ArticleBiotechnology for biofuels2013
Selecting β-glucosidases to support cellulases in cellulose saccharification.
Article in Biotechnology for biofuels, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 53 papers.
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Who cites it
53 citing papers in PubMed, 155 citations in OpenAlex.
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- Characterization of an alkali- and glucose-tolerant β-glucosidase from Karamay saline-alkali soil and its structural basis for glucose tolerance.BMC biotechnology · 2026Article
- Phytochemical Analysis, GC-MS Chemical Profiling, and In Vitro Antidiabetic Evaluation of South AfricanCurrent issues in molecular biology · 2026Article
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- Biochemical and Structural Characterization of a Highly Glucose-Tolerant β-Glucosidase from the TermiteInternational journal of molecular sciences · 2025Article
- Key cellulase components synergizing with lactic acid bacteria to degrade alfalfa lignocellulose to improve lactic acid fermentation.Frontiers in microbiology · 2025Article
- A novel GH3-β-glucosidase from soda lake metagenomic libraries with desirable properties for biomass degradation.Scientific reports · 2024Article
- A Recombinant Thermophilic and Glucose-Tolerant GH1 β-Glucosidase Derived from Hehua Hot Spring.Molecules (Basel, Switzerland) · 2024Article
- Constitutive overexpression of cellobiohydrolase 2 inEngineering microbiology · 2023Article
- Characterization of a New Glucose-Tolerant GH1 β-Glycosidase fromInternational journal of molecular sciences · 2023Article
- Biochemical characterization of a novel glucose-tolerant GH3 β-glucosidase (Bgl1973) from Leifsonia sp. ZF2019.Applied microbiology and biotechnology · 2022Article
- Characterization of a novel recombinant halophilic β-glucosidase of Trichoderma harzianum derived from Hainan mangrove.BMC microbiology · 2022Article
- Transmembrane transport process and endoplasmic reticulum function facilitate the role of gene cel1b in cellulase production of Trichoderma reesei.Microbial cell factories · 2022Article
- Co-immobilization of Cellulase and β-Glucosidase into Mesoporous Silica Nanoparticles for the Hydrolysis of Cellulose Extracted fromLangmuir : the ACS journal of surfaces and colloids · 2022Article
- Biological cellulose saccharification using a coculture of Clostridium thermocellum and Thermobrachium celere strain A9.Applied microbiology and biotechnology · 2022Article
- Mechanism of differential expression of β-glucosidase genes in functional microbial communities in response to carbon catabolite repression.Biotechnology for biofuels and bioproducts · 2022Article
- Fungal cellulases: protein engineering and post-translational modifications.Applied microbiology and biotechnology · 2022Review
- Improving the Substrate Affinity and Catalytic Efficiency of β-Glucosidase Bgl3A fromBiomolecules · 2021Article
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
backgroundEnzyme end-product inhibition is a major challenge in the hydrolysis of lignocellulose at a high dry matter consistency. β-glucosidases (BGs) hydrolyze cellobiose into two molecules of glucose, thereby relieving the product inhibition of cellobiohydrolases (CBHs). However, BG inhibition by glucose will eventually lead to the accumulation of cellobiose and the inhibition of CBHs. Therefore, the kinetic properties of candidate BGs must meet the requirements determined by both the kinetic properties of CBHs and the set-up of the hydrolysis process.
resultsThe kinetics of cellobiose hydrolysis and glucose inhibition of thermostable BGs from Acremonium thermophilum (AtBG3) and Thermoascus aurantiacus (TaBG3) was studied and compared to Aspergillus sp. BG purified from Novozyme®188 (N188BG). The most efficient cellobiose hydrolysis was achieved with TaBG3, followed by AtBG3 and N188BG, whereas the enzyme most sensitive to glucose inhibition was AtBG3, followed by TaBG3 and N188BG. The use of higher temperatures had an advantage in both increasing the catalytic efficiency and relieving the product inhibition of the enzymes. Our data, together with data from a literature survey, revealed a trade-off between the strength of glucose inhibition and the affinity for cellobiose; therefore, glucose-tolerant BGs tend to have low specificity constants for cellobiose hydrolysis. However, although a high specificity constant is always an advantage, in separate hydrolysis and fermentation, the priority may be given to a higher tolerance to glucose inhibition.
conclusionsThe specificity constant for cellobiose hydrolysis and the inhibition constant for glucose are the most important kinetic parameters in selecting BGs to support cellulases in cellulose hydrolysis.
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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.