ReviewBBA advances2025
Are cellulases slow? Kinetic and thermodynamic limitations for enzymatic breakdown of cellulose.
Review in BBA advances, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
7 citing papers in PubMed.
- Mechanocatalytic CC Bond Cleavage of Cellulose: A Novel Approach for Selective Production of Lactic Acid.ChemSusChem · 2026Article
- Heterologous Expression of aJournal of fungi (Basel, Switzerland) · 2026Article
- Strategies for GH functional annotation: toward harmonized and predictive CAZymology.Biotechnology for biofuels and bioproducts · 2026Article
- Modifying the upstream open reading frames of cellulase gene enhances cellulase production inSynthetic and systems biotechnology · 2026Article
- Mechanistic insights into substrate-targeting modification effects on interfacial kinetics of raw starch-degrading amylases.Applied and environmental microbiology · 2026Article
- Advances, challenges, and future directions towards a cellulolytic Escherichia coli.Biotechnology for biofuels and bioproducts · 2026Review
- Slowdown of Enzymatic Cellulose Conversion Emerges from Cellulase Mode of Action.ACS catalysis · 2026Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
8 authors.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Cellulases are of paramount interest for upcoming biorefineries that utilize residue from agriculture and forestry to produce sustainable fuels and chemicals. Specifically, cellulases are used for the conversion of recalcitrant plant biomass to fermentable sugars in a so-called saccharification process. The vast literature on enzymatic saccharification frequently refers to low catalytic rates of cellulases as a main bottleneck for industrial implementation, but such statements are rarely supported by kinetic or thermodynamic considerations. In this perspective, we first discuss activation barriers and equilibrium conditions for the hydrolysis of cellulose and how these parameters influence enzymatic turnover. Next, we propose a simple framework for kinetic description of cellulolytic enzyme reactions and show how this can pave the way for comparative biochemical analyses of cellulases acting on their native, insoluble substrate. This latter analysis emphasizes that cellulases are characterized by extraordinarily low off-rate constants, while other kinetic parameters including specificity constants and rate constants for association and bond cleavage are quite like parameters reported for related enzymes acting on soluble substrates.
Indexed as
Identifiers
What Socratic holds
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 Socratic graph.