ArticleThe Journal of biological chemistry2012
Endo-exo synergism in cellulose hydrolysis revisited.
Article in The Journal of biological chemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 60 papers.
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Who cites it
60 citing papers in PubMed, 219 citations in OpenAlex.
- Slowdown of Enzymatic Cellulose Conversion Emerges from Cellulase Mode of Action.ACS catalysis · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- Simultaneous Biosynthesis of Cellulase byWaste and biomass valorization · 2026Article
- Revisiting the endo and exo mode of action of dextran hydrolyzing enzymes, and their significance for Streptococcus mutans biofilm eradication.World journal of microbiology & biotechnology · 2025Article
- Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose.BBA advances · 2025Review
- Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening.The Journal of biological chemistry · 2024Article
- Functional characterisation of a new halotolerant seawater active glycoside hydrolase family 6 cellobiohydrolase from a salt marsh.Scientific reports · 2024Article
- Impact of Synergy Partner Cel7B on Cel7A Binding Rates: Insights from Single-Molecule Data.The journal of physical chemistry. B · 2024Article
- Mechanism-based Modelling for Fitting the Double-exponential Progress Curves of Cellulase Reaction.Journal of applied glycoscience · 2024Article
- Stoichiometric balance ratio of cellobiose and gentiobiose induces cellulase production in Talaromyces cellulolyticus.Biotechnology for biofuels and bioproducts · 2023Article
- Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023Review
- Endo-Exoglucanase Synergism for Cellulose Nanofibril Production Assessment and Characterization.Molecules (Basel, Switzerland) · 2023Article
- Enzyme Synergy in Transient Clusters of Endo- and Exocellulase Enables a Multilayer Mode of Processive Depolymerization of Cellulose.ACS catalysis · 2022Article
- Novel Two-Step Process in Cellulose Depolymerization: Hematite-Mediated Photocatalysis by Lytic Polysaccharide Monooxygenase and Fenton Reaction.Journal of agricultural and food chemistry · 2022Article
- Mapping the deformability of natural and designed cellulosomes in solution.Biotechnology for biofuels and bioproducts · 2022Article
- AA15 lytic polysaccharide monooxygenase is required for efficient chitinous cuticle turnover during insect molting.Communications biology · 2022Article
- Synergic action of an inserted carbohydrate-binding module in a glycoside hydrolase family 5 endoglucanase.Acta crystallographica. Section D, Structural biology · 2022Article
- Biochemical and Structural Analysis of a Glucose-Tolerant β-Glucosidase from the Hemicellulose-DegradingMolecules (Basel, Switzerland) · 2022Article
- Simultaneous Display of Multiple Kinds of Enzymes on the Yeast Cell Surface for Multistep Reactions.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Processive Enzymes Kept on a Leash: How Cellulase Activity in Multienzyme Complexes Directs Nanoscale Deconstruction of Cellulose.ACS catalysis · 2021Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Synergistic cooperation of different enzymes is a prerequisite for efficient degradation of cellulose. The conventional mechanistic interpretation of the synergism between randomly acting endoglucanases (EGs) and chain end-specific processive cellobiohydrolases (CBHs) is that EG-generated new chain ends on cellulose surface serve as starting points for CBHs. Here we studied the hydrolysis of bacterial cellulose (BC) by CBH TrCel7A and EG TrCel5A from Trichoderma reesei under both single-turnover and "steady state" conditions. Unaccountable by conventional interpretation, the presence of EG increased the rate constant of TrCel7A-catalyzed hydrolysis of BC in steady state. At optimal enzyme/substrate ratios, the "steady state" rate of synergistic hydrolysis became limited by the velocity of processive movement of TrCel7A on BC. A processivity value of 66 ± 7 cellobiose units measured for TrCel7A on (14)C-labeled BC was close to the leveling off degree of polymerization of BC, suggesting that TrCel7A cannot pass through the amorphous regions on BC and stalls. We propose a mechanism of endo-exo synergism whereby the degradation of amorphous regions by EG avoids the stalling of TrCel7A and leads to its accelerated recruitment. Hydrolysis of pretreated wheat straw suggested that this mechanism of synergism is operative also in the degradation of lignocellulose. Although both mechanisms of synergism are used in parallel, the contribution of conventional mechanism is significant only at high enzyme/substrate ratios.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.