Reporter Group-Labeled Synthetic Cellulose: Structural Characterization and Utilization in Mapping the Cellulose Chain-Cleavage Modes of Cellulases
Gaurav Singh Kaira, Manuel Eibinger, Chao Zhong, Bernd Nidetzky
TL;DR
Scientists created labeled cellulose to study how enzymes break down cellulose, revealing insights into enzyme activity on crystalline structures.
Contribution
Development of reporter group-labeled synthetic cellulose to map cellulase chain-cleavage modes on crystalline substrates.
Findings
Synthetic cellulose-pNP forms nanoscale sheet-like assemblies with thickness ~4 nm.
Hydrolase systems prefer processive chain cleavage from chain ends, influenced by local nanoscale structure.
T. reesei Cel7A preferentially attacks sheet edges, with degradation efficiency dependent on structure.
Abstract
Iterative β-1,4-glucosylation of p-nitrophenyl (pNP)-β-cellobioside by cellodextrin phosphorylase was applied to synthesize reducing-end reporter group-labeled cellooligosaccharides (average degree of polymerization, DP: ∼5.7; DP range: 4–10) which, upon self-assembly in solution, precipitate as a cellulose allomorph II crystalline material. Atomic force microscopy revealed that the synthetic cellulose-pNP forms nanoscale sheet-like assemblies, with thickness ∼4 nm. The labeled cellulose was used to characterize the chain cleavage specificities of cellulose-degrading enzymes. Reactions were monitored by the release of soluble products as well as the change in oligosaccharide composition of the residual solid material, measured by mass spectrometry. The products formed by hydrolase systems (Trichoderma reesei cellulases; Clostridium thermocellum cellulosome) are controlled by processive…
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Taxonomy
TopicsAdvanced Cellulose Research Studies · Polysaccharides and Plant Cell Walls · Biofuel production and bioconversion