ArticleNature communications2018
Engineering enhanced cellobiohydrolase activity.
Article in Nature communications, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 46 papers.
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Who cites it
46 citing papers in PubMed, 110 citations in OpenAlex.
- Thermostable Carbohydrate-Active Enzymes for High-Temperature Biomass Conversion: From Molecular Design to Process Integration.International journal of molecular sciences · 2026Review
- The carbohydrate-binding module of TrCel7A aids in navigating hemicellulose barriers in plant cell walls.The Journal of biological chemistry · 2026Article
- Fungal cellulases: a comprehensive review on production, innovations, and applications.Archives of microbiology · 2026Review
- Conformational gating mechanism for processive catalysis of β(1,3)-glucans.Nature communications · 2026Article
- Gatekeeping Dietary Fiber: The Role of Carbohydrate-Binding Modules in the Human Gut.Journal of microbiology and biotechnology · 2026Review
- Assessment of glycanolytic enzymes producing potentialities of three strains of Penicillium sp.Biotechnology letters · 2026Article
- Protein engineering: status report.Protein engineering, design & selection : PEDS · 2026Review
- From the bench to the reactor: engineered filamentous fungi for biochemical and biomaterial production.Biotechnology for biofuels and bioproducts · 2025Review
- Advancing continuous enzymatic hydrolysis for improved biomass saccharification.Biotechnology for biofuels and bioproducts · 2025Article
- The Role of Non-Catalytic Region in Determining the Difference in Efficiency Between Two Cellobiohydrolases Revealed Through a Genetic Approach.Journal of fungi (Basel, Switzerland) · 2025Article
- HisAMB Express · 2025Article
- Considerations for Domestication of Novel Strains of Filamentous Fungi.ACS synthetic biology · 2025Review
- High-resolution protein modeling through Cryo-EM and AI: current trends and future perspectives - a review.Frontiers in molecular biosciences · 2025Review
- Stochastic model highlights the impact of crystallinity on saccharification dynamics depending on plant chemotype and pre-treatment.PloS one · 2025Article
- A detailed sensitivity analysis identifies the key factors influencing the enzymatic saccharification of lignocellulosic biomass.Computational and structural biotechnology journal · 2024Article
- Current models in bacterial hemicellulase-encoding gene regulation.Applied microbiology and biotechnology · 2024Review
- Single-molecule tracking reveals dual front door/back door inhibition of Cel7A cellulase by its product cellobiose.Proceedings of the National Academy of Sciences of the United States of America · 2024Article
- The S-S bridge mutation between the A2 and A4 loops (T416C-I432C) of Cel7A ofApplied and environmental microbiology · 2024Article
- Engineering of glycoside hydrolase family 7 cellobiohydrolases directed by natural diversity screening.The Journal of biological chemistry · 2024Article
- A multi-plex protein expression system for production of complex enzyme formulations in Trichoderma reesei.Journal of industrial microbiology & biotechnology · 2023Article
Corrections and comments
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Authors and funding
19 authors at 1 institution in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Glycoside Hydrolase Family 7 cellobiohydrolases (GH7 CBHs) catalyze cellulose depolymerization in cellulolytic eukaryotes, making them key discovery and engineering targets. However, there remains a lack of robust structure-activity relationships for these industrially important cellulases. Here, we compare CBHs from Trichoderma reesei (TrCel7A) and Penicillium funiculosum (PfCel7A), which exhibit a multi-modular architecture consisting of catalytic domain (CD), carbohydrate-binding module, and linker. We show that PfCel7A exhibits 60% greater performance on biomass than TrCel7A. To understand the contribution of each domain to this improvement, we measure enzymatic activity for a library of CBH chimeras with swapped subdomains, demonstrating that the enhancement is mainly caused by PfCel7A CD. We solve the crystal structure of PfCel7A CD and use this information to create a second library of TrCel7A CD mutants, identifying a TrCel7A double mutant with near-equivalent activity to wild-type PfCel7A. Overall, these results reveal CBH regions that enable targeted activity improvements.
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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.