<i>Candida rugosa</i> lipase‐catalysed kinetic resolution of 2‐substituted‐aryloxyacetic esters with dimethylsulfoxide and isopropanol as additives

Ammazzalorso, Alessandra; Amoroso, Rosa; Bettoni, Giancarlo; Filippis, Barbara De; Fantacuzzi, Marialuigia; Giampietro, Letizia; Maccallini, Cristina; Tricca, Maria Luisa

doi:10.1002/chir.20505

Cited by 20 publications

(6 citation statements)

References 14 publications

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“…This study demonstrates that the HLD‐catalyzed kinetic resolution can be controlled by addition of organic co‐solvents to the reaction media, depending on the enzyme, the solvent, and the substrate. The effect of organic solvents on enzyme enantioselectivity has been already described for various types of biocatalysts, including lipase [11, 72–76], Baeyer‐Villiger monooxygenase [77], alcohol dehydrogenase [78], carbonyl reductase [8], subtilisin Carlsberg [79], and protease [80]. Several mechanisms have been proposed to rationalize the variability of enzyme enantioselectivity in organic solvents: (i) the interference of the co‐solvent molecules with the proper orientation or transformation of one enantiomer more than the other one [81, 82], (ii) the interaction of co‐solvent molecules with the surface of the enzyme or its active site, resulting in conformational alterations [83], (iii) co‐solvent‐induced shift in the racemic temperature [75].…”

Section: Resultsmentioning

confidence: 99%

Organic co‐solvents affect activity, stability and enantioselectivity of haloalkane dehalogenases

Štěpánková

Damborský

Chaloupková

2013

Biotechnology Journal

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Haloalkane dehalogenases are microbial enzymes with a wide range of biotechnological applications, including biocatalysis. The use of organic co-solvents to solubilize their hydrophobic substrates is often necessary. In order to choose the most compatible co-solvent, the effects of 14 co-solvents on activity, stability and enantioselectivity of three model enzymes, DbjA, DhaA, and LinB, were evaluated. All co-solvents caused at high concentration loss of activity and conformational changes. The highest inactivation was induced by tetrahydrofuran, while more hydrophilic co-solvents, such as ethylene glycol and dimethyl sulfoxide, were better tolerated. The effects of co-solvents at low concentration were different for each enzyme-solvent pair. An increase in DbjA activity was induced by the majority of organic co-solvents tested, while activities of DhaA and LinB decreased at comparable concentrations of the same co-solvent. Moreover, a high increase of DbjA enantioselectivity was observed. Ethylene glycol and 1,4-dioxane were shown to have the most positive impact on the enantioselectivity. The favorable influence of these co-solvents on both activity and enantioselectivity makes DbjA suitable for biocatalytic applications. This study represents the first investigation of the effects of organic co-solvents on the biocatalytic performance of haloalkane dehalogenases and will pave the way for their broader use in industrial processes.

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Section: Resultsmentioning

confidence: 99%

Organic co‐solvents affect activity, stability and enantioselectivity of haloalkane dehalogenases

Štěpánková

Damborský

Chaloupková

2013

Biotechnology Journal

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“…In another similar case of enzymatic hydrolysis resolution reported by Ammazzalorso et al., in order to obtain an enhancement of the enantioselectivity in the Candida rugosa lipase catalyzed hydrolysis of three different 2‐substituted aryloxyacetic esters 134 in aqueous buffer, DMSO and isopropanol (IPA) were tested as additives from 0 to 80% v/v content . DMSO enhanced the enantioselectivity more remarkably than IPA with an enzymatic enantiomeric preference for ( R )‐ 134 a and ( S )‐ 134 b (Table ).…”

Section: Effect Of Cosolventsmentioning

confidence: 96%

Effect of Additives on the Selectivity and Reactivity of Enzymes

Liang

Lin

2016

Chem. Rec.

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Enzymes have been widely used as efficient, eco-friendly, and biodegradable catalysts in organic chemistry due to their mild reaction conditions and high selectivity and efficiency. In recent years, the catalytic promiscuity of many enzymes in unnatural reactions has been revealed and studied by chemists and biochemists, which has expanded the application potential of enzymes. To enhance the selectivity and activity of enzymes in their natural or promiscuous reactions, many methods have been recommended, such as protein engineering, process engineering, and media engineering. Among them, the additive approach is very attractive because of its simplicity to use and high efficiency. In this paper, we will review the recent developments about the applications of additives to improve the catalytic performances of enzymes in their natural and promiscuous reactions. These additives include water, organic bases, water mimics, cosolvents, crown ethers, salts, surfactants, and some particular molecular additives.

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“…In general, low enantioselectivity for crude Candida rugosa lipases (CRL), moderate to high enantioselectivity but with low reactivity for Carica papaya lipase (CPL) were reported. [10][11][12] Many efforts have been made to improve CRL activity and enantioselectivity, for example, use of purified or isopropanol (IPA)-treated lipase, [13][14][15][16][17][18] addition of dimethyl sulfoxide (DMSO), carbon tetrachloride, or benzene, 17,[19][20][21] ionic liquids as the reaction medium, 22 and organosilicon alcohols as the acyl acceptor. 11,12,23 Nevertheless, considerations of solvent toxicity, biocatalyst recycle and downstream separation capability, and cost effective-ness because of low reactivity have hindered such methods practicably used in industry.…”

Section: Introductionmentioning

confidence: 99%

(R,S)‐2‐chlorophenoxyl pyrazolides as novel substrates for improving lipase‐catalyzed hydrolytic resolution

Kao

et al. 2011

Chirality

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The best reaction condition of Candida antartica lipase B as biocatalyst, 3-(2-pyridyl)pyrazole as leaving azole, and water-saturated methyl t-butyl ether as reaction medium at 45°C were first selected for performing the hydrolytic resolution of (R,S)-2-(4-chlorophenoxyl) azolides (1-4). In comparison with the kinetic resolution of (R,S)-2-phenylpropionyl 3-(2-pyridyl)pyrazolide or (R,S)-α-methoxyphenylacetyl 3-(2-pyridyl)pyrazolide at the same reaction condition, excellent enantioselectivity with more than two order-of-magnitudes higher activity for each enantiomer was obtained. The resolution was then extended to other (R,S)-3-(2-pyridyl)pyrazolides (5-7) containing 2-chloro, 3-chloro, or 2,4-dichloro substituent, giving good (E > 48) to excellent (E > 100) enantioselectivity. The thermodynamic analysis for 1, 2, and 4-7 demonstrates profound effects of the acyl or leaving moiety on varying enthalpic and entropic contributions to the difference of Gibbs free energies. A thorough kinetic analysis further indicates that on the basis of 6, the excellent enantiomeric ratio for 4 and 7 is due to the higher reactivity of (S)-4 and lower reactivity of (R)-7, respectively.

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Candida rugosa lipase‐catalysed kinetic resolution of 2‐substituted‐aryloxyacetic esters with dimethylsulfoxide and isopropanol as additives

Cited by 20 publications

References 14 publications

Organic co‐solvents affect activity, stability and enantioselectivity of haloalkane dehalogenases

Organic co‐solvents affect activity, stability and enantioselectivity of haloalkane dehalogenases

Effect of Additives on the Selectivity and Reactivity of Enzymes

(R,S)‐2‐chlorophenoxyl pyrazolides as novel substrates for improving lipase‐catalyzed hydrolytic resolution

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