Clark, Robb and their colleagues, including UC Berkeley professor Harvey W. Blanch and postdoctoral researcher Melinda E. Clark, and U-Md postdoctoral researcher Joel E. Graham, will publish their results Tuesday, July 5, in the online-only journal Nature Communications.
Many industrial processes employ natural enzymes, some of them isolated from organisms that live in extreme environments, such as hot springs. The enzyme used in the popular polymerase chain reaction to amplify DNA originally came from a thermophilic organism found in a geyser in Yellowstone National Park.
But many of these enzymes are not optimized for industrial processes, Clark said. For example, a fungal enzyme is currently used to break down tough plant cellulose into its constituent sugars so that the sugars can be fermented by yeast into alcohol. But the enzyme's preferred temperature is about 50oC (122oF), and it is not stable at the higher temperatures desirable to prevent other microbes from contaminating the reaction.
Hence the need to look in extreme environments for better enzymes, he said.
"This discovery is interesting because it helps define the range of natural conditions under which cellulolytic organisms exist and how prevalent these bugs are in the natural world," Clark said. "It indicates that there are a lot of potentially useful cellulases in places we haven't looked yet."
Robb and his colleagues collected sediment and water samples from the 95oC (203oF) Great Boiling Springs near the town of Gerlach in northern Nevada and grew microbes on pulverized Miscanthus gigas, a common biofuel feedstock, to isolate those that could grow with plant fiber as their only source of carbon.
After further growth on microcrystalline cellulose, the U-Md and UC Berkeley labs worked together to sequence the community o
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University of California - Berkeley