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

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Details

Original languageEnglish
Pages (from-to)515–524
Number of pages10
JournalExtremophiles
Volume20
Issue number4
Early online date30 May 2016
Publication statusPublished - Jul 2016
MoE publication typeA1 Journal article-refereed

Researchers

Research units

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

Abstract

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.

    Research areas

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

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