Difference between revisions of "Part:BBa K2043008"

Revision as of 20:54, 27 October 2016 (view source) Jazon (Talk | contribs) ← Older edit		Latest revision as of 20:59, 27 October 2016 (view source) Jazon (Talk | contribs)
(One intermediate revision by the same user not shown)
Line 10:		Line 10:
	</p>		</p>
−	References<br>	+	<b>References</b><br>
	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.		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>
	</p>		</p>
	</html>		</html>

---

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

References
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