Team:University College London/Bibliography/C208

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Revision as of 10:28, 24 August 2012

"The role of the copper-binding enzyme – laccase – in the biodegradation of polyethylene by the actinomycete Rhodococcus ruber"
(Santo, M., Weitsman, R., & Sivan, A, et al. International Biodeterioration & Biodegradation. 2012;208:1-7)
This paper summarises the discovery that laccase produced by Rhodococcus Ruber C208 has been found to have polyethylene degrading properties. It suggests that laccase catalyses the oxidation of polyethylene, leading to its degradation.
<a href="http://www.sciencedirect.com/science/article/pii/S0964830512000637" title="Reference Link" target="_blank">Paper on ScienceDirect</a>

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 <strong>"The role of the copper-binding enzyme – laccase – in the biodegradation of polyethylene by the actinomycete Rhodococcus ruber"<br /> (Santo, M., Weitsman, R., & Sivan, A, et al. International Biodeterioration & Biodegradation. 2012;208:1-7)</strong><br />
-While the paper does not directly analyse the binding of curlis to plastics, the data generated by the paper indicates the necessity of curlis for plastic adherence. The paper correlates the expression of curlis via congo red dye, with the binding of cells to plastic.<br />
+This paper summarises the discovery that laccase produced by ''Rhodococcus Ruber'' C208 has been found to have polyethylene degrading properties. It suggests that laccase catalyses the oxidation of polyethylene, leading to its degradation.<br />
 <a href="http://www.sciencedirect.com/science/article/pii/S0964830512000637" title="Reference Link" target="_blank">Paper on ScienceDirect</a>