U.S. Department of Energy Office of Biological and Environmental Research

BER Research Highlights


Evolution of Substrate Specificity in Bacterial Lytic Polysaccharide Monooxygenases
Published: August 06, 2014
Posted: January 12, 2015

Cellulose is one of the most abundant polysaccharides in nature and one of the primary components of plant cell walls. The biofuels industry has devoted significant efforts to establish processes to convert these energy-rich molecules into sugars that can be fermented into biofuels or other bioproducts. However, the hydrolysis of these polysaccharides, a key step in converting them to biofuels, is difficult due to their crystalline structure, the stability of some bonds within their structure, and how closely they are associated with structure-modifying molecules such as hemicellulose and lignin. Efficient hydrolysis requires a cocktail of different enzymes. Enzymes capable of hydrolyzing these polymers have been identified in various organisms, especially bacteria and fungi, but the pathways for deconstruction of certain polysaccharides, such as cellulose and chitin, are only partially understood. Researchers at the Department of Energy’s Great Lakes Bioenergy Research Center analyzed the sequences, structures, and evolution of two families of enzymes, fungal AA9 and bacterial AA10, both lytic polysaccharide monooxygenases (LPMOs), to understand the factors that influence substrate specificity in these families and to characterize the selective pressures that may have led to their functional diversification. Their sequence similarity suggests that both families share a distant common ancestor and that certain clades within the AA10 family are specialized for different substrates, while others went through a diversifying selection at surface-exposed regions of the protein. Understanding the diversity of these lignocellulosic-degrading enzymes in nature provides information that can help improve enzymatic cocktails used in the biofuels industry.

Reference: Book, A. J., R. M. Yennamalli, T. E. Takasuka, C. R. Currie, G. N. Phillips, and B. G. Fox. 2014. “Evolution of Substrate Specificity in Bacterial AA10 Lytic Polysaccharide Monooxygenases,” Biotechnology for Biofuels 7,109. DOI: 10.1186/1754-6834-7-109. (Reference link)

Contact: Kent Peters, SC-23.2, (301) 903-5549
Topic Areas:

  • Research Area: Genomic Analysis and Systems Biology
  • Research Area: Sustainable Biofuels and Bioproducts
  • Research Area: DOE Bioenergy Research Centers (BRC)
  • Research Area: Structural Biology, Biomolecular Characterization and Imaging

Division: SC-23.2 Biological Systems Science Division, BER

 

BER supports basic research and scientific user facilities to advance DOE missions in energy and environment. More about BER

Recent Highlights

May 10, 2019
Quantifying Decision Uncertainty in Water Management via a Coupled Agent-Based Model
Considering risk perception can improve the representation of human decision-making processes in age [more...]

May 09, 2019
Projecting Global Urban Area Growth Through 2100 Based on Historical Time Series Data and Future Scenarios
Study provides country-specific urban area growth models and the first dataset on country-level urba [more...]

May 05, 2019
Calibrating Building Energy Demand Models to Refine Long-Term Energy Planning
A new, flexible calibration approach improved model accuracy in capturing year-to-year changes in bu [more...]

May 03, 2019
Calibration and Uncertainty Analysis of Demeter for Better Downscaling of Global Land Use and Land Cover Projections
Researchers improved the Demeter model’s performance by calibrating key parameters and establi [more...]

Apr 22, 2019
Representation of U.S. Warm Temperature Extremes in Global Climate Model Ensembles
Representation of warm temperature events varies considerably among global climate models, which has [more...]

List all highlights (possible long download time)