Synergism of ionic liquids and lipases for lignocellulosic biomass valorization

Šibalić, Darijo; Šalić, Anita; Zelić, Bruno; Tran, Nam Nghiep; Hessel, Volker; Nigam, K.D.P.; Tišma, Marina

doi:10.1016/j.cej.2023.142011

Cited by 17 publications

(2 citation statements)

References 140 publications

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“…The structures of several commonly employed cations and anions are illustrated in Figure 2 . Because of their advantages such as low vapor pressure and nonflammability, ILs are considered to be highly promising green solvents and are expected to replace toxic, flammable, and volatile organic solvents [ 68 ]. ILs also exhibit good biocompatibility.…”

Section: Effect Of Different Solvents On Stability and Activity Of Li...mentioning

confidence: 99%

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art

Chen,

Jin,

Nian

et al. 2024

Molecules

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Lipases, crucial catalysts in biochemical synthesis, find extensive applications across industries such as food, medicine, and cosmetics. The efficiency of lipase-catalyzed reactions is significantly influenced by the choice of solvents. Polar organic solvents often result in a decrease, or even loss, of lipase activity. Conversely, nonpolar organic solvents induce excessive rigidity in lipases, thereby affecting their activity. While the advent of new solvents like ionic liquids and deep eutectic solvents has somewhat improved the activity and stability of lipases, it fails to address the fundamental issue of lipases’ poor solvent tolerance. Hence, the rational design of lipases for enhanced solvent tolerance can significantly boost their industrial performance. This review provides a comprehensive summary of the structural characteristics and properties of lipases in various solvent systems and emphasizes various strategies of protein engineering for non-aqueous media to improve lipases’ solvent tolerance. This study provides a theoretical foundation for further enhancing the solvent tolerance and industrial properties of lipases.

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Section: Effect Of Different Solvents On Stability and Activity Of Li...mentioning

confidence: 99%

Solvent Tolerance Improvement of Lipases Enhanced Their Applications: State of the Art

Chen,

Jin,

Nian

et al. 2024

Molecules

View full text Add to dashboard Cite

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“…This is due to their robustness, lack of cofactors and wide specificity, and ability to accept a wide variety of substrates. Their high stability has enabled the use of lipases in a wide variety of reaction media (e.g., aqueous [7,8], organic solvents [2,9], supercritical fluids [10,11], ionic liquids [12][13][14][15][16], eutectic solvents [17,18], solvent-free systems [19]), and their variety of substrates permits to use them in a diversity of industrial areas [20] (wastewater treatment [21], food [22][23][24], energy [25,26], cosmetic [27], pharmaceutical [28][29][30], fine chemistry [31][32][33][34][35][36]). They can be used in hydrolysis [7,8], acidolysis [37,38], interesterifications [39,40], esterifications [19,41,42], transesterifications [25,43], amidations [44][45][46], etc.…”

Section: Introductionmentioning

confidence: 99%

Tuning Almond Lipase Features by Using Different Immobilization Supports

Cherni,

Carballares,

Siar

et al. 2024

Catalysts

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The lipase from Prunus dulcis almonds has been immobilized for the first time. For this purpose, two different supports, an octadecyl methacrylate particulate support, and aminated agarose (monoaminoethyl-N-aminoethyl) have been utilized. Both immobilized biocatalysts show improved enzyme stability, but great changes in enzyme specificity were detected. The enzyme immobilized via ion exchange maintained its activity intact versus p-nitrophenyl butyrate, while the enzyme immobilized on the hydrophobic support fully lost its activity versus this substrate, which was confirmed to be due to substrate adsorption on the support. However, this biocatalyst was much more active versus triacetin (more than 10-fold), R- or S- methyl mandelate at pH 7. At pH 9, a strong effect of using phosphate or bicarbonate as reaction buffers was detected. Using bicarbonate, the interfacially immobilized enzyme presented no activity versus R-isomer, but it was very active versus the S-isomer and triacetin. Using a phosphate buffer during the reaction, all compounds were recognized as substrates. The enzyme immobilized via ion exchange was significantly more active using phosphate; in fact, using bicarbonate, the enzyme was inactive versus both methyl mandelate isomers. This paper shows for the first time a great interaction between the effects of the immobilization protocol and buffer used during reaction on the enantiospecificity of lipases.

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