Recombinant production and characterisation of two related GH5 endo-β-1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly different transglycosylation capacity

Autor: Martin J. Baumann, Hiroyuki Nakai, Adiphol Dilokpimol, Birte Svensson, Charlotte Held Gotfredsen, Natsuko Nakai, Maher Abou Hachem

Publikováno v: Dilokpimol, A, Nakai, H, Gotfredsen, C H, Baumann, M J, Nakai, N, Abou Hachem, M & Svensson, B 2011, ' Recombinant production and characterisation of two related GH5 endo-β-1,4-mannanases from Aspergillus nidulans FGSC A4 showing distinctly different transglycosylation capacity ', Biochimica et Biophysica Acta, vol. 1814, no. 12, pp. 1720-1729 . https://doi.org/10.1016/j.bbapap.2011.08.003

The glycoside hydrolase family 5 (GH5) endo-β-1,4-mannanases ManA and ManC from Aspergillus nidulans FGSC A4 were produced in Pichia pastoris X33 and purified in high yields of 120 and 145mg/L, respectively, from the culture supernatants. Both enzym

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::ba68236e4a4c9fd53b8574205e1f75fc
https://cris.vtt.fi/en/publications/0f378165-b3ac-479c-903f-7178859aba0c

Advantages of isothermal titration calorimetry for xylanase kinetics in comparison to chemical-reducing-end assays

Autor: Martin J. Baumann, Nina Lei, Kim Borch, Peter Westh, Kristian B. R. M. Krogh, Leigh Murphy

Publikováno v: Roskilde University

In lignocellulosic raw materials for biomass conversion, hemicelluloses constitute a substantial fraction, with xylan being the primary part. Although many pretreatments reduce the amount or change the distribution of xylan, it is important to degrad

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::a9ac1f64f807956f2a4779021ec56ad0
https://doi.org/10.1016/j.ab.2010.11.001

An enzymatic signal amplification system for calorimetric studies of cellobiohydrolases

Autor: Martin J. Baumann, Kim Borch, Leigh Murphy, Peter Westh, Matthew Sweeney

Publikováno v: Analytical Biochemistry. 404:140-148

The study of cellulolytic enzymes has traditionally been carried out using endpoint measurements by quantitation of reaction products using high-performance liquid chromatography (HPLC) or overall determination of produced reducing ends. To measure c

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::f5f0df6340f0ec8b4262dfbde3f94110
https://doi.org/10.1016/j.ab.2010.04.020

Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum

Autor: Martin J. Baumann, Jens Ø. Duus, Yvonne Westphal, Bent O. Petersen, Hiroyuki Nakai, Maher Abou Hachem, Karin Mannerstedt, Adiphol Dilokpimol, Henk A. Schols, Birte Svensson

Publikováno v: Nakai, H, Hachem, M A, Petersen, B O, Westphal, Y, Mannerstedt, K, Baumann, M J, Dilokpimol, A, Schols, H A, Duus, J Ø & Svensson, B 2010, ' Efficient chemoenzymatic oligosaccharide synthesis by reverse phosphorolysis using cellobiose phosphorylase and cellodextrin phosphorylase from Clostridium thermocellum ', Biochimie, vol. 92, no. 12, pp. 1818-26 . https://doi.org/10.1016/j.biochi.2010.07.013
Biochimie 92 (2010) 12
Biochimie, 92(12), 1818-1826

Inverting cellobiose phosphorylase (CtCBP) and cellodextrin phosphorylase (CtCDP) from Clostridium thermocellum ATCC27405 of glycoside hydrolase family 94 catalysed reverse phosphorolysis to produce cellobiose and cellodextrins in 57% and 48% yield f

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::217238c37d3dc9786f51b6ca6d1ceed3
https://doi.org/10.1016/j.biochi.2010.07.013

Mechanism-based Labeling Defines the Free Energy Change for Formation of the Covalent Glycosyl-enzyme Intermediate in a Xyloglucan endo-Transglycosylase

Autor: Kathleen Piens, Martin J. Baumann, Gustav Sundqvist, Sylvain Cottaz, Hugues Driguez, Marc Saura-Valls, Antoni Planas, Harry Brumer, Tuula T. Teeri, Régis Fauré

Publikováno v: Journal of Biological Chemistry. 283:21864-21872

Xyloglucan endo-transglycosylases (XETs) are key enzymes involved in the restructuring of plant cell walls during morphogenesis. As members of glycoside hydrolase family 16 (GH16), XETs are predicted to employ the canonical retaining mechanism of gly

Externí odkaz: https://explore.openaire.eu/search/publication?articleId=doi_dedup___::aa2b6898050673e94bb6d0fa360f7e7f
https://doi.org/10.1074/jbc.m803057200