Tuesday, 24 April, 2018

Scientists Create Enzyme That Eats Plastic Bottles

10-metre installation depicting a whale created by “Sky Ocean Rescue-A Sea to Save” and made up of 250 kg of plastic waste in front of the Auditorium Parco della Musica in central Rome Scientists Discover Enzyme That Eats The Worst Polluting Plastics
Preston Stone | 17 April, 2018, 14:16

With the hope of developing a solution to the world's chronic plastic pollution problem, British and American researchers chose to study the enzyme that the bacteria were using to digest this ubiquitous substance-and now they've made a stunning discovery.

Downing Street said £25 million of the fund will be used to help researchers investigate the issue of marine plastic from a scientific, economic and social perspective.

Known as Ideonella sakaiensis, it appears to feed exclusively on a type of plastic known as polyethylene terephthalate (PET), used widely in plastic bottles.

While the mutant PETase is so far only about 20 percent more efficient at breaking down plastic than the naturally occurring enzyme, the team says the important thing is we now know these enzymes can be optimised and augmented.

The worldwide team, led by Professor John McGeehan of the University of Portsmouth, UK, tested the evolutionary process of the enzyme, inadvertently discovering that they had improved the capabilities of the enzyme in breaking down PET bottles.

Now the researchers are trying to improve the new enzyme so they can put it to work eating up all the plastic out there.

At the moment PET takes hundreds of years to break down in the natural environment and is a major contributor to land and sea pollution.

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That's a problem, given the vast scale of plastic pollution on the planet, with billions of tonnes of discarded waste piling up in landfills and spilling into our oceans, where it even threatens to crowd out fish - seriously.

"We can all play a significant part in dealing with the plastic problem, but the scientific community who ultimately created these "wonder materials" must now use all the technology at their disposal to develop real solutions".

The structure was found to be very similar to that of the bacteria capable of breaking-down cutin, a natural polymer used as a protective coating by plants.

The research team can now apply the tools of protein engineering and evolution to continue to improve it.

The researchers set out to better understand the crystalline structure of PETase, which is believed to have come of age in a Japanese recycling center.

One possible improvement being explored is to transplant the mutant enzyme into an "extremophile bacteria" that can survive temperatures above the 70C melting point of PET - the plastic is likely to degrade 10-100 times faster when molten. The enzyme can also degrade polyethylene furandicarboxylate (PEF), a bio-based substitute for PET plastics that is being hailed as a replacement for glass beer bottles. To test their theory they then mutated the PETease to make it look even more like a cutinase.

"It's well within the possibility that in the coming years we will see an industrially viable process to turn PET, and potentially other (plastics), back into their original building blocks so that they can be sustainably recycled", McGeehan said.

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