Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

Research output: Contribution to journalArticleScientificpeer-review


  • Tianyi Yu
  • Sasikala Anbarasan
  • Yawei Wang
  • Kübra Telli
  • Aşkın Sevinç Aslan
  • Zhengding Su
  • Yin Zhou
  • Li Zhang
  • Piia Iivonen
  • Sami Havukainen
  • Tero Mentunen
  • Michael Hummel

  • Herbert Sixta

  • Baris Binay
  • Ossi Turunen
  • Hairong Xiong

Research units

  • South-Central University for Nationalities
  • Hubei University
  • Wuhan Sunhy Biology Co., Ltd
  • Gebze Technical University


The gene of Thermotoga maritima GH10 xylanase (TmXYN10B) was synthesised to study the extreme limits of this hyperthermostable enzyme at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids (ILs). TmXYN10B expressed from Pichia pastoris showed maximal activity at 100 °C and retained 92 % of maximal activity at 105 °C in a 30-min assay. Although the temperature optimum of activity was lowered by 1-ethyl-3-methylimidazolium acetate ([EMIM]OAc), TmXYN10B retained partial activity in 15–35 % hydrophilic ILs, even at 75–90 °C. TmXYN10B retained over 80 % of its activity at 90 °C in 15 % [EMIM]OAc and 15–25 % 1-ethyl-3-methylimidazolium dimethylphosphate ([EMIM]DMP) during 22-h reactions. [EMIM]OAc may rigidify the enzyme and lower Vmax. However, only minor changes in kinetic parameter Km showed that competitive inhibition by [EMIM]OAc of TmXYN10B is minimal. In conclusion, when extended enzymatic reactions under extreme conditions are required, TmXYN10B shows extraordinary potential.


Original languageEnglish
Pages (from-to)515–524
Number of pages10
Issue number4
Early online date30 May 2016
Publication statusPublished - Jul 2016
MoE publication typeA1 Journal article-refereed

    Research areas

  • Competitive inhibition, Expression in Pichia pastoris, Extreme stability, GH10 xylanase, Ionic liquids, Thermotoga maritima

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