Insight into impact of choline-based ionic liquids on bovine β-lactoglobulin structural analysis: Unexpected high thermal stability of protein

Sindhu, Anamika; Mogha, Navin Kumar; Venkatesu, Pannuru

doi:10.1016/j.ijbiomac.2018.12.166

Cited by 28 publications

(19 citation statements)

References 54 publications

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“…Moreover, Figures S5 and S6 confirms the thermal stability study of Lyz from the above data using thermodynamic parameters like the free energy of unfolding (Δ u G ) as a function of temperature, molar enthalpy change of unfolding (Δ u H , Table S7), molar heat capacity of unfolding (Δ u Cp, Table S8), and molar entropy of unfolding (Δ u S , Table S9) at denaturing temperature. The Δ H value for each sample has been furnished by the area under the excess heat capacity curve of nano-DSC . Δ u G and Δ u S have been calculated in the same manner as performed previously for thermal stability of serum albumins by our group using the Gibbs–Helmholtz equation .…”

Section: Resultsmentioning

confidence: 99%

“…The ΔH value for each sample has been furnished by the area under the excess heat capacity curve of nano-DSC. 51 Δ u G and Δ u S have been calculated in the same manner as performed previously for thermal stability of serum albumins by our group 52 using the Gibbs−Helmholtz equation. 53 From Figure S5, the shape of the ΔG curve can be observed for denaturing of Lyz in the presence of various AuNPs (naked and IL-modified AuNPs) against an increase in temperature.…”

Section: ■ Results and Discussionmentioning

confidence: 99%

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Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Kumar

Sindhu

Venkatesu

2021

ACS Appl. Nano Mater.

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The synthesis of nanoparticles using ionic liquids (ILs) has attracted intensive research; however, synthesis and surface tailoring of gold nanoparticles (AuNPs) using ILs for enzyme immobilization have not yet been reported. Herein, we synthesized the various IL-modified AuNPs using different ILs, which are having common cation 1-ethyl-3-methyl-imidazolium (EMIM) and variable anions [BF 4−1 (AuNP-IL1), (CH 3 OSO 3 ) −1 (AuNP-IL2), (CH 3 CH 2 OSO 3 ) −1 (AuNP-IL3), and Cl −1 (AuNP-IL4)] by reduction of gold salt. The formation of IL modified AuNPs has been confirmed using UV−vis, zeta-potential, FTIR, and transmission electron microscopy (TEM). Thereafter, the centrifuged IL-modified AuNPs are being immobilized with a lysozyme (Lyz) enzyme to evaluate the effect of different AuNP covering groups (capping agent and IL's anions) for Lyz microbial activity, thermal and structural stabilities through interaction studies, spectroscopic techniques, and morphology investigation by TEM. AuNP-IL1 has increased the microbial activity of Lyz up to 2.6 fold at the concentration of 4 nM, and AuNP-IL2 is highly efficient to dextrously preserve enzyme activity against packaging for 4 weeks. The higher Michaelis−Menten constant (K M ) has been observed for Lyz immobilized in the AuNP-IL2 due to higher binding with the AuNP-IL2. Apparently, the higher specific constant (K cat /K M ) of immobilized Lyz has been observed in the case of AuNP-IL3 and shows more specific binding of Lyz with this particular IL-mediated AuNPs. The significant thermal stability enhancement about 8.11 °C is observed for transition temperature (T m ) of Lyz in the presence of sulfur group-containing IL-modified AuNPs like AuNP-IL2 and AuNP-IL3, which depends on the specific interacting ability of these AuNPs with Lyz. Therefore, the study reveals the variant character of sulfur-containing IL-modified AuNPs for higher activity and thermal and structural stability of Lyz. Surprisingly, this has created a way to monitor sulfur and hydrophobic interactions on AuNPs for enzyme immobilization through means of controlling surface modifications and interactions.

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Section: Resultsmentioning

confidence: 99%

Section: ■ Results and Discussionmentioning

confidence: 99%

Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Kumar

Sindhu

Venkatesu

2021

ACS Appl. Nano Mater.

Self Cite

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“…The native conformation of a protein depends on the intramolecular interactions between the functional groups and the intermolecular interactions between solvents and protein functional groups. Besides the temperature, there are also other factors that contribute to changes in protein conformation that may lead to denaturation, namely the addition of polymers, organic solvents, changes in pH or pressure, or the addition of other co-solvents or molecules [6,7]. lead to denaturation, namely the addition of polymers, organic solvents, changes in pH or pressure, or the addition of other co-solvents or molecules [6,7].…”

Section: Introductionmentioning

confidence: 99%

“…Besides the temperature, there are also other factors that contribute to changes in protein conformation that may lead to denaturation, namely the addition of polymers, organic solvents, changes in pH or pressure, or the addition of other co-solvents or molecules [6,7]. lead to denaturation, namely the addition of polymers, organic solvents, changes in pH or pressure, or the addition of other co-solvents or molecules [6,7]. In terms of dosage form assessment, liquid formulations are more convenient for the end user, since there is no need for product reconstitution and errors of volume added for its reconstitution [8].…”

Section: Introductionmentioning

confidence: 99%

An Overview on the Recent Advances in Alternative Solvents as Stabilizers of Proteins and Enzymes

et al. 2022

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Currently, the use of alternative solvents is increasing, namely ionic liquids (ILs) and deep eutectic solvents (DESs) in diverse fields of knowledge, such as biochemistry, chemistry, chemical engineering, biotechnology and biomedicine. Particularly, when compared to traditional solvents, these alternative solvents have great importance for biomolecules due to the enhanced solubility, structure stability and the biological activity of biomolecules, such as protein and enzymes. Thus, in this review article, the recent developments and efforts on the technological developments carried out with ILs and DESs for the stabilization and activation of proteins and enzymes are provided. The most studied IL- and DES-based formulations for proteins and enzymes are discussed and the molecular mechanisms and interactions related to the increased stability promoted by these alternative solvents are disclosed, while emphasizing their main advantages.

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“…Numerous studies have demonstrated that the performance of important biomolecules such as proteins and enzymes can be substantially improved by using ILs. Several studies revealed that the functionality of these biomolecules can be improved in the presence of ILs [31][32][33][34][35][36][37][38][39]. Relevant works have been published demonstrating that proper ILs improve the activity and stability of various proteins or enzymes, comprising lysozyme (lyz), laccase, alcohol dehydrogenases, and cytochrome c (cyt-c), among others [17].…”

Section: Introductionmentioning

confidence: 99%

Advances Achieved by Ionic-Liquid-Based Materials as Alternative Supports and Purification Platforms for Proteins and Enzymes

et al. 2021

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Ionic liquids (ILs) have been applied in several fields in which enzymes and proteins play a noteworthy role, for instance in biorefinery, biotechnology, and pharmaceutical sciences, among others. Despite their use as solvents and co-solvents, their combination with materials for protein- and enzyme-based applications has raised significant attention in the past few years. Among them, significant advances were brought by supported ionic liquids (SILs), in which ILs are introduced to modify the surface and properties of materials, e.g., as ligands when covalently bond or when physiosorbed. SILs have been mainly investigated as alternative supports for enzymes in biocatalysis and as new supports in preparative liquid chromatography for the purification of high-value proteins and enzymes. In this manuscript, we provide an overview on the most relevant advances by using SILs as supports for enzymes and as purification platforms for a variety of proteins and enzymes. The interaction mechanisms occurring between proteins and SILs/ILs are highlighted, allowing the design of efficient processes involving SILs. The work developed is discussed in light of the respective development phase and innovation level of the applied technologies. Advantages and disadvantages are identified, as well as the missing links to pave their use in relevant applications.

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Insight into impact of choline-based ionic liquids on bovine β-lactoglobulin structural analysis: Unexpected high thermal stability of protein

Cited by 28 publications

References 54 publications

Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

Ionic Liquid-Modified Gold Nanoparticles for Enhancing Antimicrobial Activity and Thermal Stability of Enzymes

An Overview on the Recent Advances in Alternative Solvents as Stabilizers of Proteins and Enzymes

Advances Achieved by Ionic-Liquid-Based Materials as Alternative Supports and Purification Platforms for Proteins and Enzymes

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