Scientists accidentally create mutant enzyme that eats plastic bottles

Scientists accidentally create mutant enzyme that eats plastic bottles

Scientists have created a mutant enzyme that breaks down plastic drinks bottles – by accident. The breakthrough could help solve the global plastic pollution crisis by enabling for the first time the full recycling of bottles.

The new research was spurred by the discovery in 2016 of the first bacterium that had naturally evolved to eat plastic, at a waste dump in Japan. Scientists have now revealed the detailed structure of the crucial enzyme produced by the bug.

The international team then tweaked the enzyme to see how it had evolved, but tests showed they had inadvertently made the molecule even better at breaking down the PET (polyethylene terephthalate) plastic used for soft drink bottles. “What actually turned out was we improved the enzyme, which was a bit of a shock,” said Prof John McGeehan, at the University of Portsmouth, UK, who led the research. “It’s great and a real finding.”

The mutant enzyme takes a few days to start breaking down the plastic – far faster than the centuries it takes in the oceans. But the researchers are optimistic this can be speeded up even further and become a viable large-scale process.

“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,” said McGeehan. “It means we won’t need to dig up any more oil and, fundamentally, it should reduce the amount of plastic in the environment.”

About 1m plastic bottles are sold each minute around the globe and, with just 14% recycled, many end up in the oceans where they have polluted even the remotest parts, harming marine life and potentially people who eat seafood. “It is incredibly resistant to degradation. Some of those images are horrific,” said McGeehan. “It is one of these wonder materials that has been made a little bit too well.”

However, currently even those bottles that are recycled can only be turned into opaque fibres for clothing or carpets. The new enzyme indicates a way to recycle clear plastic bottles back into clear plastic bottles, which could slash the need to produce new plastic.

“You are always up against the fact that oil is cheap, so virgin PET is cheap,” said McGeehan. “It is so easy for manufacturers to generate more of that stuff, rather than even try to recycle. But I believe there is a public driver here: perception is changing so much that companies are starting to look at how they can properly recycle these.”

Quick guide

What are PET plastics?

PET – or polyethylene terephthalate – is the most common plastic used for soft drinks bottles. This is because it is lightweight, shatterproof, easy to mould and colour and cheap to produce. The key raw material is oil. PET in a different form is also used in clothing, where it is called polyester.

The estimated recycling rates for PET bottles vary significantly around the world, from 31% in the US, to 48% in Europe, 72% in Japan and 90% in India, where rag pickers collect the bottles to sell to waste traders. Deposit return schemes are very successful in some countries. But, globally, many bottles end polluting the environment.

PET bottles that are recycled have to be cleaned, sorted by colour, then shredded and dried to produce PET flakes. These can then be used to make new plastic but, due to impurities, it is not usually possible to make new, clear PET bottles. Instead, recycled bottles are mostly used to make polyester fibres.

The new research, published in the journal Proceedings of the National Academy of Sciences, began by determining the precise structure of the enzyme produced by the Japanese bug. The team used the Diamond Light Source, near Oxford, UK, an intense beam of X-rays that is 10bn times brighter than the sun and can reveal individual atoms.

The structure of the enzyme looked very similar to one evolved by many bacteria to break down cutin, a natural polymer used as a protective coating by plants. But when the team manipulated the enzyme to explore this connection, they accidentally improved its ability to eat PET.

“It is a modest improvement – 20% better – but that is not the point,” said McGeehan. “It’s incredible because it tells us that the enzyme is not yet optimised. It gives us scope to use all the technology used in other enzyme development for years and years and make a super-fast enzyme.”

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