A5041118875- Biofuel production and bioconversion
- Enzyme Catalysis and Immobilization
- Enzyme Production and Characterization
- Enzyme-mediated dye degradation
- Advanced Cellulose Research Studies
- Catalysis for Biomass Conversion
- Microbial Metabolic Engineering and Bioproduction
- Protein Structure and Dynamics
- Enzyme function and inhibition
- Enzyme Structure and Function
- Electrochemical sensors and biosensors
- Carbon Dioxide Capture Technologies
- Hemoglobin structure and function
- Analytical Chemistry and Chromatography
- Innovative Microfluidic and Catalytic Techniques Innovation
- Algal biology and biofuel production
- Microplastics and Plastic Pollution
- Chemistry and Chemical Engineering
- Recycling and Waste Management Techniques
- Polysaccharides and Plant Cell Walls
- Adsorption, diffusion, and thermodynamic properties of materials
- biodegradable polymer synthesis and properties
Technical University of Denmark
2020-2024
Roskilde University
2014-2020
Swedish Chemicals Agency
2018
John Wiley & Sons (United States)
2017-2018
Hudson Institute
2018
Bioengineering Center
2017
National Center for Genetic Engineering and Biotechnology
2017
Novozymes (Denmark)
2015
The Sabatier principle states that optimal catalysis occurs when interactions between catalyst and substrate are of intermediary strength. Although qualitative in nature, this concept has proven extremely useful within (nonbiochemical) heterogeneous catalysis. In the current work, we show may be applied to an interfacial enzyme reaction. Specifically, studied breakdown cellulose by different cellulases (wild types variants) found results could rationalized so-called volcano plots emblematic...
Lytic polysaccharide monooxygenases (LPMOs) have attracted attention due to their ability boost cellulolytic enzyme cocktails for application in biorefineries. However, the interplay between LPMOs and individual glycoside hydrolases remains poorly understood. We investigated how activity of two cellobiohydrolases (Cel7A Cel6A) an endoglucanase (Cel7B) from Trichoderma reesei were affected by a C1-oxidizing LPMO Thielavia terrestris (TtAA9). quantified products mixture hydrolase estimated...
Abstract Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions interfacial enzyme catalysis remain sparse, this is partly due to a shortage coherent experimental data guide assess such work. In work, we produced kinetically characterized 83 cellulases, which revealed conspicuous linear free energy relationship (LFER) between substrate binding strength activation barrier. The scaling occurred...
Synergy between cellulolytic enzymes is essential in both natural and industrial breakdown of biomass. In addition to synergy endo- exo-lytic enzymes, a lesser known but equally conspicuous occurs among exo-acting, processive cellobiohydrolases (CBHs) such as Cel7A Cel6A from Hypocrea jecorina. We studied this system using microcrystalline cellulose substrate found degree 1.3 2.2 depending on the experimental conditions. enzyme variants without carbohydrate binding module (CBM) its linker...
The cellobiohydrolase (CBH) Cel6A is an important component of enzyme cocktails for industrial degradation lignocellulosic biomass. However, the kinetics this acting on its natural, insoluble substrate remains sparsely investigated. Here, we studied from Trichoderma reesei with respect to adsorption, processivity, and both in steady-state pre-steady-state regimes, microcrystalline amorphous cellulose. We found that slow dissociation (koff ) was limiting overall reaction rate, suggest leads...
The ascomycete fungus Trichoderma reesei is the predominant source of enzymes for industrial conversion lignocellulose. Its glycoside hydrolase family 7 cellobiohydrolase (GH7 CBH) TreCel7A constitutes nearly half enzyme cocktail by weight and major workhorse in cellulose hydrolysis process. orthologs from atroviride (TatCel7A) harzianum (ThaCel7A) show high sequence identity with TreCel7A, ~ 80%, represent naturally evolved combinations cellulose-binding tunnel-enclosing loop motifs, which...
Adsorption of cellulases on the cellulose surface is an integral part catalytic mechanism, and a detailed description adsorption process therefore required for fundamental understanding this industrially important class enzymes. However, mode has proven intricate, several key questions remain open. Perhaps most notably it not clear whether adsorbed enzyme in dynamic equilibrium with free population or irreversibly associated no slow dissociation. To address this, we have systematically...
Various cellulases consist of a catalytic domain connected to carbohydrate-binding module (CBM) by flexible linker peptide. The if often strongly O-glycosylated and typically has length 20-50 amino acid residues. Functional roles, other than connecting the two folded domains, its glycans, have been widely discussed, but experimental evidence remains sparse. One most studied cellulose degrading enzymes is multi-domain cellobiohydrolase Cel7A from Hypocrea jecorina. Here, we designed variants...
This work shows that differential scanning calorimetry (DSC) can be used to monitor the stability of substrate-adsorbed cellulases during long-term hydrolysis insoluble cellulose. Thermal transitions adsorbed enzyme were measured regularly in subsets a progressing hydrolysis, and size transition peak was as gauge population native enzyme. Analogous measurements made for enzymes pure buffer. Investigations two cellobiohydrolases, Cel6A Cel7A, from Trichoderma reesei, which is an anamorph...
Lytic polysaccharide monooxygenases (LPMOs) are known to act synergistically with glycoside hydrolases in industrial cellulolytic cocktails. However, a few studies have reported severe impeding effects of C1-oxidizing LPMOs on the activity reducing-end cellobiohydrolases. The mechanism for this effect remains unknown, but it may important implications as cellobiohydrolases make up significant part such To elucidate whether is general different and study underlying mechanism, we conducted...
Abstract We have measured activity and substrate affinity of the thermostable cellobiohydrolase, Cel7A, from Rasamsonia emersonii over a broad range temperatures. For wild type enzyme, which does not Carbohydrate Binding Module (CBM), higher temperature only led to moderately increased against cellulose, we ascribed this pronounced, induced desorption enzyme surface. also tested “high affinity” variant R. Cel7A with linker CBM related enzyme. At room temperature, was similar type, but more...
Abstract The glycoside hydrolase (GH) family 6 is an important group of enzymes that constitute essential part industrial enzyme cocktails used to convert lignocellulose into fermentable sugars. In nature, from this often have a carbohydrate binding module (CBM) the CBM 1. These modules are known promote adsorption cellulose surface and influence enzymatic activity. Here, we investigated functional diversity CBMs found within GH6 family. This was done by constructing five chimeric based on...
The kinetic theory of enzymes that modify insoluble substrates is still underdeveloped, despite the prevalence this type reaction both in vivo and industrial applications. Here, we present a steady-state approach to investigate inhibition occurring at solid-liquid interface. We propose conduct experiments under enzyme excess (E0 ≫ S0), i.e. opposite limit compared with conventional Michaelis-Menten framework. This inverse condition practical for elucidates how inhibitor reduces activity...
Direct removal of carbon dioxide from atmospheric air has been widely advocated as a key tool in the strive towards zero emissions. One class technology for direct capture (DAC) uses aqueous sorbents air-liquid contactors to extract CO2. Here we present first systematic data on enzyme assisted DAC and show that even very low (sub µM) concentrations carbonic anhydrase (CA) exert strong acceleration CO2 absorption. We also found CA promoted ability retain high efficiency flow rate was raised...
Abstract Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions interfacial enzyme catalysis remain sparse, this is partly due to a shortage coherent experimental data guide assess such work. We have produced kinetically characterized 83 cellulases, which revealed conspicuous linear free energy relationship (LFER) between strength substrate binding activation barrier. This common scaling occurred...