Journal
JOURNAL OF THE AMERICAN CHEMICAL SOCIETY
Volume 143, Issue 13, Pages 5172-5181Publisher
AMER CHEMICAL SOC
DOI: 10.1021/jacs.1c01352
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Funding
- NSF [CHE-1708526]
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This article introduces a synthetic glucosidase prepared through molecular imprinting and post-functionalization of cross-linked surfactant micelles, which shows excellent performance in hydrolyzing cellobiose and cellulose under various conditions. The catalyst is stable even at high temperatures and can hydrolyze cellulose several times faster than commercial cellulases in certain solvent mixtures.
Molecular imprinting is a powerful and yet simple method to create multifunctional binding sites within a crosslinked polymer network. We report a new class of synthetic glucosidase prepared through molecular imprinting and post-functionalization of cross-linked surfactant micelles. These catalysts are protein-sized water-soluble nanoparticles that can be modified in multiple ways. As their natural counterparts, they bind a glucose-containing oligo- or polysaccharide. They contain acidic groups near the glycosidic bond to be cleaved, with the number and distance of the acid groups tuned systematically. Hydrolysis of cellulose in a key step in biomass conversion but is hampered by the incalcitrance of the highly crystalline cellulose fibers. The synthetic glucosidases are shown to hydrolyze cellobiose and cellulose under a variety of conditions. The best catalyst, with a biomimetic double acid catalytic motif, can hydrolyze cellulose with one-fifth of the activity of commercial cellulases in aqueous buffer. As a highly cross-linked polymeric nanoparticle, the synthetic catalyst is stable at elevated temperatures in both aqueous and nonaqueous solvents. In a polar aprotic solvent/ionic liquid mixture, it hydrolyzes cellulose several times faster than commercial cellulases in aqueous buffer. When deposited on magnetic nanoparticles, it retains 75% of its activity after 10 cycles of usage.
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