Enzyme Catalysed Synthesis in Ambient Temperature Ionic Liquids

Husum, Tommy Lykke; Jørgensen, Christel Thea; Christensen, Morten Würtz; Kirk, Ole

doi:10.3109/10242420109003648

Cited by 67 publications

(35 citation statements)

References 14 publications

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“…In this system, usually an aqueous working phase and an organic extractive phase are present. Nowadays, the role of ILs in biphasic reactions is to replace the organic solvents [2,4,[21][22][23][24][25][26], making the system environmentally friendly and enhancing the activity and selectivity of enzyme. A beneficial side effect is the increased stability, indicating longer t ½ .…”

Section: Monophasic Reactions Compared With Biphasic Reactions In Thementioning

confidence: 99%

On the background of enhanced stability and reusability of enzymes in ionic liquids

Fehér

Major

Bélafi–Bakó

et al. 2007

Biochemical Society Transactions

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The ability of ILs (ionic liquids) to provide an environment of increased stability and, in this way, improve the recyclability of enzymes has been studied. The description of this phenomenon is not easy; there are several approaches for explanation. In this mini-review, the results from different research groups are summarized, with the aim of explaining the strong stability effect of ILs on several enzymes. Spectroscopic methods (e.g. fluorescence and CD, IR spectroscopy, mass spectroscopy and NMR) and investigations of polarity and kosmotropicity of ions are promising methods. Since higher stability means that we may be able to reuse enzymes more times, the recyclability of enzymes was also in the focus. From this point of view, the advantages and disadvantages of applying monophasic or biphasic systems are discussed too, presenting the coupled techniques as well.

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Section: Monophasic Reactions Compared With Biphasic Reactions In Thementioning

confidence: 99%

On the background of enhanced stability and reusability of enzymes in ionic liquids

Fehér

Major

Bélafi–Bakó

et al. 2007

Biochemical Society Transactions

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“…COO]; 22 a highly enantioselective resolution of amino acids was achieved in phosphate buffer using PPL; 57 Novozyme 435 (or CAL-B) has been widely applied in many enzymatic reactions performed in ILs, with high enzyme activities being reported. 19,[58][59][60][61][62] However, low enzyme enantioselectivities of alcalase and Novozyme 435 were also seen in some IL systems. 62 The data listed in Table 1 clearly illustrate that three proteases produced higher ee than two lipases.…”

Section: Effect Of Il Concentrationsmentioning

confidence: 99%

Using ionic liquid [EMIM][CH3COO] as an enzyme-‘friendly’ co-solvent for resolution of amino acids

Zhao

Jackson

Song

et al. 2006

Tetrahedron: Asymmetry

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“…Constantinescu et al 72 also confirmed that the thermal stability of ribonuclease A (RNase A) in aqueous solution of ILs follows the Hofmeister series. Several studies 11,73,74 reported low/no activities of β-glycosidase in aqueous solutions of [BMIM] [BF 4 ], which may be explained by the chaotropic nature of BF 4 − in solutions. 74 An excellent review by Yang 75 systematically discussed the possible mechanisms of Hofmeister effects of ILs on the enzyme activity and stability.…”

Section: Ion Kosmotropicitymentioning

confidence: 99%

Methods for stabilizing and activating enzymes in ionic liquids—a review

Zhao

2010

J of Chemical Tech & Biotech

339

241

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Ionic liquids (ILs) have evolved as a new type of non-aqueous solvents for biocatalysis, mainly due to their unique and tunable physical properties. A number of recent review papers have described a variety of enzymatic reactions conducted in IL solutions; on the other hand, it is important to systematically analyze methods that have been developed for stabilizing and activating enzymes in ILs. This review discusses the biocatalysis in ILs from two unique aspects (1) factors that impact the enzyme's activity and stability, (2) methods that have been adopted or developed to activate and/or stabilize enzymes in ionic media. Factors that may influence the catalytic performance of enzymes include IL polarity, hydrogen-bond basicity/anion nucleophilicity, IL network, ion kosmotropicity, viscosity, hydrophobicity, the enzyme dissolution, and surfactant effect. To improve the enzyme's activity and stability in ILs, major methods being explored include the enzyme immobilization (on solid support, sol-gel, or CLEA), physical or covalent attachment to PEG, rinsing with n-propanol methods (PREP and EPRP), water-in-IL microemulsions, IL coating, and the design of enzyme-compatible ionic solvents. It is exciting to notice that new ILs are being synthesized to be more compatible with enzymes. To utilize the full potential of ILs, it is necessary to further improve these methods for better enzyme compatibility. This is what has been accomplished in the field of biocatalysis in conventional organic solvents. c 2010 Society of Chemical Industry Keywords: ionic liquid; enzyme activity; enzyme stabilization; immobilization; biocatalysis NOTATION CationsBMIM + = 1-butyl-3-methylimidazolium C 2 OC 1 MIM + = 1-(2-methoxy)ethyl-3-methylimidazolium C 2 OHMIM + = 1-(2-hydroxy)ethyl-3-methylimidazolium EMIM + = 1-ethyl-3-methylimidazolium

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Enzyme Catalysed Synthesis in Ambient Temperature Ionic Liquids

Cited by 67 publications

References 14 publications

On the background of enhanced stability and reusability of enzymes in ionic liquids

On the background of enhanced stability and reusability of enzymes in ionic liquids

Using ionic liquid [EMIM][CH3COO] as an enzyme-‘friendly’ co-solvent for resolution of amino acids

Methods for stabilizing and activating enzymes in ionic liquids—a review

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