br> | ||
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| + | Guo, Jing, et al. "Identification and characterization of a cellulose binding heptapeptide revealed by phage display." Biomacromolecules 14.6 (2013): 1795-1805. | ||
| + | <br> | ||
</p> | </p> | ||
Latest revision as of 04:30, 28 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 (FBD10) on the 5'-end of the sequence using Golden Gate assembly method. FBD10 is the positive control obtained from literature with affinity for cellulose. This 7 amino acid sequence was obtained by the phage display technique. They screened for small peptide ligands that selectively bind to the Cellulose nano whiskers. These peptides were selected on the target by bio-panning, by which a pool of randomized peptides were screened based on the binding affinity to cellulose. After three round of bio-panning, a consensus peptide sequence of “WHWRAWY” was found to efficiently bind to cellulose.
References
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.
Guo, Jing, et al. "Identification and characterization of a cellulose binding heptapeptide revealed by phage display." Biomacromolecules 14.6 (2013): 1795-1805.
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]