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Addition of a carbohydrate-binding module enhances cellulase penetration into cellulose substrates
Authors
PD Adams
G Cheng
+10 more
RB Elandt
MZ Hadi
RA Heins
MS Kent
EY Kim
V Reyes-Ortiz
KL Sale
BA Simmons
D Tullman-Ercek
BC Vernon
Publication date
11 July 2013
Publisher
eScholarship, University of California
Abstract
Introduction. Cellulases are of great interest for application in biomass degradation, yet the molecular details of the mode of action of glycoside hydrolases during degradation of insoluble cellulose remain elusive. To further improve these enzymes for application at industrial conditions, it is critical to gain a better understanding of not only the details of the degradation process, but also the function of accessory modules. Method. We fused a carbohydrate-binding module (CBM) from family 2a to two thermophilic endoglucanases. We then applied neutron reflectometry to determine the mechanism of the resulting enhancements. Results: Catalytic activity of the chimeric enzymes was enhanced up to three fold on insoluble cellulose substrates as compared to wild type. Importantly, we demonstrate that the wild type enzymes affect primarily the surface properties of an amorphous cellulose film, while the chimeras containing a CBM alter the bulk properties of the amorphous film. Conclusion: Our findings suggest that the CBM improves the efficiency of these cellulases by enabling digestion within the bulk of the film. © 2013 Reyes-Ortiz et al.; licensee BioMed Central Ltd
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Last time updated on 25/12/2021