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Hinckley, Glen T.; Mozhaev, Vadim V.; Budde, Cheryl; Khmelnitsky, Yuri L.

doi:10.1023/a:1021305229969

Cited by 119 publications

(48 citation statements)

References 13 publications

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“…However, the effect of IL-induced denaturation on the enzyme appears to be a major factor resulting in lowered activity compared to that of laccase in aqueous solutions. 23 The IL [C 4 mim]Cl has been shown to have a significant denaturing effect on some enzymes, even in aqueous solution, due in part to the intrinsically high Cl -ion concentration and activity in the reaction media. 24 Interactions between Clions and charged amino acid residues on the exterior of some proteins can threaten the integrity of the secondary structure and, thus, the activity of the enzyme.…”

Section: Resultsmentioning

confidence: 99%

Production of Bioactive Cellulose Films Reconstituted from Ionic Liquids

et al. 2004

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A new method for introducing enzymes into cellulosic matrixes which can be formed into membranes, films, or beads has been developed using a cellulose-in-ionic-liquid dissolution and regeneration process. Initial results on the formation of thin cellulose films incorporating dispersed laccase indicate that active enzyme-encapsulated films can be prepared using this methodology and that precoating the enzyme with a second, hydrophobic ionic liquid prior to dispersion in the cellulose/ionic liquid solution can provide an increase in enzyme activity relative to that of untreated films, presumably by providing a stabilizing microenvironment for the enzyme.

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Section: Resultsmentioning

confidence: 99%

Production of Bioactive Cellulose Films Reconstituted from Ionic Liquids

et al. 2004

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“…Examples include a-chymotrypsin-catalyzed aminoacid ester transesterification [5][6][7]; enantioselective lipase-catalyzed esterification, transesterification, perhydrolysis, and aminolysis reactions [8]; b-galactosidase-catalyzed galactosylation [9,10]; thermolysin-catalyzed aspartame synthesis [11]; and peroxidase-catalyzed phenolic oxidation [12,13]. This diverse repertoire of enzymatic reactions demonstrates the potential value of RTILs as novel media for enzymatic reactions.…”

Section: Introductionmentioning

confidence: 99%

Enzyme–Carbon Nanotube Conjugates in Room-temperature Ionic Liquids

Eker

Asuri

Murugesan

et al. 2007

Appl Biochem Biotechnol

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Room-temperature ionic liquids (RTILs) are intriguing solvents, which are recognized as "green" alternatives to volatile organics. Although RTILs are nonvolatile and can dissolve a wide range of charged, polar, and nonpolar organic and inorganic molecules, there remain substantial challenges in their use, not the least of which is the solvents' high viscosity that leads to potential mass transfer limitations. In the course of this work, we discovered that the simple adsorption of the bacterial protease, proteinase K, onto singlewalled carbon nanotubes (SWNTs) results in intrinsically high catalytic turnover. The high surface area and the nanoscopic dimensions of SWNTs offered high enzyme loading and low mass transfer resistance. Furthermore, the enzyme-SWNT conjugates displayed enhanced thermal stability in RTILs over the native suspended enzyme counterpart and allowed facile reuse. These enzyme-SWNT conjugates may therefore provide a way to overcome key operational limitations of RTIL systems.

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“…Since the pioneering studies by some groups [8][9][10], many biocatalytic reactions in ILs have been actively conducted with lipases [11][12][13][14], proteases [15,16], oxidoreductases [17,18], and even with a whole-cell biocatalyst [19]. When compared to reactions performed in conventional organic solvents, ILs provide a more suitable environment for enzymes [16,20] and are obviously less harmful to cell membranes [19], resulting in high catalytic performance.…”

Section: Introductionmentioning

confidence: 99%

Activation of lipase in ionic liquids by modification with comb-shaped poly(ethylene glycol)

Nakashima

Okada

Maruyama

et al. 2006

Science and Technology of Advanced Materials

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Outstanding activation of an enzyme in ionic liquids (ILs) has been demonstrated by covalent modification with comb-shaped poly(ethylene glycol) (PEG) (PM 13 N]) containing 0.5% (v/v) of water, whereas native lipase did not dissolve in any of the ILs. The results for transesterification of 2-phenyl-1-propanol with vinyl acetate using lipase in ILs revealed that the PM 13 -CRL conjugate exhibits a high catalytic activity while suspended native lipase shows little activity. The hydrophobicity of ILs somewhat affected the enzyme activity and a more hydrophobic IL such as [Emim][Tf 2 N] was preferable for the lipase reaction, as was also observed in enzymatic reaction in conventional organic solvents. The enzyme activities in ILs were much higher than those in organic solvents, the excellent activity being associated with unique properties such as the hydrophobicity and the high polarity of ILs. Furthermore, the PM 13 --CRL conjugate exhibited a high storage stability in [Emim][Tf 2 N]. r

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Untitled

Cited by 119 publications

References 13 publications

Production of Bioactive Cellulose Films Reconstituted from Ionic Liquids

Production of Bioactive Cellulose Films Reconstituted from Ionic Liquids

Enzyme–Carbon Nanotube Conjugates in Room-temperature Ionic Liquids

Activation of lipase in ionic liquids by modification with comb-shaped poly(ethylene glycol)

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