Choline acetate enhanced the catalytic performance of Candida rogusa lipase in AOT reverse micelles

Xue, Luyan; Zhao, Yin; Yu, Li; Sun, Yanwen; Yan, Keqian; Liu, Ying; Huang, Xirong; Qu, Yinbo

doi:10.1016/j.colsurfb.2012.12.050

Cited by 32 publications

(15 citation statements)

References 36 publications

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“…Choline acetate is an IL consisting of a kosmotropic anion and a chaotropic cation. The Huang group found that at low concentrations (up to 5 mmol L −1 ), choline acetate could improve the hydrolytic activity of Candida rogusa lipase in AOT/water/isooctane reverse micelles (Fig. ), and cause no lipase conformational changes as evidenced by fluorescence spectra.…”

Section: Specific Ion Effect Of Ils On Protein Structures and Enzyme mentioning

confidence: 99%

Protein stabilization and enzyme activation in ionic liquids: specific ion effects

Zhao

2015

J of Chemical Tech & Biotech

251

192

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There are still debates on whether the hydration of ions perturbs the water structure, and what is the degree of such disturbance; therefore, the origin of Hofmeister effect on protein stabilization continues being questioned. For this reason, it is suggested to use the ‘specific ion effect’ instead of other misleading terms such as Hofmeister effect, Hofmeister series, lyotropic effect, and lyotropic series. In this review, we firstly discuss the controversial aspect of inorganic ion effects on water structures, and several possible contributors to the specific ion effect of protein stability. Due to recent overwhelming attraction of ionic liquids (ILs) as benign solvents in many enzymatic reactions, we further evaluate the structural properties and molecular-level interactions in neat ILs and their aqueous solutions. Next, we systematically compare the specific ion effects of ILs on enzyme stability and activity, and conclude that (a) the specificity of many enzymatic systems in diluted aqueous IL solutions is roughly in line with the traditional Hofmeister series albeit some exceptions; (b) however, the specificity follows a different track in concentrated or neat ILs because other factors (such as hydrogen-bond basicity, nucelophilicity, and hydrophobicity, etc) are playing leading roles. In addition, we demonstrate some examples of biocatalytic reactions in IL systems that are guided by the empirical specificity rule.

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Section: Specific Ion Effect Of Ils On Protein Structures and Enzyme mentioning

confidence: 99%

Protein stabilization and enzyme activation in ionic liquids: specific ion effects

Zhao

2015

J of Chemical Tech & Biotech

251

192

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“…Previously, it was shown that [Ch][Ac] activated Candida rugosa lipase in the hydrolysis of p ‐nitrophenyl butyrate ( p ‐NPB), and this effect was attributed to the changes in the lipase conformation and the increase in the nucleophilicity of the water . Although the substrate and the lipase strain are different, because of the similarity of the results using aqueous solutions of [Ch][Ac], it can be concluded that herein, the increase in the lipase activity was also a result of a modification of the conformation due to the presence of [Ch][Ac].…”

Section: Resultsmentioning

confidence: 88%

“…The [Ch][Ac] promoted an increase in the enzyme activity independent of the IL concentration compared to the control (enzyme solution without IL). Previously, Xue et al evaluated the effect of this IL on the activity of lipase from Candida rogusa and demonstrated that the oxygen atoms of the cholinium cation and the acetate anion can form hydrogen bonds with water molecules around the lipase, increasing the nucleophilicity of the water and, consequently, increases the catalytic efficiency of the enzyme. Furthermore, the authors also evaluated the individual activating effect of each ion, concluding that the cation has a stronger activation effect than the anion.…”

Section: Resultsmentioning

confidence: 99%

“…The interactions between the protein and the ions are determined by the ion size and the magnitude on the ion's surface charge . Several ILs, such as [Ch][Ac], are formed by a salting‐out anion and a salting‐in cation, and this combination can be a promising medium for the stabilization of proteins, in addition to enhancing the hydrolytic activity of lipase . Thus, to clarify the activity of lipase in [Ch] + ‐ILs aqueous solutions, it is necessary not only to understand the enzyme behavior but also to relate the effects to the characteristics of the corresponding ions.…”

Section: Resultsmentioning

confidence: 99%

“…51 Several ILs, such as [Ch][Ac], are formed by a salting-out anion and a salting-in cation, and this combination can be a promising medium for the stabilization of proteins, 52 in addition to enhancing the hydrolytic activity of lipase. 43 In general, the stabilization or destabilization of proteins in the presence of different ions is ranked according to the Hofmeister series, namely, the salting-out (high charge density) and salting-in (low charge density) aptitude of the ions. 45 The ion better suited to salt-out proteins tend to form hydration complexes away from the hydrophobic moieties of the proteins, while ions more suitable for salting-in favor the hydration of the protein surface.…”

Section: Lipase Stability In Aqueous Solutions Of [Ch] + -Ilsmentioning

confidence: 99%

See 2 more Smart Citations

Effects of cholinium‐based ionic liquids on Aspergillus niger lipase: Stabilizers or inhibitors

Nascimento

Picheli

Lopes

et al. 2019

Biotechnology Progress

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Lipases are well‐known biocatalysts used in several industrial processes/applications. Thus, as with other enzymes, changes in their surrounding environment and/or their thermodynamic parameters can induce structural changes that can increase, decrease, or even inhibit their catalytic activity. The use of ionic compounds as solvents or additives is a common approach for adjusting reaction conditions and, consequently, for controlling the biocatalytic activity of enzymes. Herein, to elucidate the effects of ionic compounds on the structure of lipase, the stability and enzymatic activity of lipase from Aspergillus niger in aqueous solutions (at 0.05, 0.10, 0.50, and 1.00 M) of six cholinium‐based ionic liquids (cholinium chloride [Ch]Cl; cholinium acetate ([Ch][Ac]); cholinium propanoate ([Ch][Prop]); cholinium butanoate ([Ch][But]); cholinium pentanoate ([Ch][Pent]); and cholinium hexanoate ([Ch][Hex])) were evaluated over 24 hr. The enzymatic activity of lipase was maintained or enhanced in the lower concentrations of all the [Ch]+‐ILs (below 0.1 M). [Ch][Ac] maintained the biocatalytic behavior of lipase, independent of the IL concentration and incubation time. However, above 0.1 M, [Ch][Pent] and [Ch][Hex] caused complete inhibition of the catalytic activity of the enzyme, demonstrating that the increase in the anionic alkyl chain length strongly affected the conformation of the lipase. The hydrophobicity and concentration of the [Ch]+‐ILs play an important role in the enzyme activity, and these parameters can be controlled by adjusting the anionic alkyl chain length. The inhibitory effects of [Ch][Pent] and [Ch][Hex] may be of great interest to the pharmaceutical industry to induce pharmacological inhibition of gastric and pancreatic lipases.

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Ionic Liquids in Soft Confinement

Falcone

Correa

Silber

et al. 2015

Ionic Liquid‐Based Surfactant Science

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Choline acetate enhanced the catalytic performance of Candida rogusa lipase in AOT reverse micelles

Cited by 32 publications

References 36 publications

Protein stabilization and enzyme activation in ionic liquids: specific ion effects

Protein stabilization and enzyme activation in ionic liquids: specific ion effects

Effects of cholinium‐based ionic liquids on Aspergillus niger lipase: Stabilizers or inhibitors

Ionic Liquids in Soft Confinement

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