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

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

doi:10.1007/s00792-016-0841-y

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

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^*

^*Corresponding author for this work

Department of Bioproducts and Biosystems

Research output: Contribution to journal › Article › Scientific › peer-review

25 Citations (Scopus)

250 Downloads (Pure)

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.

Original language	English
Pages (from-to)	515–524
Number of pages	10
Journal	Extremophiles
Volume	20
Issue number	4
Early online date	30 May 2016
DOIs	https://doi.org/10.1007/s00792-016-0841-y
Publication status	Published - Jul 2016
MoE publication type	A1 Journal article-refereed

Keywords

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

Access to Document

10.1007/s00792-016-0841-yLicence: CC BY

art%3A10.1007%2Fs00792-016-0841-yFinal published version, 1.04 MBLicence: CC BY

Cite this

Yu, T., Anbarasan, S., Wang, Y., Telli, K., Aslan, A. S., Su, Z., Zhou, Y., Zhang, L., Iivonen, P., Havukainen, S., Mentunen, T., Hummel, M., Sixta, H., Binay, B., Turunen, O., & Xiong, H. (2016). Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids. Extremophiles, 20(4), 515–524. https://doi.org/10.1007/s00792-016-0841-y

@article{fb54891ba6c34be082d791c26b77eb71,

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

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.",

keywords = "Competitive inhibition, Expression in Pichia pastoris, Extreme stability, GH10 xylanase, Ionic liquids, Thermotoga maritima",

author = "Tianyi Yu and Sasikala Anbarasan and Yawei Wang and K{\"u}bra Telli and Aslan, {A{\c s}kın Sevin{\c c}} and Zhengding Su and Yin Zhou and Li Zhang and Piia Iivonen and Sami Havukainen and Tero Mentunen and Michael Hummel and Herbert Sixta and Baris Binay and Ossi Turunen and Hairong Xiong",

year = "2016",

month = jul,

doi = "10.1007/s00792-016-0841-y",

language = "English",

volume = "20",

pages = "515–524",

journal = "Extremophiles",

issn = "1431-0651",

publisher = "Springer",

number = "4",

}

Yu, T, Anbarasan, S, Wang, Y, Telli, K, Aslan, AS, Su, Z, Zhou, Y, Zhang, L, Iivonen, P, Havukainen, S, Mentunen, T, Hummel, M , Sixta, H, Binay, B, Turunen, O & Xiong, H 2016, 'Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids', Extremophiles, vol. 20, no. 4, pp. 515–524. https://doi.org/10.1007/s00792-016-0841-y

TY - JOUR

T1 - Hyperthermostable Thermotoga maritima xylanase XYN10B shows high activity at high temperatures in the presence of biomass-dissolving hydrophilic ionic liquids

AU - Yu, Tianyi

AU - Anbarasan, Sasikala

AU - Wang, Yawei

AU - Telli, Kübra

AU - Aslan, Aşkın Sevinç

AU - Su, Zhengding

AU - Zhou, Yin

AU - Zhang, Li

AU - Iivonen, Piia

AU - Havukainen, Sami

AU - Mentunen, Tero

AU - Hummel, Michael

AU - Sixta, Herbert

AU - Binay, Baris

AU - Turunen, Ossi

AU - Xiong, Hairong

PY - 2016/7

Y1 - 2016/7

N2 - 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.

AB - 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.

KW - Competitive inhibition

KW - Expression in Pichia pastoris

KW - Extreme stability

KW - GH10 xylanase

KW - Ionic liquids

KW - Thermotoga maritima

UR - http://www.scopus.com/inward/record.url?scp=84973149468&partnerID=8YFLogxK

U2 - 10.1007/s00792-016-0841-y

DO - 10.1007/s00792-016-0841-y

M3 - Article

AN - SCOPUS:84973149468

SN - 1431-0651

VL - 20

SP - 515

EP - 524

JO - Extremophiles

JF - Extremophiles

IS - 4

ER -

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Bioeconomy Research Infrastructure

Cite this

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

Abstract

Keywords

Access to Document

Other files and links

Fingerprint

Equipment

Bioeconomy Research Infrastructure

Cite this