Team:University College London/Module 3

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Latest revision as of 18:16, 26 September 2012

Description

As an alternative to the Aggregation system, we are developing another solution – Degradation of plastic. This will focus on Polyethylene degradation, for which numerous bacteria and fungi, naturally capable of this act, have been found. Certain multi-copper enzymes have been found to degrade polyethylene and polypropylene, and we are looking in particular at Laccase, the enzyme responsible for the polyethylene degrading properties in the previously mentioned bacteria and fungi.

Laccases in fact exhibit activity towards an ‘extraordinary’ range of substrates. This is due to the conserved copper binding sites that couple the oxidation reactions of a reducing susbtrate to the cleavage of a dioxygen bond. As such, the oxidoreductase is able to catalyse redox reactions for various substrates.

This suggests that the enzymatic activity of laccase oxidises the polyethylene macromolecule. As such, it is thought that a series of oxidation reactions catabolised by laccase is responsible for plastic degradation.

The laccase system (BBa_K729002) will be driven by a strong constitutive promoter (BBa_J23119) - we expect overexpression of the protein to allow laccase to leak into the extracellular medium.

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-= Module 3: Degradation =
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 == Description ==
-As an alternative to '''Island Formation''' Modules (Modules 1 and 2), we are also developing an alternative solution – '''Degradation''' of plastic. This will focus on '''Polyethylene''' degradation, for which numerous bacteria and fungi are capable of degrading.  Certain Multi-copper enzymes have been found to degrade Polyethylene and Polypropylene, and we are looking in particular at an enzyme called '''laccase''' that has been found to degrade Polyethylene in a number of bacteria and fungi.
+As an alternative to the Aggregation system, we are developing another solution – '''Degradation''' of plastic. This will focus on '''Polyethylene''' degradation, for which numerous bacteria and fungi, naturally capable of this act, have been found.  Certain multi-copper enzymes have been found to degrade polyethylene and polypropylene, and we are looking in particular at '''Laccase''', the enzyme responsible for the polyethylene degrading properties in the previously mentioned bacteria and fungi.
-The laccase system (BBa_K729002) will be driven by a strong '''constitutive''' promoter (BBa_J23119) which initiates the '''extracellular release''' of the laccase enzyme. Laccases in fact exhibit an ‘extraordinary’ range of substrates. It has conserved copper binding site that couple the  '''oxidation reactions''' of a reducing susbtrate to the cleavage of a dioxygen bond. This series of oxidation reactions can be used for plastic '''degradation'''.
+Laccases in fact exhibit activity towards an ‘extraordinary’ range of substrates. This is due to the conserved copper binding sites that couple the '''oxidation reactions''' of a reducing susbtrate to the cleavage of a dioxygen bond. As such, the oxidoreductase is able to catalyse redox reactions for various substrates.
+This suggests that the enzymatic activity of laccase oxidises the polyethylene macromolecule. As such, it is thought that a series of oxidation reactions catabolised by laccase is responsible for plastic '''degradation'''.
+The laccase system (BBa_K729002) will be driven by a strong constitutive promoter (BBa_J23119) - we expect '''overexpression''' of the protein to allow laccase to leak into the '''extracellular''' medium.
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