Gribbles — why these wood-feasting microbial Vikings might be energy stars

June 10, 2013 |

The star enzyme itself

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The 3D X-ray structure allows scientists to see inside the enzyme and reveals how it binds and digests cellulose chains. 
Image: John McGeehan, University of Portsmouth

Dr Simon Cragg of the University of Portsmouth reports: “Enzymes of this type are common in fungi, but this is the first animal enzyme to be explored and it has much to teach us.”.

Dr McGeehan added: “Now we have the blueprint of this enzyme, we just need to copy it.T he 3D structure has revealed that although the skeleton of the gribble enzyme is very similar to the equivalent enzymes in fungi, the surface is unrecognisable. It appears that the consequence of evolution in a marine environment is an acidic coat that protects the enzyme from high concentrations of salt. This unusual salt tolerance and stability represent exciting properties with great potential benefit to industry.”

“The robust nature of the enzymes makes it compatible for use in conjunction with sea water, which would lower the costs of processing. Its robustness would also give the enzymes a longer working life and allow it to be recovered and re-used during processing.”

What’s the bottom line – we look at the implications and next steps, by clicking the page links below.

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