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Issue 6, 2011
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Stabilizing immobilized cellulase by ionic liquids for saccharification of cellulose solutions in 1-butyl-3-methylimidazolium chloride

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Abstract

A new approach to improve the cellulase stability against 1-butyl-3-methylimidazolium chloride ([Bmim][Cl]), based on coating of immobilized enzyme particles with hydrophobic ILs, is proposed. The stability of commercial cellulase (Celluclast®), immobilized onto a polymeric support (Amberlite XAD4), was first studied in ten different ionic liquids (ILs) at 50 and 80 °C. Hydrophobic ILs clearly enhanced the enzyme thermal stability. Butyltrimethyl-ammonium bis(trifluoromethylsulfonyl)imide ([N1114][NTf2]) enhances half-life time of the immobilized enzyme at 50 °C up to 4 times, while [Bmim][Cl] behaved as a powerful enzyme deactivating agent. Thus, the stability of cellulase in hydrophobic IL/[Bmim][Cl] mixtures was greatly improved with respect to [Bmim][Cl] alone. A stabilized cellulase derivative obtained by coating immobilized enzyme particles with [N1114][NTf2], has been then successfully used for the saccharification of dissolved cellulose in [Bmim][Cl] (i.e. up to 50% hydrolysis in 24 h) at 50 °C and 1.5 w/v water content.

Graphical abstract: Stabilizing immobilized cellulase by ionic liquids for saccharification of cellulose solutions in 1-butyl-3-methylimidazolium chloride

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Publication details

The article was received on 17 Mar 2011, accepted on 11 Apr 2011 and first published on 16 May 2011


Article type: Communication
DOI: 10.1039/C1GC15294G
Green Chem., 2011,13, 1406-1410

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    Stabilizing immobilized cellulase by ionic liquids for saccharification of cellulose solutions in 1-butyl-3-methylimidazolium chloride

    P. Lozano, B. Bernal, J. M. Bernal, M. Pucheault and M. Vaultier, Green Chem., 2011, 13, 1406
    DOI: 10.1039/C1GC15294G

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