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In recent years, the enzymatic recycling of plastics has emerged as an attractive and environmentally friendly strategy to help alleviate the problems associated with plastic waste. Several methods exist for recycling plastics; however, enzymes could potentially offer a more cost-effective and energy efficient alternative. In addition, they could be used to selectively break down specific components of mixed plastic waste streams that are currently difficult to recycle using existing technologies.
In a recent publication, a team from the Manchester Institute of Biotechnology used Diamond Macromolecular Crystallography beamlines to characterise a new engineered protein selected through direct evolution. The authors selected the catalytic activity of the enzyme to operate more efficiently at elevated temperatures. The most efficient variant protein named HotPETase can function at temperatures up to 70°C. X-ray diffraction was used to analyse the structure of the new engineered protein, and to find major residues involved in the protein stability. The fine resolution of the structure allowed the team to further analyse the catalytic activity.
This study shows the possibility offered by directed evolution of enzymes with a high throughput screening platform. The development of robust plastic degrading enzymes such as HotPETase, along with the availability of a versatile enzyme engineering platform, make important contributions towards the development of a biotechnological solution to the plastic waste challenge. Structural analysis of proteins can be done routinely at Diamond. Characterisation of these proteins helps scientists to better understand how they work, and how they can be improved for the benefit of society. In this case, the discovery of an enhanced protein will offer new possibilities to the recycling industry.
Bell, E. L., Smithson, R., Kilbride, S., Foster, J., Hardy, F. J., Ramachandran, S., Tedstone, A. A., Haigh, S. J., Garforth, A. A., Day, P. J. R., Levy, C., Shaver, M. P., & Green, A. P. Directed evolution of an efficient and thermostable PET depolymerase. Nature Catalysis. (2022). DOI: 10.1038/s41929-022-00821-3
ERC, the Medical Research Council and Buddi, the UK Catalysis Hub, EPSRC, the Henry Royce Institute for Advanced Materials, the ISCF Smart Sustainable Plastic Packaging fund.
Beamlines involved: I03, I04, I04-1
Proposals: MX12788-50, MX17773-25, MX17773-34 and MX17773-52
Scientific discipline: Earth Sciences & Environment; Biotechnology; Biochemistry; Catalysis; Chemistry; Structural biology; Engineering & Technology; Life Sciences & Biotech
Technique: X-ray Diffraction
Diamond press office: Isabelle Boscaro-Clarke. Head of communications. [email protected]
Beamline I03: Dave Hall, MX Group Leader, [email protected]
Beamline I04: Ralf Flaig, Principal Beamline Scientist, [email protected]
Beamline I04-1: Frank Von Delft, Principal Beamline Scientist, [email protected]
Corresponding author: Anthony P. Green, University of Manchester
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