Enhanced activity of hyperthermostable Pyrococcus horikoshii endoglucanase in superbase ionic liquids
Uloženo v:
| Název: | Enhanced activity of hyperthermostable Pyrococcus horikoshii endoglucanase in superbase ionic liquids |
|---|---|
| Autoři: | Hakim Hebal, Joonas Hämäläinen, Laura Makkonen, Alistair W. T. King, Ilkka Kilpeläinen, Sandip Bankar, Nawel Boucherba, Ossi Turunen |
| Přispěvatelé: | Department of Chemistry, Synthesis and Analysis, Helsinki Institute of Sustainability Science (HELSUS), Doctoral Programme in Chemistry and Molecular Sciences, Department of Bioproducts and Biosystems, Bioprocess engineering, University of Béjaïa, St1 Biofuels Oy, Aalto University, University of Helsinki, University of Eastern Finland, Aalto-yliopisto |
| Zdroj: | Biotechnol Lett |
| Informace o vydavateli: | Springer Science and Business Media LLC, 2022. |
| Rok vydání: | 2022 |
| Témata: | 0301 basic medicine, INHIBITION, Ionic Liquids, IMPROVEMENT, PRETREATMENT, ENZYMATIC-HYDROLYSIS, Cellulase/metabolism, GH10 XYLANASE, 03 medical and health sciences, Cellulase, SACCHARIFICATION, DISSOLUTION, Biomass engineering, Cellulose/metabolism, Cations, Biomass, Cellulose, 0303 health sciences, STABILITY, Enzyme kinetics, Ionic liquids, Original Research Paper, Enzyme inhibition, Chemical sciences, Hyperthermostable endoglucanase, THERMOTOGA-MARITIMA, CELLULOSE, Pyrococcus horikoshii/metabolism, Pyrococcus horikoshii, Ionic Liquids/chemistry |
| Popis: | Objectives Ionic liquids (ILs) that dissolve biomass are harmful to the enzymes that degrade lignocellulose. Enzyme hyperthermostability promotes a tolerance to ILs. Therefore, the limits of hyperthemophilic Pyrococcus horikoschii endoglucanase (PhEG) to tolerate 11 superbase ILs were explored. Results PhEG was found to be most tolerant to 1-ethyl-3-methylimidazolium acetate ([EMIM]OAc) in soluble 1% carboxymethylcellulose (CMC) and insoluble 1% Avicel substrates. At 35% concentration, this IL caused an increase in enzyme activity (up to 1.5-fold) with CMC. Several ILs were more enzyme inhibiting with insoluble Avicel than with soluble CMC. Km increased greatly in the presence ILs, indicating significant competitive inhibition. Increased hydrophobicity of the IL cation or anion was associated with the strongest enzyme inhibition and activation. Surprisingly, PhEG activity was increased 2.0–2.5-fold by several ILs in 4% substrate. Cations exerted the main role in competitive inhibition of the enzyme as revealed by their greater binding energy to the active site. Conclusions These results reveal new ways to design a beneficial combination of ILs and enzymes for the hydrolysis of lignocellulose, and the strong potential of PhEG in industrial, high substrate concentrations in aqueous IL solutions. |
| Druh dokumentu: | Article Other literature type |
| Popis souboru: | application/pdf |
| Jazyk: | English |
| ISSN: | 1573-6776 0141-5492 |
| DOI: | 10.1007/s10529-022-03268-5 |
| Přístupová URL adresa: | https://pubmed.ncbi.nlm.nih.gov/35763164 https://cris.vtt.fi/en/publications/1e73266c-393e-4eba-a591-739448281c21 https://doi.org/10.1007/s10529-022-03268-5 http://hdl.handle.net/10138/346991 https://aaltodoc.aalto.fi/handle/123456789/119520 |
| Rights: | CC BY URL: http://creativecommons.org/licenses/by/4.0/Open AccessThis article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons licence, and indicate if changes were made. The images or other third party material in this article are included in the article's Creative Commons licence, unless indicated otherwise in a credit line to the material. If material is not included in the article's Creative Commons licence and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this licence, visit http://creativecommons.org/licenses/by/4.0/ (http://creativecommons.org/licenses/by/4.0/) . |
| Přístupové číslo: | edsair.doi.dedup.....c703eeaf2744ef8328676085599e31c7 |
| Databáze: | OpenAIRE |
Full Text Finder 
Nájsť tento článok vo Web of Science | Abstrakt: | Objectives Ionic liquids (ILs) that dissolve biomass are harmful to the enzymes that degrade lignocellulose. Enzyme hyperthermostability promotes a tolerance to ILs. Therefore, the limits of hyperthemophilic Pyrococcus horikoschii endoglucanase (PhEG) to tolerate 11 superbase ILs were explored. Results PhEG was found to be most tolerant to 1-ethyl-3-methylimidazolium acetate ([EMIM]OAc) in soluble 1% carboxymethylcellulose (CMC) and insoluble 1% Avicel substrates. At 35% concentration, this IL caused an increase in enzyme activity (up to 1.5-fold) with CMC. Several ILs were more enzyme inhibiting with insoluble Avicel than with soluble CMC. Km increased greatly in the presence ILs, indicating significant competitive inhibition. Increased hydrophobicity of the IL cation or anion was associated with the strongest enzyme inhibition and activation. Surprisingly, PhEG activity was increased 2.0–2.5-fold by several ILs in 4% substrate. Cations exerted the main role in competitive inhibition of the enzyme as revealed by their greater binding energy to the active site. Conclusions These results reveal new ways to design a beneficial combination of ILs and enzymes for the hydrolysis of lignocellulose, and the strong potential of PhEG in industrial, high substrate concentrations in aqueous IL solutions. |
|---|---|
| ISSN: | 15736776 01415492 |
| DOI: | 10.1007/s10529-022-03268-5 |