Cross-linked Candida antarctica lipase B is active in denaturing ionic liquids

Toral, Antonio Ruiz; Ríos, Antonia Pérez de los; Hernandez, Francisco Jose Arraez; Janssen, Michiel H. A.; Schoevaart, Rob; Rantwijk, Fred van; Sheldon, Roger A.

doi:10.1016/j.enzmictec.2006.08.027

Cited by 127 publications

(61 citation statements)

References 23 publications

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“…105,142 -147 Higher enzyme stability is expected for CLEAs in ILs than free enzymes. Toral et al 39 immobilized CALB through two methods: a CLEA method without a solid support (resulting in CALB-CL), and adsorbed and cross-linked on a polypropylene carrier (resulting in CALB-PP). They carried out several reactions using these two enzyme preparations in denaturing ILs ( 4 ] doped DNA network casting on a gold electrode; the new biosensor exhibited a short response time (2 s), a low detection limit (3.5 µmol L −1 ), a wide linear range (0.01-7.4 mmol L −1 ), as well as a high sensitivity and stability.…”

Section: C) Cross-linked Enzyme Aggregates (Cleas  )mentioning

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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Section: C) Cross-linked Enzyme Aggregates (Cleas  )mentioning

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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“…Additionally, factors such as viscosity, hydrophobicity/hydrophilicity, and IL impurities are known to influence enzyme performance. Immobilization [8,26] and chemical modifications of enzymes through PEGylation [27,28] and succinylation [29][30][31] have been reported to improve activity, stability, and/or enzymes resistance to ILs.…”

Section: Introductionmentioning

confidence: 99%

Towards Understanding Directed Evolution: More than Half of All Amino Acid Positions Contribute to Ionic Liquid Resistance of Bacillus subtilis Lipase A

et al. 2015

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Ionic liquids (ILs) are attractive (co-)solvents for biocatalysis. However, in high concentration (>10 % IL), enzymes usually show decreased activity. No general principles have been discovered to improve IL resistance of enzymes by protein engineering. We present a systematic study to elucidate general engineering principles by site saturation mutagenesis on the complete gene bsla. Screening in presence of four [BMIM]-based ILs revealed two unexpected lessons on directed evolution: 1) resistance improvement was obtainable at 50-69 % of all amino acid positions, thus explaining the success of small sized random mutant libraries; 2) 6-13 % of substitutions led to improved resistance. Among these, 66-95 % were substitutions by chemically different amino acids (e.g., aromatic to polar/aliphatic/charged amino acids), thus indicating that mutagenesis methods introducing such changes should, at least for lipases like BSLA, be favored to improve IL resistance.

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“…Moreover, the amount of halide content was determined by a silver chromate test following a similar protocol to that described by Sheldon and co-workers. 30 Additionally, it should also be considered that the AER used in the exchange can be recycled by treatment with 10% NaOH aqueous solution, and the recovered AER (OH¯ form) can be reutilized for a new anion loading. The chosen strong AER was Amberlyst® A-26 but other similar AERs such Aberlite® IRA-400, which allow the use of aqueous mixtures and nonaqueous solvents, can be used instead.…”

Section: Halide-to-anion Exchange: Aer (A¯ Form) Methodsmentioning

confidence: 99%

“…1-buthyl-3-methylimidazolium salts 1a·A, 1 1-buthyl-3-methyltriazolium iodide 2a·I, 15 1-benzyl-3-methyltriazolium iodide 2b·I, 15 The amount of halide contents was determined by a silver chromate test following a similar protocol to that described by Sheldon and co-workers. 30 An aqueous solution (5 mL) of potassium chromate (5 % p/v in Milli-Q water, 0.257 M) was added to the sample (5-10 mg). To 1 mL of the resulting dark yellow solution was added a minimum amount of silver nitrate aqueous solution (0.24 % p/v in Milli-Q water, 0.014 M).…”

Section: Issue In Honor Of Prof Rosa M a Claramunt Arkivoc 2014 (Ii)mentioning

confidence: 99%

Azolium-based systems: application of an anion exchange resin (A- form) method and 1H NMR analysis of the charged-assisted (C–H)+•anion hydrogen bonds

Dinarés¹,

Mesquida²,

Ibáñez³

et al. 2013

Arkivoc

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Dedicated to Prof. Rosa M. Claramunt on the occasion of her 65th birthday AbstractThe counteranion exchange of quaternary 1,2,3-triazolium salts was examined using a simple method that permitted halide ions to be swap for a variety of anions using an anion exchange resin (A¯ form). The method was applied to 1,2,3-triazolium-based ionic liquids and the iodideto-anion exchange proceeded in excellent to quantitative yields, concomitantly removing halide impurities. Additionally, an anion exchange resin (N 3¯ form) was used to obtain the benzyl azide from benzyl halide under mild reaction. Likewise, following a similar protocol, bis(azidomethyl)arenes were also synthesized in excellent yields. The results of a proton NMR spectroscopic study of simple azolium-based ion pairs are discussed, with attention focused on the significance of the charged-assisted (C-H) + ···anion hydrogen bonds of simple azolium systems such as 1-butyl-3-methylimidazolium and 1-benzyl-3-methyl-1,2,3-triazolium salts.

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Cross-linked Candida antarctica lipase B is active in denaturing ionic liquids

Cited by 127 publications

References 23 publications

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

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

Towards Understanding Directed Evolution: More than Half of All Amino Acid Positions Contribute to Ionic Liquid Resistance of Bacillus subtilis Lipase A

Azolium-based systems: application of an anion exchange resin (A- form) method and 1H NMR analysis of the charged-assisted (C–H)+•anion hydrogen bonds

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