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    Home»Chemistry»Scientists Turn Discarded Wood Waste Into Valuable Chemicals
    Chemistry

    Scientists Turn Discarded Wood Waste Into Valuable Chemicals

    By University of AdelaideApril 14, 2025No Comments3 Mins Read
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    Lignin Processing Enzyme
    The newly identified enzyme highlighted in pink. Credit: University of Adelaide

    A new enzyme can turn lignin waste into valuable chemicals using green, hydrogen peroxide-based processing, offering a cleaner, sustainable alternative to petroleum-based methods.

    Approximately 98% of lignin, a by-product of forestry derived from plants, is currently discarded. However, a newly discovered enzyme may enable the efficient extraction of valuable molecules from this waste using environmentally friendly, green chemistry methods.

    These extracted molecules serve as the building blocks for products such as fragrances, flavorings, fuels, and pharmaceuticals, transforming a largely unused waste stream into a valuable resource.

    “Traditional chemical processes for the synthesis of these types of chemicals rely on petroleum-based starting compounds and heavy metal catalysts, making them non-renewable and inherently toxic processes,” says Dr Fiona Whelan, a Cryo-electron Microscopist from Adelaide Microscopy at the University of Adelaide, whose study was published in Nature Communications.

    “This new catalytic processing method will support the development of other new green chemistry ‘enzyme factories’ or biorefineries to turn the lignin and other biological waste streams into a valuable repository of fine chemicals.”

    Understanding Lignin and Its Potential

    Lignin is the name given to the hard polymers that act as mechanical support in hard- and softwoods and is one of the most abundant polymers on Earth.

    Agriculture and forestry amass around 100 million tonnes of waste lignin per year, but this could be diverted to become a promising renewable and sustainable feedstock for chemicals currently obtained from fossil fuels.

    “Strategies for using lignin involve a combination of chemical and biological processes,” says Associate Professor Stephen Bell, from the University’s School of Physics, Chemistry and Earth Sciences.

    “High temperatures, high pressure, strong acids, and poisonous solvents are used to break up the polymers in the waste stream.

    “The valuable compounds trapped in the waste are then extracted and undergo further chemical processing at temperatures higher than 400°C to ‘valorize’ the lignin. These processes are expensive and bad for the environment.”

    A Biological Breakthrough

    Hardwood lignin has two key chemical components that require processing to make useful compounds.

    Researchers had previously discovered an enzyme that could be used to break down one of these compounds, which is also found in softwood, but no biological breakdown process had been identified that could use the second more complex hardwood compound, comprising about 50 percent of the waste.

    “Biological breakdown of lignin occurs in a complex microbial quorum, with fungal enzymes likely breaking up hard polymers, and bacteria taking the unreactive smaller compounds and processing them to get metabolic energy,” said Dr Whelan.

    “Looking to the microbial kingdom, we identified that a soil bacterium, Amycolatopsis thermoflava, contains enzymes that could process molecules from lignin cheaply, using hydrogen peroxide to drive the reaction – making valorization much less harmful to the environment.”

    The research team has used this new enzyme as a model for retrofitting the hydrogen peroxide driven activity into other enzymes to generate green chemistry approaches of the future for the generation of high-value chemicals of use in the flavor, fragrance, and medicinal chemistry industries.

    Reference: “Structural insights into S-lignin O-demethylation via a rare class of heme peroxygenase enzymes” by Alix C. Harlington, Tuhin Das, Keith E. Shearwin, Stephen G. Bell and Fiona Whelan, 20 February 2025, Nature Communications.
    DOI: 10.1038/s41467-025-57129-6

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    Biotechnology Enzyme University of Adelaide
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