A new Synthetic enzyme has been shown to chew lignin, a solid polymer that helps woody plants maintain their structure. Lignin also retains a large amount of renewable energy and building materials. Reporting today (May 31, 2022) in the journal Nature Communications, a team of researchers from Washington State University and the Department of Energy at the Pacific Northwest National Laboratory (PNNL) have shown that their synthetic enzyme successfully digests lignin, which has strongly resisted previous attempts. to develop it into an economically viable source of energy.
Lignin, the world’s second-largest renewable carbon source, is being depleted as a fuel source. When wood is heated for cooking, lignin byproducts help to transmit that flavor to the food. But heat releases all that carbon into the atmosphere instead of replacing it with other uses. Our bio-acting enzyme has shown promise in degrading real lignin, which is considered a success, “said Xiao Zhang, co-author of the paper and associate professor at WSU’s Gene and Linda Voiland School of Chemical Engineering and Bioengineering. Zhang also holds joint time in the PNNL.
“We think there is an opportunity to develop a new class of catalysts and to really deal with biological and chemical limitations.” biofuels and chemical production, ”added Chun-Long Chen, co-author, Pacific Northwest National Laboratory researcher and associate professor of chemical engineering and chemistry at the University of Washington. covered with rotting mushrooms o in the forest. Enzymes provide a process that is less harmful to the environment than chemical degradation, which requires higher temperatures and consumes more energy than is produced. However, natural enzymes deteriorate over time, making it difficult to use them in the industrial process. They are expensive too.
“It is really difficult to produce these enzymes from microbes in small quantities for use,” Zhang said. “Then once you have separated them, they are very weak and unstable. But these enzymes provide a good opportunity to stimulate models that copy their basic structure. ”
Although researchers have not been able to utilize natural enzymes to work, in recent decades they have learned much about their mechanisms. A recent review article by Zhang’s research team highlights the challenges and barriers to the use of degrading lignin enzymes. “Understanding these barriers provides new insights into the design of biomimetic enzymes,” added Zhang.
Peptoid scaffold is important
In the present study, researchers have replaced peptides that surround the active site of natural enzymes with molecules similar to proteins called peptoids. These peptoids then self-assemble into nanoscale crystalline sheets. Peptoids were first developed in the 1990s to mimic the functioning of proteins. They have a few unique features, including high stability, that allow scientists to deal with the deficiency of natural enzymes. In this case, they provide a high concentration of active sites, which are impossible to obtain by natural enzyme.
“We can better organize these functional sites and streamline their local environments to create incentives,” said Chen, “and we have a very high level of active sites, instead of a single functional site.”Naturally, these synthetic enzymes are more stable and robust than natural versions, so they can operate at temperatures as high as 60 degrees Celsius (140 degrees Fahrenheit), temperatures that can damage the natural enzyme. This job really opens up new opportunities, ”said Chen. “This is an important step forward in being able to convert lignin into essential products using a healthy natural way.”If a new bio-mimetic enzyme can be further developed to increase the conversion rate, producing more selective products, it has the potential to rise to industrial scale. The technology provides new routes to renewable biofuel aircraft and bio-based materials, among other applications.
Source Journal Reference: “Highly stable and tunable peptoid/hemin enzymatic mimetics with natural peroxidase-like activities”, Nature Communications 2022. DOI: 10.1038/s41467-022-30285-9
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