ArticleScientific reports2019
An engineered GH1 β-glucosidase displays enhanced glucose tolerance and increased sugar release from lignocellulosic materials.
Article in Scientific reports, 2019. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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Who cites it
21 citing papers in PubMed, 72 citations in OpenAlex.
- Temperature-Dependent Conformational Dynamics of Substrate Entrance Loops in β-Glucosidase: Insights from Molecular Dynamics Simulations.International journal of molecular sciences · 2026Article
- Buffalo rumen microbial cellulase as a candidate enzyme for hydrolysis of rice straw into glucose: A preliminary study.Open veterinary journal · 2025Article
- Plasticity of symbiotroph-saprotroph lifestyles of Piloderma croceum associated with Quercus robur L.Communications biology · 2025Article
- Biochemical Characterization of a Novel, Glucose-Tolerant β-Glucosidase from Jiangella ureilytica KC603, and Determination of Resveratrol Production Capacity from Polydatin.Applied biochemistry and biotechnology · 2025Article
- Overexpression of theInternational journal of molecular sciences · 2025Article
- Development of a β-glucosidase improved for glucose retroinhibition for cellulosic ethanol production: an integrated bioinformatics and genetic engineering approach.Biotechnology for biofuels and bioproducts · 2025Article
- Fluorogenic, Subsingle-Turnover Monitoring of Enzymatic Reactions Involving NAD(P)H Provides a Generalized Platform for Directed Ultrahigh-Throughput Evolution of Biocatalysts in Microdroplets.Journal of the American Chemical Society · 2025Article
- Profiling of the β-glucosidases identified in the genome ofApplied and environmental microbiology · 2023Article
- Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review.Molecules (Basel, Switzerland) · 2023Review
- Engineering cellulases for conversion of lignocellulosic biomass.Protein engineering, design & selection : PEDS · 2023Review
- Bioethanol Production from Lignocellulosic Biomass-Challenges and Solutions.Molecules (Basel, Switzerland) · 2022Review
- Transmembrane transport process and endoplasmic reticulum function facilitate the role of gene cel1b in cellulase production of Trichoderma reesei.Microbial cell factories · 2022Article
- Biochemical and Structural Analysis of a Glucose-Tolerant β-Glucosidase from the Hemicellulose-DegradingMolecules (Basel, Switzerland) · 2022Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
- Review
- Article
- Production Optimization, Structural Analysis, and Prebiotic- and Anti-Inflammatory Effects of Gluco-Oligosaccharides Produced byMicroorganisms · 2021Article
- Article
- Engineering Robust Cellulases for Tailored Lignocellulosic Degradation Cocktails.International journal of molecular sciences · 2020Review
- Progress in Ameliorating Beneficial Characteristics of Microbial Cellulases by Genetic Engineering Approaches for Cellulose Saccharification.Frontiers in microbiology · 2020Review
Corrections and comments
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Authors and funding
10 authors at 3 institutions in 2 countries.
Funding
Abstract
β-glucosidases play a critical role among the enzymes in enzymatic cocktails designed for plant biomass deconstruction. By catalysing the breakdown of β-1, 4-glycosidic linkages, β-glucosidases produce free fermentable glucose and alleviate the inhibition of other cellulases by cellobiose during saccharification. Despite this benefit, most characterised fungal β-glucosidases show weak activity at high glucose concentrations, limiting enzymatic hydrolysis of plant biomass in industrial settings. In this study, structural analyses combined with site-directed mutagenesis efficiently improved the functional properties of a GH1 β-glucosidase highly expressed by Trichoderma harzianum (ThBgl) under biomass degradation conditions. The tailored enzyme displayed high glucose tolerance levels, confirming that glucose tolerance can be achieved by the substitution of two amino acids that act as gatekeepers, changing active-site accessibility and preventing product inhibition. Furthermore, the enhanced efficiency of the engineered enzyme in terms of the amount of glucose released and ethanol yield was confirmed by saccharification and simultaneous saccharification and fermentation experiments using a wide range of plant biomass feedstocks. Our results not only experimentally confirm the structural basis of glucose tolerance in GH1 β-glucosidases but also demonstrate a strategy to improve technologies for bioethanol production based on enzymatic hydrolysis.
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