ArticleThe Journal of biological chemistry2014
Predicting enzyme adsorption to lignin films by calculating enzyme surface hydrophobicity.
Article in The Journal of biological chemistry, 2014. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 30 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
30 citing papers in PubMed, 135 citations in OpenAlex.
- Biochemical and inhibitor analysis of recombinant cellobiohydrolases from Phanerochaete chrysosporium.Biotechnology for biofuels and bioproducts · 2024Article
- Facile preparation of flame-retardant cellulose composite with biodegradable and water resistant properties for electronic device applications.Scientific reports · 2023Article
- Inhibitory effect of lignin on the hydrolysis of xylan by thermophilic and thermolabile GH11 xylanases.Biotechnology for biofuels and bioproducts · 2022Article
- Fluorescent Imaging of Extracellular Fungal Enzymes Bound onto Plant Cell Walls.International journal of molecular sciences · 2022Article
- Comparative Evaluation of Adsorption of Major Enzymes in a Cellulase Cocktail Obtained fromPolymers · 2022Article
- A review on marine plastisphere: biodiversity, formation, and role in degradation.Computational and structural biotechnology journal · 2022Review
- Recombinant Family 1 Carbohydrate-Binding Modules Derived From Fungal Cellulase Enhance Enzymatic Degradation of Lignocellulose as Novel Effective Accessory Protein.Frontiers in microbiology · 2022Article
- Influence of Calcium Silicate and Hydrophobic Agent Coatings on Thermal, Water Barrier, Mechanical and Biodegradation Properties of Cellulose.Nanomaterials (Basel, Switzerland) · 2021Article
- Investigating the effects of substrate morphology and experimental conditions on the enzymatic hydrolysis of lignocellulosic biomass through modeling.Biotechnology for biofuels · 2021Article
- Non-productive binding of cellobiohydrolase i investigated by surface plasmon resonance spectroscopy.Cellulose (London, England) · 2021Article
- Carbohydrate-binding moduleChemical science · 2020Article
- Exploring why sodium lignosulfonate influenced enzymatic hydrolysis efficiency of cellulose from the perspective of substrate-enzyme adsorption.Biotechnology for biofuels · 2020Article
- Studies of adsorptive capacity of bacterial β-glucosidases on lignocresol aiming the enzymatic recycling in bioprocesses.Biotechnology reports (Amsterdam, Netherlands) · 2019Article
- The Self-Assembly of Lignin and Its Application in Nanoparticle Synthesis: A Short Review.Nanomaterials (Basel, Switzerland) · 2019Review
- Enzymatic sugar production from elephant grass and reed straw through pretreatments and hydrolysis with addition of thioredoxin-His-S.Biotechnology for biofuels · 2019Article
- Cellulases adsorb reversibly on biomass lignin.Biotechnology and bioengineering · 2018Article
- From Protein Features to Sensing Surfaces.Sensors (Basel, Switzerland) · 2018Review
- Synchrotron Time-Lapse Imaging of Lignocellulosic Biomass Hydrolysis: Tracking Enzyme Localization by Protein Autofluorescence and Biochemical Modification of Cell Walls by Microfluidic Infrared Microspectroscopy.Frontiers in plant science · 2018Article
- Altering the linker in processive GH5 endoglucanase 1 modulates lignin binding and catalytic properties.Biotechnology for biofuels · 2018Article
- Microbial enzymes for the recycling of recalcitrant petroleum-based plastics: how far are we?Microbial biotechnology · 2017Review
Corrections and comments
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Authors and funding
12 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The inhibitory action of lignin on cellulase cocktails is a major challenge to the biological saccharification of plant cell wall polysaccharides. Although the mechanism remains unclear, hydrophobic interactions between enzymes and lignin are hypothesized to drive adsorption. Here we evaluate the role of hydrophobic interactions in enzyme-lignin binding. The hydrophobicity of the enzyme surface was quantified using an estimation of the clustering of nonpolar atoms, identifying potential interaction sites. The adsorption of enzymes to lignin surfaces, measured using the quartz crystal microbalance, correlates to the hydrophobic cluster scores. Further, these results suggest a minimum hydrophobic cluster size for a protein to preferentially adsorb to lignin. The impact of electrostatic contribution was ruled out by comparing the isoelectric point (pI) values to the adsorption of proteins to lignin surfaces. These results demonstrate the ability to predict enzyme-lignin adsorption and could potentially be used to design improved cellulase cocktails, thus lowering the overall cost of biofuel production.
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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.