Plastic-eating Enzyme ‘Cocktail’ Provides Potential Plastic Waste Solution
A plastic-eating enzyme ‘cocktail’ has been created by scientists who re-engineered the plastic-eating enzyme PETase, according to the study reported in the Proceedings of the National Academy of Sciences Journal.
In order to fasten the process of breaking plastic, PETase is combined with a second enzyme, found in the same rubbish dwelling bacterium that consumes plastic bottles for its diet.
An opportunity for reducing plastic pollution to a great extent and reducing the greenhouse gases driving climate change is created with this research study which enables the endless recycling of plastic as PETase and the new combined MHETase-PETase together breakdown plastic back into its building blocks by digesting polyethylene terephthalate (PET).
Polyethylene terephthalate or PET is the common most thermoplastic. It is used in the manufacture of single-use drinks bottles, carpets, clothing, and so on. The degradation time of PET, which could take hundreds of years, can be reduced to days with the help of PETase.
A revolution in plastic recycling was set with the initial discovery of the team when they created the natural PETase enzyme in the laboratory to be around 20% quicker at breaking down PET, which gave rise to a potential low-energy solution for tackling plastic waste.
In order to create greater improvements, the same research team has now combined a second enzyme called MHETase to PETase as its ‘partner’. The speed of PET breakdown was doubled by simply mixing PETase with MHETase. This activity was further increased by three times to create a ‘super-enzyme’ by setting up a connection between the two enzymes.
The researchers who engineered PETase, Dr. Gregg Beckham, and Professor John McGeehan from the National Renewable Energy Laboratory (NREL) in the United States, and the University of Portsmouth respectively, co-led the research team.
Professor McGeehan said that they wanted to see if PETase and MHETase can be used together as one attacks the surface of the plastics and the latter chops thing up further, and they observed that these two did indeed work better together in their first experiments. They found that in comparison to the naturally evolved separate enzymes, the novel chimeric enzyme is around three times faster. With this, it is now possible to reduce our dependence on fossil resources such as gas and oil, as this allows for plastics to be made and reused endlessly.
The Diamond Light Source, located at Oxfordshire was used by Professor McGeehan in this study. This synchrotron was used as a microscope as it is much powerful to see individual atoms and it employs intense beams of X-rays 10 billion times brighter than the Sun, which enabled the team to solve the MHETase enzyme’s 3D structure. The team could start developing a faster enzyme system with the help of molecular blueprints obtained through this.
Various approaches including bioinformatics, biochemical, computational, and structure approaches were combined to unravel molecular information into its structure and how it functions in the new research. Many scientists working in different positions were involved in this study.
Taking enzymes from the natural environment, the Centre for Enzyme Innovation modifies them to develop new enzymes for the industry using synthetic biology.
Source
Plastic-eating Enzyme ‘Cocktail’ Provides Potential Plastic Waste Solution
