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

doi:10.1016/j.procbio.2020.03.022

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^*

^*Corresponding author for this work

Not published at VTT

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

11 Citations (Scopus)

Abstract

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 3.2.1.8) 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 language	English
Pages (from-to)	148-156
Number of pages	9
Journal	Process Biochemistry
Volume	95
DOIs	https://doi.org/10.1016/j.procbio.2020.03.022
Publication status	Published - Aug 2020
MoE publication type	A1 Journal article-refereed

Keywords

Biocatalysis
Enzyme inhibition
Enzyme kinetics
GH10 xylanase
GH11 xylanase
Ionic liquid

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10.1016/j.procbio.2020.03.022

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@article{19f093dc24d943ff9bcf41e6d75c9454,

title = "Inhibition of hyperthermostable xylanases by superbase ionic liquids",

abstract = "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 3.2.1.8) 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.",

keywords = "Biocatalysis, Enzyme inhibition, Enzyme kinetics, GH10 xylanase, GH11 xylanase, Ionic liquid",

author = "Hakim Hebal and Arno Parviainen and Sasikala Anbarasan and He Li and Laura Makkonen and Sandip Bankar and King, {Alistair W.T.} and Ilkka Kilpel{\"a}inen and Said Benallaoua and Ossi Turunen",

note = "Funding Information: We would like to thank Johanna Aura for her technical assistance. We would also like to thank CLIC Innovation (ACel programme) and Business Finland for their support. Publisher Copyright: {\textcopyright} 2020 Elsevier Ltd",

year = "2020",

month = aug,

doi = "10.1016/j.procbio.2020.03.022",

language = "English",

volume = "95",

pages = "148--156",

journal = "Process Biochemistry",

issn = "1359-5113",

publisher = "Elsevier",

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TY - JOUR

T1 - Inhibition of hyperthermostable xylanases by superbase ionic liquids

AU - Hebal, Hakim

AU - Parviainen, Arno

AU - Anbarasan, Sasikala

AU - Li, He

AU - Makkonen, Laura

AU - Bankar, Sandip

AU - King, Alistair W.T.

AU - Kilpeläinen, Ilkka

AU - Benallaoua, Said

AU - Turunen, Ossi

N1 - Funding Information: We would like to thank Johanna Aura for her technical assistance. We would also like to thank CLIC Innovation (ACel programme) and Business Finland for their support. Publisher Copyright: © 2020 Elsevier Ltd

PY - 2020/8

Y1 - 2020/8

N2 - 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 3.2.1.8) 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.

AB - 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 3.2.1.8) 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.

KW - Biocatalysis

KW - Enzyme inhibition

KW - Enzyme kinetics

KW - GH10 xylanase

KW - GH11 xylanase

KW - Ionic liquid

UR - http://www.scopus.com/inward/record.url?scp=85085655135&partnerID=8YFLogxK

U2 - 10.1016/j.procbio.2020.03.022

DO - 10.1016/j.procbio.2020.03.022

M3 - Article

AN - SCOPUS:85085655135

SN - 1359-5113

VL - 95

SP - 148

EP - 156

JO - Process Biochemistry

JF - Process Biochemistry

ER -

Inhibition of hyperthermostable xylanases by superbase ionic liquids

Abstract

Keywords

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