Scientists accidentally engineer a plastic-eating enzyme



Prof. John McGeehan, an X-ray crystallographer at the University of Portsmouth, stands next to equipment at the Diamond Light Source, the United Kingdom national synchrotron, that he used to reveal the atomic structure of an enzyme his team has engineered to digest a common form of plastic.

In studying the plastic-eating enzyme that the bacterium produced, they were looking at how the enzyme evolved - in the process, a tweak to the enzyme revealed that they had inadvertently made it even better at breaking down the bottle plastic, PET (polyethylene terephthalate). PET can last hundreds of years in a natural environment.

Portsmouth University's Prof John McGeehan and Dr Gregg Beckham at NREL solved the crystal structure of PETase - an enzyme that digests PET- and used this 3D information to understand how it works.


Working with USA colleagues, the Portsmouth scientists subjected PETase to intense X-ray beams at the Diamond Light Source synchrotron facility in Harwell, Oxfordshire.

The mutant enzyme takes a few days to start breaking down the plastic and experts have said that they're confident the process can be accelerated even further into a large scale process. A computer modeling of PETase showed that it resembles another enzyme found in fungus and bacteria, the cutinase. During this work, they inadvertently engineered an enzyme that is better still at degrading the plastic than the one that evolved in nature.

The researchers found that the PETase mutant was better than the natural PETase in degrading PET.

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However, Ideonella sakaiensis on its own is not useful in industrial recycling on its own as it digests plastic too slowly.

'What we are hoping to do is use this enzyme to turn this plastic back into its original components, so we can literally recycle it back to plastic, ' Prof John McGeehan, at the University of Portsmouth, told The Guardian.

The engineered enzyme has the added benefit of being able to degrade polyethylene furandicarboxylate (PEF), a PET alternative that has been floated as a replacement for glass beer bottles.

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This suggested that PETase had evolved in an environment with PET present, so the researchers mutated the PETase active site to behave more like cutinase, in search of more evidence of this theory.

PET is relatively easy to recycle, but over half of global PET waste is not collected for recycling, according to research from the Ellen MacArthur Foundation, and only 7 percent of bottles are recycled into new bottles (most go into lower-value products).

"The engineering process is much the same as for enzymes now being used in bio-washing detergents and in the manufacture of biofuels ― the technology exists", said McGeehan. "But the scientific community who ultimately created these 'wonder-materials, ' must now use all the technology at their disposal to develop real solutions".

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Now however, The Guardian is reporting that the discovery of an enzyme in a Japanese dump in 2016 has now reaped dividends enormously thanks to an accidental breakthrough made by a team of scientists from the University of Portsmouth, UK.

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