ArticlePloS one2016
Improvements in Glucose Sensitivity and Stability of Trichoderma reesei β-Glucosidase Using Site-Directed Mutagenesis.
Article in PloS one, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 papers.
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Who cites it
16 citing papers in PubMed, 65 citations in OpenAlex.
- Cellulase Production by Ultraviolet-Derived MutantInternational journal of molecular sciences · 2025Article
- A thermostable and highly active fungal GH3 β-glucosidase generated by random and saturation mutagenesis.Proceedings of the Japan Academy. Series B, Physical and biological sciences · 2025Article
- Recent Advances in β-Glucosidase Sequence and Structure Engineering: A Brief Review.Molecules (Basel, Switzerland) · 2023Review
- Physico-Chemical Characterization of an Exocellular Sugars Tolerant Β-Glucosidase from GrapeMicroorganisms · 2023Article
- Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
- Glutantβase: a database for improving the rational design of glucose-tolerant β-glucosidases.BMC molecular and cell biology · 2020Article
- Progress in Ameliorating Beneficial Characteristics of Microbial Cellulases by Genetic Engineering Approaches for Cellulose Saccharification.Frontiers in microbiology · 2020Review
- A Novel High Glucose-Tolerant β-Glucosidase: Targeted Computational Approach for Metagenomic Screening.Frontiers in bioengineering and biotechnology · 2020Article
- Molecular Dynamics Gives New Insights into the Glucose Tolerance and Inhibition Mechanisms on β-Glucosidases.Molecules (Basel, Switzerland) · 2019Article
- An engineered GH1 β-glucosidase displays enhanced glucose tolerance and increased sugar release from lignocellulosic materials.Scientific reports · 2019Article
- A Computational Method to Propose Mutations in Enzymes Based on Structural Signature Variation (SSV).International journal of molecular sciences · 2019Article
- Synergies in coupled hydrolysis and fermentation of cellulose using a Trichoderma reesei enzyme preparation and a recombinant Saccharomyces cerevisiae strain.World journal of microbiology & biotechnology · 2017Article
- When substrate inhibits and inhibitor activates: implications of β-glucosidases.Biotechnology for biofuels · 2017Article
- Engineering the GH1 β-glucosidase from Humicola insolens: Insights on the stimulation of activity by glucose and xylose.PloS one · 2017Article
- Using the β-glucosidase catalyzed reaction product glucose to improve the ionic liquid tolerance of β-glucosidases.Biotechnology for biofuels · 2016Article
Corrections and comments
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3 authors at 1 institution in 1 country.
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Abstract
Glucose sensitivity and pH and thermal stabilities of Trichoderma reesei Cel1A (Bgl II) were improved by site-directed mutagenesis of only two amino acid residues (L167W or P172L) at the entrance of the active site. The Cel1A mutant showed high glucose tolerance (50% of inhibitory concentration = 650 mM), glucose stimulation (2.0 fold at 50 mM glucose), and enhanced specific activity (2.4-fold) compared with those of the wild-type Cel1A. Furthermore, the mutant enzyme showed stability at a wide pH range of 4.5-9.0 and possessed high thermal stability up to 50 °C with 80% of the residual activities compared with the stability seen at the pH range of 6.5-7.0 and temperatures of up to 40 °C in the wild-type Cel1A. Kinetic studies for hydrolysis revealed that the Cel1A mutant was competitively inhibited by glucose at similar levels as the wild-type enzyme. Additionally, the mutant enzyme exhibited substrate inhibition, which gradually disappeared with an increasing glucose concentration. These data suggest that the glucose stimulation was caused by relieve the substrate inhibition in the presence of glucose. To conclude, all the properties improved by the mutagenesis would be great advantages in degradation of cellulosic biomass together with cellulases.
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