%0 Journal Article %A Broeker, Jannis %A Mechelke, Matthias %A Baudrexl, Melanie %A Mennerich, Denise %A Hornburg, Daniel %A Mann, Matthias %A Schwarz, Wolfgang %A Liebl, Wolfgang %A Zverlov, Vladimir %D 2018 %T MOESM1 of The hemicellulose-degrading enzyme system of the thermophilic bacterium Clostridium stercorarium: comparative characterisation and addition of new hemicellulolytic glycoside hydrolases %U https://springernature.figshare.com/articles/journal_contribution/MOESM1_of_The_hemicellulose-degrading_enzyme_system_of_the_thermophilic_bacterium_Clostridium_stercorarium_comparative_characterisation_and_addition_of_new_hemicellulolytic_glycoside_hydrolases/7006562 %R 10.6084/m9.figshare.7006562.v1 %2 https://springernature.figshare.com/ndownloader/files/12854516 %K Biomass degradation %K Enzyme characterisation %K Proteome analysis %K Arabinoxylan %K Xylanase %K Substrate specificity %K Product specificity %X Additional file 1. This file contains additional tables and figures as follows: (i) Table S1. PCR primer for the amplification of the 50 selected glycoside hydrolase genes of C. stercorarium. (ii) Table S2. Polysaccharide and p-nitrophenyl substrates including the final concentration in enzymatic assays. (iii) Table S3. Glycoside hydrolase (GH) families present in the C. stercorarium genome. (iv) Figure S1. SDS-PAGEs of 10 examples of the 50 C. stercorarium proteins recombinantly produced by E. coli and purified by IMAC. (v) Figure S2. Schematic structure of the glycoside hydrolases with proven activity from C. stercorarium. (vi) Table S4. Studied enzymes in the secretome or intracellular proteome of C. stercorarium analysed by LC-MS/MS. (vii) Figure S3. Hydrolytic products of different polysaccharides analysed by Thin-layer chromatography (TLC). Polysaccharides were hydrolysed by a) Xyn10C, b) Xyn11A, c) Xyn10D, d) Arf51B, e) Arf43C, f) Axh43A, g) Abn43A, h) Cel9Z, i) Man26A, j) Bga35A, k) Bga2B. (viii) Figure S4. Relative activity of characterised enzymes at different pH. pH profiles of a) xylanases Xyn11A & Xyn10B-D, b) Axh43A and α-arabinofuranosidases Arf51B & Arf43C, c) β-galactosidases Bga2B & Bga35A, d) Bxl3B, Cel9Z, Man26A, and Abn43A. (ix) Figure S5. Relative activity of characterised enzymes at different temperatures. Temperature profiles of a) xylanases Xyn11A & Xyn10B-D, b) Axh43A and α-arabinofuranosidases Arf51B & Arf43C, c) β-galactosidases Bga2B & Bga35A, d) Bxl3B, Cel9Z, Man26A, and Abn43A. %I figshare