NREL researchers gain insights into how glycosylation affects key cellulase enzyme

December 12, 2017 |

In Colorado, researchers from the U.S. Department of Energy’s National Renewable Energy Laboratory  have gained new insights into how glycosylation—the natural attachment of sugars to proteins—affects a key cellulase enzyme. This work could be used to improve enzyme performance to better break down biomass and convert waste plant matter to renewable fuels and products. Namely, the more effective the enzyme, the more efficient and economical the process will be.

The new research, which focuses on the enzyme Cel7A that breaks down cellulose in plants to sugars, is detailed in the Proceedings of the National Academy of Sciences (PNAS) in a manuscript titled “Distinct roles of N- and O-glycans in cellulase activity and stability.” This study sheds light on the specific functions of small sugars, or glycans, that microbes attach to their enzymes. This enzymatic modification by the addition of sugars is referred to as “glycosylation” and it is known to have a substantial impact on enzyme function.

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