Glycosylation Helps Cellulase Enzymes Bind to Plant Cell Walls (Fact Sheet)

关键词: AFFINITY;    AMINO ACIDS;    BIOFUELS;    CARBOHYDRATES;    CELLULASE;    CELLULOSE;    COMPUTERIZED SIMULATION;    ENZYMES;    GLUCOSE;    METABOLISM;    MUTATIONS;    NATIONAL RENEWABLE ENERGY LABORATORY;    PLANT CELLS;    PRODUCTION;    PROTEIN ENGINEERING;    PROTEINS;    SACCHARIDES;    TUNING NREL HIGHLIGHT;    GLYCOSYLATION;    CELLULASE;    BIOFUELS;    BIOSCIENCES;    Chemical and Biosciences;   

DOI  :  10.2172/1044446
RP-ID  :  NREL/FS-2700-54284
PID  :  OSTI ID: 1044446
Others  :  TRN: US201214%%671

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来源: SciTech Connect

【 摘 要 】

Computer simulations suggest a new strategy to design enhanced enzymes for biofuels production. Large-scale computer simulations predict that the addition of glycosylation on carbohydrate-binding modules can dramatically improve the binding affinity of these protein domains over amino acid mutations alone. These simulations suggest that glycosylation can be used as a protein engineering tool to enhance the activity of cellulase enzymes, which are a key component in the conversion of cellulose to soluble sugars in the production of biofuels. Glycosylation is the covalent attachment of carbohydrate molecules to protein side chains, and is present in many proteins across all kingdoms of life. Moreover, glycosylation is known to serve a wide variety of functions in biological recognition, cell signaling, and metabolism. Cellulase enzymes, which are responsible for deconstructing cellulose found in plant cell walls to glucose, contain glycosylation that when modified can affect enzymatic activity-often in an unpredictable manner. To gain insight into the role of glycosylation on cellulase activity, scientists at the National Renewable Energy Laboratory (NREL) used computer simulation to predict that adding glycosylation on the carbohydrate-binding module of a cellulase enzyme dramatically boosts the binding affinity to cellulose-more than standard protein engineering approaches in which amino acids are mutated. Because it is known that higher binding affinity in cellulases leads to higher activity, this work suggests a new route to designing enhanced enzymes for biofuels production. More generally, this work suggests that tuning glycosylation in cellulase enzymes is a key factor to consider when engineering biochemical conversion processes, and that more work is needed to understand how glycosylation affects cellulase activity at the molecular level.