Effect of ionic liquids on the structure, stability and activity of two related α-amylases

Dabirmanesh, Bahareh; Daneshjou, Sara; Sepahi, Abbas Akhavan; Ranjbar, Bijan; Khavari-Nejad, Ramazan Ali; Gill, Pooria; Heydari, Akbar; Khajeh, Khosro

doi:10.1016/j.ijbiomac.2010.10.001

Cited by 63 publications

(25 citation statements)

References 28 publications

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“…MD simulations of 100 ns declare that as the water content increases, conformational stability of α-amylase enhances. This conclusion is in agreement with experimental observations that had previously reported the exceptional behavior of [HMIm][Cl] in reducing α-amylase stability [11]. In accordance to the RMSD and ILprotein distance data, higher stability of the enzyme at higher percentages of water regresses back to the fact that water molecules provide a dynamic barrier to enzyme accessibility by the IL.…”

Section: Resultssupporting

confidence: 92%

Conformation changes and diffusion of α-amylase in 1-hexyle-3-methylimidazolium chloride ionic liquid: A molecular dynamics simulation perspective

Mohammadyazdani

Bozorgmehr

Momen-Heravi

2016

Journal of Molecular Liquids

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Section: Resultssupporting

confidence: 92%

Conformation changes and diffusion of α-amylase in 1-hexyle-3-methylimidazolium chloride ionic liquid: A molecular dynamics simulation perspective

Mohammadyazdani

Bozorgmehr

Momen-Heravi

2016

Journal of Molecular Liquids

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“…The shift values for T m and a trend for the dependence of T m on the [ch][dhp] content are very similar to ours, having the distinct slope break at 0.5 mol/L (see Figure 2 of [ 11 ]). However, as can be judged based on the incomplete Figure 1 of [ 14 ], the increase in T m was accompanied by the substantial increase in Δ H cal . Unfortunately, the whole trend for Δ H cal (and, even more so, for Δ S m ) is not reported in [ 11 ].…”

Section: Resultsmentioning

confidence: 99%

Notable Stabilization of α-Chymotrypsin by the Protic Ionic Additive, [ch][dhp]: Calorimetric Evidence for a Fine Enthalpy/Entropy Balance

Uchaneishvili¹,

Makharadze²,

Shushanyan

et al. 2014

International Scholarly Research Notices

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An impact of 0.5 to 3 M choline dihydrogen phosphate, [ch][dhp], the biotechnologically relevant ionic substance, on the thermal stability of a model globular protein, α-chymotrypsin (α-CT), has been studied exploiting the highly sensitive differential scanning calorimetry (DSC) technique. The notable overall stabilizing effect of 11 ± 2 K regarding the thermal transition (melting) temperature, T m, has been detected. For this kind of series, for the first time, the calorimetric melting enthalpy (ΔH cal) and transition entropy (ΔS m) parameters have been determined simultaneously throughout. The first analysis indicated a two-phase impact implying (a) the initial, dramatic drop in both ΔH cal and ΔS m, obviously connected to specific, direct interaction between the [ch][dhp] components and α-CT's charged groups (within 0 to 1 mol/L [ch][dhp]), leading to the essential rearrangement of the interfacial hydrogen-bonded (HB) network; and (b) the follow-up (within 1 to 3.0 mol/L [ch][dhp]), modest changes in ΔH cal and lack of changes in ΔS m, seemingly connected with a subsequent steady strengthening of already reformed HB network, respectively. These changes, presumably, are primarily facilitated by Coulombic interactions between the [dhp] anions and solvent-exposed positively charged amino groups of α-CT.

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“…In addition, Khajeh et al. report had noted that ILs can have an anti‐aggregation role on protein structure during thermal unfolding …”

Section: Figurementioning

confidence: 99%

Ionic Liquid-Based Periodic Mesoporous Organosilica: An Innovative Matrix for Enzyme Immobilization

2017

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Employment of enzyme immobilization technique for α‐amylase, provides useful approaches to improve enzyme resistance to harsh conditions and reusability. Two silica supports, Ionic Liquid‐Based Periodic Mesoporous Organosilica which we call it PMO‐IL, and SBA‐15, have been used for immobilization of α‐amylase. We found that proper electrostatic interactions result in a higher immobilization yield of PMO‐IL rather than SBA‐15. The kinetics parameters show that α‐amylase@PMO‐IL activity has slightly decreased in comparison to free enzyme and the stability studies indicate that it is even more active than free enzyme in the natural pH which shows the improving role of ionic liquid on enzyme structure and function. Also, both immobilized enzymes have 2 times more stability at 70 °C and 80 °C after 60 min in comparison to free enzyme. Finally, the recovery efficiency of α‐amylase@PMO‐IL is 88% of its initial activity after 4 cycles which is 23% more than a previous report.

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Effect of ionic liquids on the structure, stability and activity of two related α-amylases

Cited by 63 publications

References 28 publications

Conformation changes and diffusion of α-amylase in 1-hexyle-3-methylimidazolium chloride ionic liquid: A molecular dynamics simulation perspective

Conformation changes and diffusion of α-amylase in 1-hexyle-3-methylimidazolium chloride ionic liquid: A molecular dynamics simulation perspective

Notable Stabilization of α-Chymotrypsin by the Protic Ionic Additive, [ch][dhp]: Calorimetric Evidence for a Fine Enthalpy/Entropy Balance

Ionic Liquid-Based Periodic Mesoporous Organosilica: An Innovative Matrix for Enzyme Immobilization

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