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    RETURN OF WORLD'S LARGEST FLOOD PREVENTION EVENT TO BIRMINGHAM NEC

    On the 11th & 12th of September, the world’s largest flood prevention exhibition and conference will be returning to the Birmingham NEC.

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     Sobye Trial Success

    The ‘Sobye’ self-cleaning belt filter from Jacopa’s Swedish manufacturing partner, Nordic Water provides an automatic, compact solution for primary treatment to replace settlement tanks. The filter has recently undergone extremely successful trials at a unique Scottish Water test facility demonstrating excellent process performance and proving the effectiveness of the system.

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    Groundbreaking SuDS Material Tackles Highway Metals Pollution

    A groundbreaking new sustainable drainage material has addressed the challenge of removing toxic heavy metals pollution from highway runoff with a versatile solution that will be simple for highways authorities to incorporate into roadside schemes, writes SDS Market Development Manager, Jo Bradley.

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    Casella launches intrinsically safe low flow pump for chemical exposure monitoring

    Casella, air sampling, noise and vibration specialist, has launched its advanced and lightweight low flow pump, the VAPex Pro. The elite low flow pump is the ideal solution for seamless reporting on employee's levels of chemical exposure, saving occupational hygienists' crucial time in their working day.

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Tuesday, 17 April 2018 12:20

Hope for planet as scientists engineer enzyme that eats plastic bottles

Bottles made of plastic that persist in the environment for hundreds of years could become a pollution of the past thanks to the discovery of an enzyme that eats the substance, and work by scientists to further improve it by engineering.

plastic enzyme PETase copyThe discovery could result in a recycling solution for millions of tonnes of plastic bottles, made of polyethylene terephthalate, or PET.

The research was led by teams at England's University of Portsmouth and the US Department of Energy's National Renewable Energy Laboratory (NREL) and is published in Proceedings of the National Academy of Sciences (PNAS).

Professor John McGeehan at the University of Portsmouth and Dr Gregg Beckham at NREL solved the crystal structure of PETase—a recently discovered enzyme that digests PET— and used this 3D information to understand how it works. During this study, they inadvertently engineered an enzyme that is even better at degrading the plastic than the one that evolved in nature.

The researchers are now working on improving the enzyme further to allow it to be used industrially to break down plastics in a fraction of the time.

Professor McGeehan, Director of the Institute of Biological and Biomedical Sciences in the School of Biological Sciences at Portsmouth, said: "Few could have predicted that since plastics became popular in the 1960s huge plastic waste patches would be found floating in oceans, or washed up on once pristine beaches all over the world.

plastic enzyme McGEEHAN copy"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 researchers made the breakthrough when they were examining the structure of a natural enzyme which is thought to have evolved in a waste recycling centre in Japan, allowing a bacterium to degrade plastic as a food source.

PET, patented as a plastic in the 1940s, has not existed in nature for very long, so the team set out to determine how the enzyme evolved and if it might be possible to improve it.

Plastic enzyme pollution in oceans1The goal was to determine its structure, but they ended up going a step further and accidentally engineered an enzyme which was even better at breaking down PET plastics.

"Serendipity often plays a significant role in fundamental scientific research and our discovery here is no exception," Professor McGeehan said.

"Although the improvement is modest, this unanticipated discovery suggests that there is room to further improve these enzymes, moving us closer to a recycling solution for the ever-growing mountain of discarded plastics."

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

The University of Portsmouth and NREL collaborated with scientists at the Diamond Light Source in the United Kingdom, a synchrotron that uses intense beams of X-rays 10 billion times brighter than the sun to act as a microscope powerful enough to see individual atoms.

Aerial view of Diamond. Image courtesy Diamond Light Source copyUsing their latest laboratory, beamline I23, an ultra-high-resolution 3D model of the PETase enzyme was generated in exquisite detail.

Professor McGeehan said: "The Diamond Light Source recently created one of the most advanced X-ray beamlines in the world and having access to this facility allowed us to see the 3D atomic structure of PETase in incredible detail. Being able to see the inner workings of this biological catalyst provided us with the blueprints to engineer a faster and more efficient enzyme."

Chief Executive of the Diamond Light Source, Professor Andrew Harrison, said: "With input from five institutions in three different countries, this research is a fine example of how international collaboration can help make significant scientific breakthroughs.

"The detail that the team were able to draw out from the results achieved on the I23 beamline at Diamond will be invaluable in looking to tailor the enzyme for use in large-scale industrial recycling processes. The impact of such an innovative solution to plastic waste would be global. It is fantastic that UK scientists and facilities are helping to lead the way."

With help from the computational modeling scientists at the University of South Florida and the University of Campinas in Brazil, the team discovered that PETase looks very similar to a cutinase, but it has some unusual features including a more open active site, able to accommodate man-made rather than natural polymers. These differences indicated that PETase may have evolved in a PET-containing environment to enable the enzyme to degrade PET. To test that hypothesis, the researchers mutated the PETase active site to make it more like a cutinase.

plastci enzyme reaction copyAnd that was when the unexpected happened – the researchers found that the PETase mutant was better than the natural PETase in degrading PET.

Significantly, the enzyme can also degrade polyethylene furandicarboxylate, or PEF, a bio-based substitute for PET plastics that is being hailed as a replacement for glass beer bottles.

Professor McGeehan said: "The engineering process is much the same as for enzymes currently being used in bio-washing detergents and in the manufacture of biofuels – the technology exists and it's well within the possibility that in the coming years we will see an industrially viable process to turn PET and potentially other substrates like PEF, PLA, and PBS, back into their original building blocks so that they can be sustainably recycled."

The paper's lead author is a postgraduate student jointly funded by the University of Portsmouth and NREL, Harry Austin.

He said: "This research is just the beginning and there is much more to be done in this area. I am delighted to be part of an international team that is tackling one of the biggest problems facing our planet."

Responding to news that scientists have engineered an enzyme which can digest some of the most common polluting plastics, A Plastic Planet co-founder Sian Sutherland said: "Plastic pollution is an insidious nightmare that harms us all. There are 6.3 billion tonnes of plastic waste already on the planet, much of which is either at the bottom of landfill or floating in our oceans.

Plastic enzyme pollution on beach2 "While we applaud all scientific developments that look to help us deal with plastic pollution, the only viable answer to stopping the plastic problem is by turning off the tap.

"In 1950 the world produced 2 million tonnes of plastic each year, now we produce over 330 million tonnes. That number is set to treble by 2050 to close to a billion tonnes a year.

"We can't afford to rely on developing enzymes to let us off the hook. Our collective addition to plastic is wrecking the earth, and only a dramatic transformation in how we relate to plastic will solve the problem. The answer has to come from us. We have to change.

"It makes little sense to see something as fleeting as food encased in something as indestructible as plastic. That is why we will continue to call for a Plastic Free Aisle in all supermarkets to stem the flow of plastic pollution."