ArticlemBio2010
Cellulase-xylanase synergy in designer cellulosomes for enhanced degradation of a complex cellulosic substrate.
Article in mBio, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 43 papers.
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Who cites it
43 citing papers in PubMed, 124 citations in OpenAlex.
- Thermostable Carbohydrate-Active Enzymes for High-Temperature Biomass Conversion: From Molecular Design to Process Integration.International journal of molecular sciences · 2026Review
- Integrative SAXS and AFM analysis of engineered carbohydrate-active enzyme assemblies with tunable spatial organization.Protein science : a publication of the Protein Society · 2026Article
- Bio-inspired designer cellulosomes show strongest synergy on industrial substrates under natural-like conditions.Journal of industrial microbiology & biotechnology · 2026Article
- Carbohydrate Depolymerization by Intricate Cellulosomal Systems.Methods in molecular biology (Clifton, N.J.) · 2023Article
- Conversion of the free Cellvibrio japonicus xyloglucan degradation system to the cellulosomal mode.Applied microbiology and biotechnology · 2022Article
- Combinatorial assembly and optimisation of designer cellulosomes: a galactomannan case study.Biotechnology for biofuels and bioproducts · 2022Article
- Comparative genomics reveals cellobiose hydrolysis mechanism ofFrontiers in microbiology · 2022Article
- Rapid adaptation for fibre degradation by changes in plasmid stoichiometry within Lactobacillus plantarum at the synthetic community level.Microbial biotechnology · 2020Article
- Characterisation of the Effect of the Spatial Organisation of Hemicellulases on the Hydrolysis of Plant Biomass Polymer.International journal of molecular sciences · 2020Article
- Cellulolytic thermophilic microorganisms in white biotechnology: a review.Folia microbiologica · 2020Review
- Elucidating structure-performance relationships in whole-cell cooperative enzyme catalysis.Nature catalysis · 2019Article
- Assembly of Synthetic Functional Cellulosomal Structures onto the Cell Surface of Lactobacillus plantarum, a Potent Member of the Gut Microbiome.Applied and environmental microbiology · 2018Article
- Determination of the native features of the exoglucanase Cel48S fromBiotechnology for biofuels · 2018Article
- Biomolecular engineering for nanobio/bionanotechnology.Nano convergence · 2017Review
- Toward combined delignification and saccharification of wheat straw by a laccase-containing designer cellulosome.Proceedings of the National Academy of Sciences of the United States of America · 2016Article
- Article
- Adaptor Scaffoldins: An Original Strategy for Extended Designer Cellulosomes, Inspired from Nature.mBio · 2016Article
- Biochemical characterization of extra- and intracellular endoxylanse from thermophilic bacterium Caldicellulosiruptor kronotskyensis.Scientific reports · 2016Article
- Enhancement of cellulosome-mediated deconstruction of cellulose by improving enzyme thermostability.Biotechnology for biofuels · 2016Article
- Cellulosomal expansin: functionality and incorporation into the complex.Biotechnology for biofuels · 2016Article
Corrections and comments
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Authors and funding
8 authors at 5 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Designer cellulosomes are precision-engineered multienzyme complexes in which the molecular architecture and enzyme content are exquisitely controlled. This system was used to examine enzyme cooperation for improved synergy among Thermobifida fusca glycoside hydrolases. Two T. fusca cellulases, Cel48A exoglucanase and Cel5A endoglucanase, and two T. fusca xylanases, endoxylanases Xyn10B and Xyn11A, were selected as enzymatic components of a mixed cellulase/xylanase-containing designer cellulosome. The resultant mixed multienzyme complex was fabricated on a single scaffoldin subunit bearing all four enzymes. Conversion of T. fusca enzymes to the cellulosomal mode followed by their subsequent incorporation into a tetravalent cellulosome led to assemblies with enhanced activity (~2.4-fold) on wheat straw as a complex cellulosic substrate. The enhanced synergy was caused by the proximity of the enzymes on the complex compared to the free-enzyme systems. The hydrolytic properties of the tetravalent designer cellulosome were compared with the combined action of two separate divalent cellulase- and xylanase-containing cellulosomes. Significantly, the tetravalent designer cellulosome system exhibited an ~2-fold enhancement in enzymatic activity compared to the activity of the mixture of two distinct divalent scaffoldin-borne enzymes. These results provide additional evidence that close proximity between cellulases and xylanases is key to the observed concerted degradation of the complex cellulosic substrate in which the integrated enzymes complement each other by promoting access to the relevant polysaccharide components of the substrate. The data demonstrate that cooperation among xylanases and cellulases can be augmented by their integration into a single designer cellulosome.
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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.