Page 54 - Plastics News April 2019
P. 54

teChnoLogy



         'Molecular scissors' for plastic waste



             research team  has  solved the molecular structure   a PET bottle, chemically decomposed the PET polymer
         A  of the enzyme MHETase at BESSY II. MHETase was      and synthesised a small chemical fragment from it that
         discovered in bacteria and together with a second enzyme   binds to MHETase but can no longer be cleaved by it.
         -- PETase -- is able to break down the widely used plastic   From this 'blocked' MHETase, tiny crystals were grown
         PET into its basic building blocks. This 3D structure already   for structural investigations at the HZB. "The structural
         allowed the researchers to produce a MHETase variant with   investigations enabled us to watch MHETase virtually 'at
         optimized activity in order to use it, together with PETase,   work' and develop strategies for  how to optimise this
         for a sustainable recycling of PET. The enzyme MHETase   enzyme," explains Weber."Thanks to the joint research
         is a huge and complex molecule. MHET-molecules from    group format, we have  the  means  to offer  beamtime
                                                                access on the highly demanded BESSY II MX beamlines for
                                                                measurements very quickly at any time," says Dr. Manfred
                                                                Weiss, who is responsible for the BESSY II MX beamlines.
                                                                The three-dimensional architecture of MHETase actually
                                                                displays some special features: enzymes such as MHETase
                                                                bind  to  their  target  molecule  first  before  a  chemical
                                                                reaction occurs. For breakdown of a molecule you need a
                                                                tailor-made enzyme: "We can now exactly localise where
                                                                the MHET molecule docks to MHETase and how MHET is
                                                                then split into its two building blocks terephthalic acid
         PET plastic dock at the active site inside the MHETase and   and ethylene glycol," says Weber. However, neither PETase
         are broken down into their basic building blocks. Dr. Gert   nor MHETase are particularly efficient yet.
         Weber, biochemist and structural biologist from the joint   "Plastics have only been around on this scale for a few
         Protein Crystallography research group at the Helmholtz-  decades -- even bacteria with their rapid successions of
         Zentrum Berlin and Freie Universität Berlin says, "In order   generations and rapid adaptability have not managed
         to see how MHETase binds to PET and decomposes it, you   to develop a perfect solution through the evolutionary
         need a fragment of plastic that binds to MHETase but is   process of trial and error over such a short time," explains
         not cleaved by it.” "MHETase is considerably larger than   Weber. "Thanks to the clarification of the structure of this
         PETase and even more complex.                          very important enzyme, we have now also been able to
         A single MHETase molecule consists of 600 amino acids,   plan, produce and biochemically characterise variants that
         or about 4000 atoms. MHETase has a surface that is     show significantly higher activity than natural MHETase and
         about twice as large as the surface of PETase and has   are even active against another intermediate product of
         therefore considerably more potential to optimise it for   PET degradation, BHET," adds Uwe Bornscheuer. In future,
         decomposition of PET," explains Dr. Gert Weber .During   Uwe Bornscheuer will work on systematically optimising
         an interim professorship at the University of Greifswald,   the enzymes PETase and MHETase for their task -- the
         Weber  there  contacted  the  biotechnologist  Prof.  Uwe   decomposition of PET. Gert Weber plans to supplement
         Bornscheuer  at  the  Institute  of  Biochemistry,  who   these studies with further work on biological structures in
         was already involved with plastic-degrading enzymes.   order to systematically develop plastic-digesting enzymes
         Together, they developed the idea of solving the structure   for environmental applications. Access to the measuring
         of MHETase and then using this insight to optimise the   stations and the IT infrastructure of HZB is indispensable
         enzyme for applications in PET recycling. To do this, they   for this.Producing these kinds of enzymes in closed
         first had to extract the enzyme from bacterial cells and   biotechnological cycles, for example, could be a way to
         purify it. Within this collaboration, the teams have now   really break down PET plastics and other polymers into
         succeeded in obtaining the complex three-dimensional   their basic building blocks. This would also be the key
         architecture of MHETase at BESSY II, the synchrotron   to ideal recycling and a long-term solution to the plastic
         source  at  HZB  in  Berlin.   A  member  of  Weber's  prior   waste problem: production of plastic would be a closed
         research team in Greifswald, Dr. Gottfried Palm, cut up   cycle and no longer dependent on crude oil.


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