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Germany: Renewable Enzymes for Plastics Production Biotechnical Production of Butadiene

| Editor: Alexander Stark

Researches at the German Max-Planck Instiute for marine microbiology developed a procedure to produce enzymes for plastics production from renewable raw materials.

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Structure of linalool dehydratase/isomerase. Five identical proteins form a five-membered rosette. In black, the substrates bound on the enzyme are shown.
Structure of linalool dehydratase/isomerase. Five identical proteins form a five-membered rosette. In black, the substrates bound on the enzyme are shown.
(Picture: Max Planck Insitute for Marine Microbiology)

Bremen/Germany – Butadiene is a key compound in the manufacturing process of plastics. Researchers at the Max-Planck Institute for marine microbiology were able to elucidate the exact three-dimensional structure of the enzyme and the binding sites of geraniol and myrcene on the enzyme. The scientists described their findings as an important milestone on the way from the petrochemical industry towards the energy-economic use of natural resources.

Researchers of the Max Planck Institute for Marine Microbiology in Bremen have published in 2010 the discovery of an enzyme, which converts the rose-scented geraniol in the coriander-scented coriandrol ((S) -linalool) and further in the hop-scented myrcene. However, this enzyme, the linalool dehydratase/isomerase is also capable of forming butadiene from natural raw materials, such as fermentation products.

Important Intermediates in Plastics Production

Butadiene and isoprene are intermediates for nylon production, high-melting plastics (ABS polymers) and rubber products. Over ten million tons of butadiene and isoprene are annually with a market of over € 15 billion. So far butadiene is produced elaborately by cracking of petroleum. Therefore, the chemical industry has a great interest in energy-economic alternatives to butadiene synthesis.

Practical Use of Enzymes

To make effective use of the enzyme in the industry, you have to know the internal architecture and how and where the actual reaction takes place.

Sina Weiden Weber and Ulrich Ermler from the Max Planck-Institute of Biophysics in Frankfurt and Robert Marmulla and Jens Harder from the Max Planck-Institute for Marine Microbiology in Bremen succeeded in the elucidation of the molecular structure of the enzyme. The enzyme is composed of five identical subunits and has a unique binding site for monoterpene alcohols.

"The linalool dehydratase/isomerase structure, the precise knowledge of geraniol and myrcene-binding sites and the insight into the catalytic mechanisms will now enable industrial companies to optimize this actually monoterpenes degrading enzyme for the biotechnological production of butadiene and isoprene" says Jens Harder.

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