Inhibition of hyperthermostable xylanases by superbase ionic liquids

Hakim Hebal, Arno Parviainen, Sasikala Anbarasan, He Li, Laura Makkonen, Sandip Bankar, Alistair W.T. King, Ilkka Kilpeläinen, Said Benallaoua, Ossi Turunen

Research output: Contribution to journalArticleScientificpeer-review

10 Citations (Scopus)


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 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.

Original languageEnglish
Pages (from-to)148-156
Number of pages9
JournalProcess Biochemistry
Publication statusPublished - Aug 2020
MoE publication typeA1 Journal article-refereed


  • Biocatalysis
  • Enzyme inhibition
  • Enzyme kinetics
  • GH10 xylanase
  • GH11 xylanase
  • Ionic liquid


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