ArticleBiotechnology for biofuels2013
Product inhibition of cellulases studied with 14C-labeled cellulose substrates.
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 37 papers.
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Who cites it
37 citing papers in PubMed.
- Proteomic Characterization of theInternational journal of molecular sciences · 2025Article
- Advancing continuous enzymatic hydrolysis for improved biomass saccharification.Biotechnology for biofuels and bioproducts · 2025Article
- The Effect of Technological Conditions on ABE Fermentation and Butanol Production of Rye Straw and the Composition of Volatile Compounds.Molecules (Basel, Switzerland) · 2024Article
- A Multiomics Perspective on Plant Cell Wall-Degrading Enzyme Production: Insights from the Unexploited FungusJournal of fungi (Basel, Switzerland) · 2024Article
- 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
- Metagenomic mining and structure-function studies of a hyper-thermostable cellobiohydrolase from hot spring sediment.Communications biology · 2022Article
- Article
- LPMOInternational journal of molecular sciences · 2020Article
- Substrate-Related Factors Affecting Cellulosome-Induced Hydrolysis for Lignocellulose Valorization.International journal of molecular sciences · 2019Review
- Heterologous co-expression of two β-glucanases and a cellobiose phosphorylase resulted in a significant increase in the cellulolytic activity of the Caldicellulosiruptor bescii exoproteome.Journal of industrial microbiology & biotechnology · 2019Article
- Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungusThe Journal of biological chemistry · 2019Article
- Unique genetic cassettes in aScience advances · 2018Article
- Structure, computational and biochemical analysis of PcCel45A endoglucanase from Phanerochaete chrysosporium and catalytic mechanisms of GH45 subfamily C members.Scientific reports · 2018Article
- Expression of a Cellobiose Phosphorylase from Thermotoga maritima in Caldicellulosiruptor bescii Improves the Phosphorolytic Pathway and Results in a Dramatic Increase in Cellulolytic Activity.Applied and environmental microbiology · 2018Article
- Online evaluation of the metabolic activity ofJournal of biological engineering · 2018Article
- Fine-Tuned Enzymatic Hydrolysis of Organosolv Pretreated Forest Materials for the Efficient Production of Cellobiose.Frontiers in chemistry · 2018Article
- Role for ribosome-associated complex and stress-seventy subfamily B (RAC-Ssb) in integral membrane protein translation.The Journal of biological chemistry · 2017Article
- Heterologous expression of a β-D-glucosidase in Caldicellulosiruptor bescii has a surprisingly modest effect on the activity of the exoproteome and growth on crystalline cellulose.Journal of industrial microbiology & biotechnology · 2017Article
- 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
- Comparative insights into the saccharification potentials of a relatively unexplored but robustBiotechnology for biofuels · 2017Article
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Abstract
backgroundAs a green alternative for the production of transportation fuels, the enzymatic hydrolysis of lignocellulose and subsequent fermentation to ethanol are being intensively researched. To be economically feasible, the hydrolysis of lignocellulose must be conducted at a high concentration of solids, which results in high concentrations of hydrolysis end-products, cellobiose and glucose, making the relief of product inhibition of cellulases a major challenge in the process. However, little quantitative information on the product inhibition of individual cellulases acting on cellulose substrates is available because it is experimentally difficult to assess the hydrolysis of the heterogeneous polymeric substrate in the high background of added products.
resultsThe cellobiose and glucose inhibition of thermostable cellulases from Acremonium thermophilum, Thermoascus aurantiacus, and Chaetomium thermophilum acting on uniformly 14C-labeled bacterial cellulose and its derivatives, 14C-bacterial microcrystalline cellulose and 14C-amorphous cellulose, was studied. Cellulases from Trichoderma reesei were used for comparison. The enzymes most sensitive to cellobiose inhibition were glycoside hydrolase (GH) family 7 cellobiohydrolases (CBHs), followed by family 6 CBHs and endoglucanases (EGs). The strength of glucose inhibition followed the same order. The product inhibition of all enzymes was relieved at higher temperatures. The inhibition strength measured for GH7 CBHs with low molecular-weight model substrates did not correlate with that measured with 14C-cellulose substrates.
conclusionsGH7 CBHs are the primary targets for product inhibition of the synergistic hydrolysis of cellulose. The inhibition must be studied on cellulose substrates instead of on low molecular-weight model substrates when selecting enzymes for lignocellulose hydrolysis. The advantages of using higher temperatures are an increase in the catalytic efficiency of enzymes and the relief of product inhibition.
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