Zobrazeno 1 - 6
of 6
pro vyhledávání: '"Nanna Sandager Røjel"'
Autor:
Jeppe Kari, Trine Holst Sørensen, Kenneth Jensen, Kim Borch, Nanna Sandager Røjel, Peter Westh, Corinna Schiano-di-Cola
Publikováno v:
Schiano-de-Cola, C, Røjel, N, Jensen, K, Kari, J, Sørensen, T H, Borch, K & Westh, P 2019, ' Systematic deletions in the cellobiohydrolase (CBH) Cel7A from the fungus Trichoderma reesei reveal flexible loops critical for CBH activity ', Journal of Biological Chemistry, vol. 294, no. 6, pp. 1807-1815 . https://doi.org/10.1074/jbc.RA118.006699
Glycoside hydrolase family 7 (GH7) cellulases are some of the most efficient degraders of cellulose, making them particularly relevant for industries seeking to produce renewable fuels from lignocellulosic biomass. The secretome of the cellulolytic m
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::1321de82b5e55212d219151d1ad7db60
https://doi.org/10.1074/jbc.ra118.006699
https://doi.org/10.1074/jbc.ra118.006699
Autor:
Jeppe Kari, Trine Holst Sørensen, Kim Borch, Malene B. Keller, Brett Mcbrayer, Silke Flindt Badino, Nanna Sandager Røjel, Peter Westh, Benedikt M. Blossom
Publikováno v:
The Journal of Biological Chemistry
Keller, M B, Badino, S F, Røjel, N, Sørensen, T H, Kari, J, McBrayer, B, Borch, K, Blossom, B M & Westh, P 2021, ' A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases ', Journal of Biological Chemistry, vol. 296, 100504 . https://doi.org/10.1016/j.jbc.2021.100504
Keller, M B, Badino, S F, Røjel, N, Sørensen, T H, Kari, J, Mcbrayer, B, Borch, K, Blossom, B M & Westh, P 2021, ' A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases ', Journal of Biological Chemistry, vol. 296, 100504 . https://doi.org/10.1016/j.jbc.2021.100504
Keller, M B, Badino, S F, Røjel, N, Sørensen, T H, Kari, J, McBrayer, B, Borch, K, Blossom, B M & Westh, P 2021, ' A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases ', Journal of Biological Chemistry, vol. 296, 100504 . https://doi.org/10.1016/j.jbc.2021.100504
Keller, M B, Badino, S F, Røjel, N, Sørensen, T H, Kari, J, Mcbrayer, B, Borch, K, Blossom, B M & Westh, P 2021, ' A comparative biochemical investigation of the impeding effect of C1-oxidizing LPMOs on cellobiohydrolases ', Journal of Biological Chemistry, vol. 296, 100504 . https://doi.org/10.1016/j.jbc.2021.100504
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 of reducin
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::60f0884f31c3f9ff4cab6efffabb9760
https://pubmed.ncbi.nlm.nih.gov/33675751
https://pubmed.ncbi.nlm.nih.gov/33675751
Autor:
Jeppe Kari, Ana Mafalda Cavaleiro, Silke Flindt Badino, Gustavo A. Molina, Nanna Sandager Røjel, Stefan Jarl Christensen, Kenneth Jensen, Corinna Schiano-di-Cola, Johan Pelck Olsen, Bartlomiej Kolaczkowski, Kim Borch, Nikolaj Spodsberg, Peter Westh, Malene B. Keller, Krogh Kbrm, Trine Holst Sørensen, Peters Ghj, Kay Schaller
Enzyme reactions, both in Nature and technical applications, commonly occur at the interface of immiscible phases. Nevertheless, stringent descriptions of interfacial enzyme catalysis remain sparse, and this is partly due to a shortage of coherent ex
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_________::3c71bb616cc34f4b09b77f7d808185b1
https://doi.org/10.1101/2020.05.20.105569
https://doi.org/10.1101/2020.05.20.105569
Autor:
Kim Borch, Nanna Sandager Røjel, Brett Mcbrayer, Trine Holst Sørensen, Peter Westh, Silke Flindt Badino, Michael Skovbo Windahl
Publikováno v:
Biochimica et biophysica acta. Proteins and proteomics. 1868(3)
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::8a12e0388dd53bc76333d0133504b9bc
https://pubmed.ncbi.nlm.nih.gov/31911207
https://pubmed.ncbi.nlm.nih.gov/31911207
Publikováno v:
Røjel, N, Kari, J, Sørensen, T H, Borch, K & Westh, P 2020, ' pH-profiles of cellulases depend on the substrate and architecture of the binding region ', Biotechnology and Bioengineering, vol. 117, no. 2, pp. 382-391 . https://doi.org/10.1002/bit.27206
Understanding the pH effect of cellulolytic enzymes is of great technological importance. In this study, we have examined the influence of pH on activity and stability for central cellulases (Cel7A, Cel7B, Cel6A from Trichoderma reesei, and Cel7A fro
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ce2e6509b131a54a921cbb9bc5663cbc
https://pubmed.ncbi.nlm.nih.gov/31631319
https://pubmed.ncbi.nlm.nih.gov/31631319
Autor:
Nanna Sandager Røjel, Kim Borch, Corinna Schiano-di-Cola, Peter Westh, Mafalda A. Cavaleiro, Silke Flindt Badino, Jeppe Kari, Trine Holst Sørensen, Radina Naytchova Tokin, Cynthia S. Vesterager, Stefan Jarl Christensen
Publikováno v:
Biotechnology and bioengineering. 115(4)
We have measured activity and substrate affinity of the thermostable cellobiohydrolase, Cel7A, from Rasamsonia emersonii over a broad range of temperatures. For the wild type enzyme, which does not have a Carbohydrate Binding Module (CBM), higher tem
Externí odkaz:
https://explore.openaire.eu/search/publication?articleId=doi_dedup___::7efba2d22c1f06c369a8f6b6b612cf54
https://pubmed.ncbi.nlm.nih.gov/29240229
https://pubmed.ncbi.nlm.nih.gov/29240229