Inhibition of hyperthermostable xylanases by superbase ionic liquids |
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| Affiliation: | 1. Laboratory of Applied Microbiology, Faculty of Nature Sciences and Life, University of Bejaia, Targa Ouzemmour, 06000, Algeria;2. Department of Chemistry, FI-00014, University of Helsinki, Finland;3. Department of Bioproducts and Biosystems, School of Chemical Engineering, FI-00076, Aalto University, Finland;4. School of Forest Sciences, University of Eastern Finland, FI-80101, Joensuu, Finland;1. College of Physics and Chemistry, Henan Polytechnic University, Jiaozuo 454003, China;2. Technology Center of Ningbo Entry⿿Exit Inspection and Quarantine Bureau, Ningbo 315012, China;1. Department of Microbiology, Science Laboratory Building, Faculty of Science, King Mongkut''s University of Technology, Thonburi, Thailand;2. Theoretical and Computational Physics Group, Department of Physics, KMUTT, Thailand, Faculty of Science, King Mongkut''s University of Technology, Thonburi, Thailand;3. Theoretical and Computational Science Center (TaCS), Science Laboratory Building, Faculty of Science, King Mongkut''s University of Technology Thonburi (KMUTT), 126 Pracha-Uthit Road, Bang Mod, Thrung Khru, Bangkok, 10140, Thailand;4. Department of Physics, Faculty of Science, Kano University of Science and Technology, Wudil, Kano, Nigeria;1. Zoology Department, College of Sciences, King Saud University, P.O. Box 2455, Riyadh, 11451, Saudi Arabia;2. DNA Research Chair, Zoology Department, College of Sciences, King Saud University, P.O. Box 2455, Riyadh, 11451, Saudi Arabia;3. Department of Pharmacognosy, College of Pharmacy, King Saud University, P.O. Box 2457, Riyadh, 11451, Saudi Arabia;4. Department of Botany & Microbiology, College of Sciences, King Saud University, P.O Box 2455, Riyadh, 11451, Saudi Arabia;1. Departamento de Biotecnología, Universidad Autónoma Metropolitana-Iztapalapa, CP 9340, Ado. P. 55-535, Vicentina, Mexico City, Mexico;2. Laboratorio de Bioquímica-Genética y Unidad de Proteómica, Instituto Nacional de Pediatría, Secretaria de Salud Mexico City, Mexico;1. Enzymology Laboratory, University of Brasília, Campus Universitário Darcy Ribeiro, Brasília, DF, 70910-900, Brazil;2. Laboratory of Chemistry, Cellulose and Energy, Department of Forest Sciences, ESALQ, University of São Paulo, Piracicaba, SP, 13418-220, Brazil;3. Molecular Biophysics Laboratory, University of Brasília, Campus Universitário Darcy Ribeiro, Brasília, DF, 70910-900, Brazil |
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| Abstract: | The use of enzymes in aqueous solutions of ionic liquids (ILs) could be useful for the enzymatic treatment of lignocellulose. Hydrophilic ILs that dissolve lignocellulose are harmful to enzymes. The toleration limits and enzyme-friendly superbase IL combinations were investigated for the hyperthermophilic Thermopolyspora flexuosa GH10 xylanase (endo-1,4-β-xylanase EC 3.2.1.8) TfXYN10A and Dictyoglomus thermophilum GH11 xylanase DtXYN11B. TfXYN10A was more tolerant than DtXYN11B to acetate or propionate-based ILs. However, when the anion of the ILs was bigger (guaiacolate), GH11 xylanase showed higher tolerance to ILs. 1-Ethyl-3-methylimidazolium acetate ([EMIM]OAc), followed by 1,1,3,3-tetramethylguanidine acetate ([TMGH]OAc), were the most enzyme-friendly ILs for TfXYN10A and [TMGH]+-based ILs were tolerated best by DtXYN11B. Double-ring cations and a large size anion were associated with the strongest enzyme inhibition. Competitive inhibition appears to be a general factor in the reduction of enzyme activity. However, with guaiacolate ILs, the denaturation of proteins may also contribute to the reduction in enzyme activity. Molecular docking with IL cations and anions indicated that the binding mode and shape of the active site affect competitive inhibition, and the co-binding of cations and anions to separate active site positions caused the strongest enzyme inhibition. |
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| Keywords: | Biocatalysis GH10 xylanase GH11 xylanase Enzyme kinetics Enzyme inhibition Ionic liquid |
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