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Hot springs microbe yields record-breaking, heat-tolerant enzyme
Date:7/5/2011

f surviving microbes to obtain a metagenome, which indicated that three different species of Archaea were able to utilize cellulose as food. Using genetic techniques, they plucked out the specific genes involved in cellulose degradation, and linked the most active high-temperature cellulase, dubbed EBI-244, to the most abundant of the three Archaea.

Based on the structure of the enzyme, "this could represent a new type of cellulase or a very unusual member of a previously known family," Clark said.

The enzyme is so stable that it works in hot solutions approaching conditions that could be used to pretreat feedstocks like Miscanthus to break down the lignocelluloses and liberate cellulose. This suggests that cellulases may someday be used in the same reaction vessel in which feedstocks are pretreated.

The newly discovered hyperthermophilic cellulase may actually work at too high a temperature for some processes, Clark said. By collecting more hyperthermophilic cellulases, protein engineers may be able to create a version of the enzyme optimized to work at a lower temperature, but with the robust structural stability of the wild microbe.

"We might even find a cellulase that could be used as-is," he said, "but at least they will give us information to engineer new cellulases, and a better understanding of the diversity of nature."


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Contact: Robert Sanders
rsanders@berkeley.edu
510-643-6998
University of California - Berkeley
Source:Eurekalert  

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