The effect of ionic liquid on the structure of active site pocket and catalytic activity of a β-glucosidase from Halothermothrix orenii

Konar, Sukanya; Sinha, Sushant K.; Datta, Supratim; Ghorai, Pradip Kr.

doi:10.1016/j.molliq.2020.112879

Cited by 23 publications

(15 citation statements)

References 42 publications

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“…Also, other studies support the implication of the IL viscosity effect of higher IL concentrations in the reduction of enzyme activity based on the effect on mass transfer (Zhao et al 2009;Engel et al 2010;Lai et al 2011). Konar et al (2020) found that the self-diffusion coefficient (D) of the substrate p-nitrophenyl-b-D-glucopyranoside (pNPGlc) in ILs was nearly half compared to its diffusion coefficient in glucose solution. Therefore, the number of substrate molecules in the active site tunnel is significantly higher in 2 M glucose than in 40% [EMIM]Cl.…”

Section: Properties Of Il Moleculesmentioning

confidence: 88%

“…However, the anion also has a role, especially when the size is higher. Anions were observed to contribute to the competitive inhibition of a hyperthermostable GH1 b-glucosidase B8CYA8 (Konar et al 2020) and a hyperthermostable GH10 xylanase TfXYN10A (Hebal et al 2020). Increasing hydrophobicity of cation and anion leads to higher competitive inhibition of hyperthermostable xylanases (Hebal et al 2020).…”

Section: Properties Of Il Moleculesmentioning

confidence: 99%

“…Since the IL cation typically has a significant hydrophobic part and both cation and anion can form hydrogen bonds, the ILs could by binding to various parts of the protein, in principle, affect the structural mobility, which in turn affects the protein functioning. On the other hand, opposite local effects can be observed; the activity decrease of GH1 b-glucosidase B8CYA8 in the presence of increasing concentrations of 1-ethyl-3methylimidazolium chloride ([EMIM]Cl) (40 and 70%) was concluded to happen by the localized increase in fluctuations of active site pocket residues, which affects the reaction rate (Konar et al 2020).…”

Section: Effect Of Ils On Enzyme Activitymentioning

confidence: 99%

“…Some insight into details on how ILs perturb the activity of hyperthermostable cellulases and xylanases have come from molecular dynamic (MD) simulations and molecular docking. Most of these studies were done with imidazolium ILs (Chawachart et al 2014;Johnson and Snow 2017;Summers et al 2017;Manna and Ghosh 2020;Konar et al 2020), but other docking studies included superbase ILs (Hebal et al 2020). The charge of the active site seems to contribute to the extent of competitive inhibition by the IL ions.…”

Section: Enzyme-related Factors In Il Effectmentioning

confidence: 99%

“…Inhibition of GH1 b-glucosidase B8CYA8 in the presence of a high concentration of [EMIM]Cl (40 and 70%) was attributed to an increase in accumulation of both [EMIM] þ and [Cl] À at the active site entrance and in the active site tunnel. This accumulation would hinder substrate accessibility to the active site (Konar et al 2020).…”

Section: Properties Of Il Moleculesmentioning

confidence: 99%

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Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Hebal

Boucherba

Bi̇nay

et al. 2021

Biocatalysis and Biotransformation

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The biochemical conversion route in the utilization of biomass has required intensive development of processing methods for reducing recalcitrance of cellulose to enzymatic hydrolysis. Since discovering hydrophilic ionic liquids (ILs) are efficient lignocellulose solvents, considerable efforts have been made to demonstrate their potential applications in cellulose hydrolysis. However, most of the commercial lignocellulose hydrolyzing enzymes are largely deactivated or inhibited in the presence of even low concentrations of ILs. The link found between enzyme thermostability and IL tolerance leads to the consideration that hyperthermostable enzymes are good candidates to be used together with ILs. Hyperthermostable cellulases and xylanases that are highly tolerant to aqueous solutions of ILs show resistance to competitive inhibition by IL cations and have lower amounts of structural motifs (loop and helix structures) that are prone to denaturation by IL anions. In addition, they have a net negative protein surface charge that contributes to repulsion of anions. This review provides recent developments in understanding the behaviour of hyperthermostable cellulases and xylanases in ILs by elucidating protein-IL interactions. It also outlines the current research demonstrating the potential of rational enzyme engineering to improve enzyme tolerance to ILs based on comprehension of IL-induced deactivation mechanisms.

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Section: Properties Of Il Moleculesmentioning

confidence: 88%

Section: Properties Of Il Moleculesmentioning

confidence: 99%

Section: Effect Of Ils On Enzyme Activitymentioning

confidence: 99%

Section: Enzyme-related Factors In Il Effectmentioning

confidence: 99%

Section: Properties Of Il Moleculesmentioning

confidence: 99%

See 3 more Smart Citations

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Hebal

Boucherba

Bi̇nay

et al. 2021

Biocatalysis and Biotransformation

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Biophysical and structural characterization of tetramethrin serum protein complex and its toxicological implications

Singh,

Gopi,

Rani

et al. 2024

J of Molecular Recognition

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Tetramethrin (TMT) is a commonly used insecticide and has a carcinogenic and neurodegenerative effect on humans. The binding mechanism and toxicological implications of TMT to human serum albumin (HSA) were examined in this study employing a combination of biophysical and computational methods indicating moderate binding affinity and potential hepato and renal toxicity. Fluorescence quenching experiments showed that TMT binds to HSA with a moderate affinity, and the binding process was spontaneous and predominantly enthalpy‐driven. Circular dichroism spectroscopy revealed that TMT binding did not induce any significant conformational changes in HSA, resulting in no changes in its alpha‐helix content. The binding site and modalities of TMT interactions with HSA as computed by molecular docking and molecular dynamics simulations revealed that it binds to Sudlow site II of HSA via hydrophobic interactions through its dimethylcyclopropane carboxylate methyl propanyl group. The structural dynamics of TMT induce proper fit into the binding site creating increased and stabilizing interactions. Additionally, molecular mechanics–Poisson Boltzmann surface area calculations also indicated that non‐polar and van der Waals were found to be the major contributors to the high binding free energy of the complex. Quantum mechanics (QM) revealed the conformational energies of the binding confirmation and the degree of deviation from the global minimum energy conformation of TMT. The results of this study provide a comprehensive understanding of the binding mechanism of TMT with HSA, which is important for evaluating the toxicity of this insecticide in humans.

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Inactivation and process intensification of β-glucosidase in biomass utilization

Meng

et al. 2023

Appl Microbiol Biotechnol

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The effect of ionic liquid on the structure of active site pocket and catalytic activity of a β-glucosidase from Halothermothrix orenii

Cited by 23 publications

References 42 publications

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Activity and stability of hyperthermostable cellulases and xylanases in ionic liquids

Biophysical and structural characterization of tetramethrin serum protein complex and its toxicological implications

Inactivation and process intensification of β-glucosidase in biomass utilization

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