Search

Your search keyword '"Felby, Claus"' showing total 777 results
Start Over Author "Felby, Claus"
777 results on '"Felby, Claus"'

2. Undefined cellulase formulations hinder scientific reproducibility

Author

Himmel, Michael E, Abbas, Charles A, Baker, John O, Bayer, Edward A, Bomble, Yannick J, Brunecky, Roman, Chen, Xiaowen, Felby, Claus, Jeoh, Tina, Kumar, Rajeev, McCleary, Barry V, Pletschke, Brett I, Tucker, Melvin P, Wyman, Charles E, and Decker, Stephen R

Subjects
Biological Sciences, Industrial Biotechnology, Cellulase, Cellulose, Biofuels, Assays, Commercial cellulase formulations, Chemical Engineering, Biochemistry and cell biology, Industrial biotechnology
Abstract

In the shadow of a burgeoning biomass-to-fuels industry, biological conversion of lignocellulose to fermentable sugars in a cost-effective manner is key to the success of second-generation and advanced biofuel production. For the effective comparison of one cellulase preparation to another, cellulase assays are typically carried out with one or more engineered cellulase formulations or natural exoproteomes of known performance serving as positive controls. When these formulations have unknown composition, as is the case with several widely used commercial products, it becomes impossible to compare or reproduce work done today to work done in the future, where, for example, such preparations may not be available. Therefore, being a critical tenet of science publishing, experimental reproducibility is endangered by the continued use of these undisclosed products. We propose the introduction of standard procedures and materials to produce specific and reproducible cellulase formulations. These formulations are to serve as yardsticks to measure improvements and performance of new cellulase formulations.

Published
2017

22. Oxidative cleavage of polysaccharides by a termite-derived superoxide dismutase boosts the degradation of biomass by glycoside hydrolases

Author

Mandelli, Fernanda, Tramontina, Robson, Cannella, David, Paradisi, Alessandro, Ciano, Luisa, Ferreira, Marcel, Rodrigues, Gisele Nunes, Alvarez, Thabata Maria, Mofatto, Luciana Souto, Carazzolle, Marcelo Falsarella, Leme, Adriana Paes, Costa-Leonardo, Ana Maria, Oliveira Neto, Mario, Davies, Gideon, Felby, Claus, Walton, Paul Howard, and Squina, Fabio

Subjects
Environmental Chemistry, Pollution
Abstract

Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in lignocellulose degradation, suggesting hereto unknown enzymatic activities in their digestome. Herein, we demonstrate that an ancient redox-active enzyme encoded by the lower termite Coptotermes gestroi, a Cu/Zn superoxide dismutase (CgSOD-1), plays a previously unknown role in plant biomass degradation. We show that CgSOD-1 transcripts and peptides are up-regulated in response to an increased level of lignocellulose recalcitrance and that CgSOD-1 localizes in the lumen of the fore- and midguts of C. gestroi together with termite main cellulase, CgEG-1-GH9. CgSOD-1 boosts the saccharification of polysaccharides by CgEG-1-GH9. We show that the boosting effect of CgSOD-1 involves an oxidative mechanism of action in which CgSOD-1 generates reactive oxygen species that subsequently cleave the polysaccharide. SOD-type enzymes constitute a new addition to the growing family of oxidases, ones which are up-regulated when exposed to recalcitrant polysaccharides, and that are used by Nature for biomass degradation.

Published
2022

23. Oxidative cleavage of polysaccharides by a termite-derived superoxide dismutase boosts the degradation of biomass by glycoside hydrolases

Author

Franco Cairo, João Paulo, Mandelli, Fernanda, Tramontina, Robson, Cannella, David, Paradisi, Alessandro, Ciano, Luisa, Ferreira, Marcel, Liberato, Marcelo Vizoná, Brenelli, Lívia, Gonçalves, Thiago, Rodrigues, Gisele Nunes, Alvarez, Thabata Maria, Mofatto, Luciana Souto, Carazzolle, Marcelo Falsarella, Pradella, José Geraldo, Leme, Adriana Paes, Costa-Leonardo, Ana Maria, Oliveira Neto, Mario, Damasio, André, Davies, Gideon, Felby, Claus, Walton, Paul Howard, and Squina, Fabio

Abstract

Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in lignocellulose degradation, suggesting hereto unknown enzymatic activities in their digestome. Herein, we demonstrate that an ancient redox-active enzyme encoded by the lower termite Coptotermes gestroi, a Cu/Zn superoxide dismutase (CgSOD-1) plays a previously unknown role in plant biomass degradation. We show that CgSOD-1 transcripts and peptides are up-regulated in response to an increased level of lignocellulose recalcitrance and that CgSOD-1 localizes in the lumen of the fore- and midguts of C. gestroi together with termite main cellulase, CgEG-1-GH9. CgSOD-1 boosts the saccharification of polysaccharides by CgEG-1-GH9. We show that the boosting effect of CgSOD-1 involves an oxidative mechanism of action in which CgSOD-1 generates reactive oxygen species that subsequently cleave the polysaccharide. SOD-type enzymes constitute a new addition to the growing family of oxidases, ones which are up-regulated when exposed to recalcitrant polysaccharides, and that are used by Nature for biomass degradation.

Published
2022

25. Oxidative cleavage of polysaccharides by a termite-derived superoxide dismutase boosts the degradation of biomass by glycoside hydrolases

Author

Franco Cairo, João Paulo L., Mandelli, Fernanda, Tramontina, Robson, Cannella, David, Paradisi, Alessandro, Ciano, Luisa, Ferreira, Marcel R., Liberato, Marcelo V., Brenelli, Lívia B., Goncalves, Thiago A., Rodrigues, Gisele N., Alvarez, Thabata M., Mofatto, Luciana S., Carazzolle, Marcelo F., Pradella, Jose G. C., Leme, Adriana F. Paes, Costa-Leonardo, Ana M., Oliveira-Neto, Mário, Damasio, André, Davies, Gideon J., Felby, Claus, Walton, Paul H., Squina, Fabio M., Franco Cairo, João Paulo L., Mandelli, Fernanda, Tramontina, Robson, Cannella, David, Paradisi, Alessandro, Ciano, Luisa, Ferreira, Marcel R., Liberato, Marcelo V., Brenelli, Lívia B., Goncalves, Thiago A., Rodrigues, Gisele N., Alvarez, Thabata M., Mofatto, Luciana S., Carazzolle, Marcelo F., Pradella, Jose G. C., Leme, Adriana F. Paes, Costa-Leonardo, Ana M., Oliveira-Neto, Mário, Damasio, André, Davies, Gideon J., Felby, Claus, Walton, Paul H., and Squina, Fabio M.

Abstract

Wood-feeding termites effectively degrade plant biomass through enzymatic degradation. Despite their high efficiencies, however, individual glycoside hydrolases isolated from termites and their symbionts exhibit anomalously low effectiveness in lignocellulose degradation, suggesting hereto unknown enzymatic activities in their digestome. Herein, we demonstrate that an ancient redox-active enzyme encoded by the lower termite Coptotermes gestroi, a Cu/Zn superoxide dismutase (CgSOD-1), plays a previously unknown role in plant biomass degradation. We show that CgSOD-1 transcripts and peptides are up-regulated in response to an increased level of lignocellulose recalcitrance and that CgSOD-1 localizes in the lumen of the fore- and midguts of C. gestroi together with termite main cellulase, CgEG-1-GH9. CgSOD-1 boosts the saccharification of polysaccharides by CgEG-1-GH9. We show that the boosting effect of CgSOD-1 involves an oxidative mechanism of action in which CgSOD-1 generates reactive oxygen species that subsequently cleave the polysaccharide. SOD-type enzymes constitute a new addition to the growing family of oxidases, ones which are up-regulated when exposed to recalcitrant polysaccharides, and that are used by Nature for biomass degradation.

Published
2022

26. Removal of hard COD from acidic eucalyptus kraft pulp bleach plant effluent streams using oxidoreductases

Author

Herold-Majumdar, Owik Matthias, Lopez Pita, Sabela, Dominguez Estevez, Fernando, Wawrzynczyk, Joanna, Loureiro, Pedro E.G., Felby, Claus, Herold-Majumdar, Owik Matthias, Lopez Pita, Sabela, Dominguez Estevez, Fernando, Wawrzynczyk, Joanna, Loureiro, Pedro E.G., and Felby, Claus

Abstract

The bleach plant of a pulp and paper (P&P) mill presents a major source of wastewater containing toxic organic matter characterized as chemical oxygen demand (COD). Due to their high oxidizing power, oxidoreductases hold promise to be a key solution for the removal of dissolved organic material. Here, four oxidoreductases from different enzyme families were selected to treat bleach plant effluents. Haloperoxidase treatment of the final effluent resulted in the highest levels of decolorization (71%) and reduction of aromatic compounds (36%). Using single compound analysis, 27 low molecular weight compounds were found to be persistent throughout the wastewater treatment process and, therefore, classified as hard COD. The tested enzymes efficiently removed several of the identified COD compounds. Hence, this study suggests that the application of oxidoreductases will serve as an environmental-friendly solution for reducing waste from P&P production.

Published
2022

32. Enzymatic Bonding Systems

Author

Felby, Claus, Olesen, Per Ole, Prasad, Paras N., editor, Mark, James E., editor, Kandil, Sherif H., editor, and Kafafi, Zakya H., editor

Published
1998
Full Text
View/download PDF

43. Double bonus:surfactant-assisted biomass pelleting benefits both the pelleting process and subsequent enzymatic saccharification of the pretreated pellets

Author

Gong, Chunxiao, Bryant, Nathan, Meng, Xianzhi, Bhagia, Samarthya, Pu, Yunqiao, Xin, Donglin, Bender Koch, Christian, Felby, Claus, Thygesen, Lisbeth Garbrecht, Ragauskas, Arthur, Thomsen, Sune Tjalfe, Gong, Chunxiao, Bryant, Nathan, Meng, Xianzhi, Bhagia, Samarthya, Pu, Yunqiao, Xin, Donglin, Bender Koch, Christian, Felby, Claus, Thygesen, Lisbeth Garbrecht, Ragauskas, Arthur, and Thomsen, Sune Tjalfe

Published
2021

Catalog

Books, media, physical & digital resources
See catalog results