Zobrazeno 1 - 10
of 17
pro vyhledávání: '"Michael Skovbo Windahl"'
Autor:
Peter Westh, Silke Flindt Badino, Kim Borch, Jeppe Kari, Søren Hvidt, Michael Skovbo Windahl, Stefan Jarl Christensen
Publikováno v:
Biotechnology and Bioengineering. 114:1639-1647
Synergy between cellulolytic enzymes is essential in both natural and industrial breakdown of biomass. In addition to synergy between endo- and exo-lytic enzymes, a lesser known but equally conspicuous synergy occurs among exo-acting, processive cell
Autor:
Corinna Schiano-di-Cola, Michael Skovbo Windahl, Stefan Jarl Christensen, Trine Holst Sørensen, Jens Preben Morth, Bartlomiej Kolaczkowski, Ana Mafalda Cavaleiro, Kim Borch, Peter Westh
Publikováno v:
Schiano di Cola, C, Kołaczkowski, B, Sørensen, T H, Christensen, S J, Cavaleiro, A M, Windahl, M S, Borch, K, Morth, J P & Westh, P 2020, ' Structural and biochemical characterization of a family 7 highly thermostable endoglucanase from the fungus Rasamsonia emersonii ', FEBS Journal, vol. 287, no. 12, pp. 2577-2596 . https://doi.org/10.1111/febs.15151
Thermostable cellulases from glycoside hydrolase family 7 (GH7) are the main components of enzymatic mixtures for industrial saccharification of lignocellulose. Activity improvement of these enzymes via rational design is a promising strategy to alle
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)
Autor:
Brett Mcbrayer, Peter Westh, Trine Holst Sørensen, Jeppe Kari, Kim Borch, Johan Pelck Olsen, Michael Skovbo Windahl
Publikováno v:
Biotechnology and Bioengineering. 114:53-62
Cel7A cellobiohydrolases perform processive hydrolysis on one strand of cellulose, which is threaded through the enzyme's substrate binding tunnel. The tunnel structure results from a groove in the catalytic domain, which is covered by a number of lo
Autor:
Kim Borch, Peter Westh, Nicolaj Cruys-Bagger, Michael Skovbo Windahl, Trine Holst Sørensen, Silke Flindt Badino
Publikováno v:
Journal of Biological Chemistry. 290:22193-22202
We measured hydrolytic rates of four purified cellulases in small increments of temperature (10-50 °C) and substrate loads (0-100 g/liter) and analyzed the data by a steady state kinetic model that accounts for the processive mechanism. We used wild
Autor:
Jeppe Kari, Nicolaj Cruys-Bagger, Kim Borch, Trine Holst Sørensen, Johan Pelck Olsen, Michael Skovbo Windahl, Kadri Alasepp, Peter Westh, Francieli Colussi
Publikováno v:
Journal of Biological Chemistry. 290:2444-2454
Cellobiohydrolases break down cellulose sequentially by sliding along the crystal surface with a single cellulose strand threaded through the catalytic tunnel of the enzyme. This so-called processive mechanism relies on a complex pattern of enzyme-su
Autor:
Kim Borch, Silke Flindt Badino, Kenneth Jensen, Michael Skovbo Windahl, Trine Holst Sørensen, Günther H.J. Peters, Peter Westh, Jenny Kim Bathke
Publikováno v:
Protein engineering, designselection : PEDS. 30(7)
Various cellulases consist of a catalytic domain connected to a carbohydrate-binding module (CBM) by a flexible linker peptide. The linker if often strongly O-glycosylated and typically has a length of 20-50 amino acid residues. Functional roles, oth
Publikováno v:
Analytical Biochemistry. 449:45-51
A new chromogenic substrate to assay the starch debranching enzymes limit dextrinase and pullulanase is described. The 2-chloro-4-nitrophenyl glycoside of a commercially available branched heptasaccharide (Glc-maltotriosyl-maltotriose) was found to b
Loop variants of the thermophile Rasamsonia emersonii Cel7A with improved activity against cellulose
Autor:
Trine Holst, Sørensen, Michael Skovbo, Windahl, Brett, McBrayer, Jeppe, Kari, Johan Pelck, Olsen, Kim, Borch, Peter, Westh
Publikováno v:
Biotechnology and bioengineering. 114(1)
Cel7A cellobiohydrolases perform processive hydrolysis on one strand of cellulose, which is threaded through the enzyme's substrate binding tunnel. The tunnel structure results from a groove in the catalytic domain, which is covered by a number of lo
Autor:
Birte Svensson, Marie Sofie Møller, Marie Bøjstrup, Anette Henriksen, Maher Abou Hachem, Monica M. Palcic, Lyann Sim, Ole Hindsgaul, Michael Skovbo Windahl
Publikováno v:
Møller, M S, Windahl, M S, Sim, L, Bøjstrup, M, Abou Hachem, M, Hindsgaul, O, Palcic, M, Svensson, B & Henriksen, A 2015, ' Oligosaccharide and Substrate Binding in the Starch Debranching Enzyme Barley Limit Dextrinase ', Journal of Molecular Biology, vol. 427, no. 6, Part B, pp. 1263-1277 . https://doi.org/10.1016/j.jmb.2014.12.019
Complete hydrolytic degradation of starch requires hydrolysis of both the α-1,4- and α-1,6-glucosidic bonds in amylopectin. Limit dextrinase (LD) is the only endogenous barley enzyme capable of hydrolyzing the α-1,6-glucosidic bond during seed ger