ArticleThe Journal of biological chemistry2012
Origin of initial burst in activity for Trichoderma reesei endo-glucanases hydrolyzing insoluble cellulose.
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 17 papers.
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17 citing papers in PubMed.
- The Effect of Accessibility of Insoluble Substrate on the Overall Kinetics of Enzymatic Degradation.Biotechnology and bioengineering · 2025Article
- Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose.BBA advances · 2025Review
- Improving the Enzymatic Activity and Stability of a Lytic Polysaccharide Monooxygenase.International journal of molecular sciences · 2023Article
- Model of Processive Catalysis with Site Clustering and Blocking and Its Application to Cellulose Hydrolysis.The journal of physical chemistry. B · 2022Article
- Machine learning reveals sequence-function relationships in family 7 glycoside hydrolases.The Journal of biological chemistry · 2021Article
- Physical constraints and functional plasticity of cellulases.Nature communications · 2021Article
- Real-Time Measurement of Cellobiose and Glucose Formation during Enzymatic Biomass Hydrolysis.Analytical chemistry · 2021Article
- Investigating the effects of substrate morphology and experimental conditions on the enzymatic hydrolysis of lignocellulosic biomass through modeling.Biotechnology for biofuels · 2021Article
- Enzyme Kinetics by Isothermal Titration Calorimetry: Allostery, Inhibition, and Dynamics.Frontiers in molecular biosciences · 2020Review
- Activity of fungal β-glucosidases on cellulose.Biotechnology for biofuels · 2020Article
- Modeling the activity burst in the initial phase of cellulose hydrolysis by the processive cellobiohydrolase Cel7A.Biotechnology and bioengineering · 2019Article
- Cloning, Expression, and Characterization of a Thermophilic Endoglucanase, AcCel12B from Acidothermus cellulolyticus 11B.International journal of molecular sciences · 2015Article
- The predominant molecular state of bound enzyme determines the strength and type of product inhibition in the hydrolysis of recalcitrant polysaccharides by processive enzymes.The Journal of biological chemistry · 2015Article
- Product inhibition of cellulases studied with 14C-labeled cellulose substrates.Biotechnology for biofuels · 2013Article
- Hallmarks of processivity in glycoside hydrolases from crystallographic and computational studies of the Serratia marcescens chitinases.The Journal of biological chemistry · 2012Article
- Endo-exo synergism in cellulose hydrolysis revisited.The Journal of biological chemistry · 2012Article
- Pre-steady-state kinetics for hydrolysis of insoluble cellulose by cellobiohydrolase Cel7A.The Journal of biological chemistry · 2012Article
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10 authors.
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No grant is acknowledged in the PubMed record.
Abstract
The kinetics of cellulose hydrolysis have long been described by an initial fast hydrolysis rate, tapering rapidly off, leading to a process that takes days rather than hours to complete. This behavior has been mainly attributed to the action of cellobiohydrolases and often linked to the processive mechanism of this exo-acting group of enzymes. The initial kinetics of endo-glucanases (EGs) is far less investigated, partly due to a limited availability of quantitative assay technologies. We have used isothermal calorimetry to monitor the early time course of the hydrolysis of insoluble cellulose by the three main EGs from Trichoderma reesei (Tr): TrCel7B (formerly EG I), TrCel5A (EG II), and TrCel12A (EG III). These endo-glucanases show a distinctive initial burst with a maximal rate that is about 5-fold higher than the rate after 5 min of hydrolysis. The burst is particularly conspicuous for TrCel7B, which reaches a maximal turnover of about 20 s(-1) at 30 °C and conducts about 1200 catalytic cycles per enzyme molecule in the initial fast phase. For TrCel5A and TrCel12A the extent of the burst is 2-300 cycles per enzyme molecule. The availability of continuous data on EG activity allows an analysis of the mechanisms underlying the initial kinetics, and it is suggested that the slowdown is linked to transient inactivation of enzyme on the cellulose surface. We propose, therefore, that the frequency of structures on the substrate surface that cause transient inactivation determine the extent of the burst phase.
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