Hyperthermostable <Emphasis Type="Italic">Thermotoga maritima</Emphasis> xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids |
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| Authors: | Tianyi Yu Sasikala Anbarasan Yawei Wang Kübra Telli A?k?n Sevinç Aslan Zhengding Su Yin Zhou Li Zhang Piia Iivonen Sami Havukainen Tero Mentunen Michael Hummel Herbert Sixta Baris Binay Ossi Turunen Hairong Xiong |
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| Institution: | 1.South-Central University for Nationalities, College of Life Science,Wuhan,China;2.Department of Biotechnology and Chemical Technology,School of Chemical Technology, Aalto University,Aalto,Finland;3.Hubei University of Technology,Wuhan,China;4.Wuhan Sunhy Biology Co., Ltd,Wuhan,China;5.Department of Forest Products Technology,School of Chemical Technology, Aalto University,Aalto,Finland;6.Department of Bioengineering,Gebze Technical University,Gebze Kocaeli,Turkey |
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| 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 V max. However, only minor changes in kinetic parameter K m 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. |
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