Single-batch, homogeneous phase depolymerization of cellulosecatalyzed by a monocomponent endocellulase in ionic liquid[BMIM][Cl]

tThe stability and enzymatic activity of an industrial, recombinant cellulase dissolved either in 1-butyl-3-methylimidazolium chloride [BMIM][Cl] or in mixtures of [BMIM][Cl]/aqueous buffer have beeninvestigated and the results are here reported. The preparation used was a recombinant monocompo-nent endocellulase from Trichoderma reesei or EGIII (now renamed Cel12A), commercially referred to asIndiAge®Super GX Plus. The key parameters studied were: the effect of temperature in the range between75 and 90◦C, the enzyme stability at 75◦C and the ability of EGIII to hydrolyze cellulose in the presenceof [BMIM][Cl]. This cellulase preparation turns out to be more stable and active in pure ionic liquid ratherthan in buffer. These results indicate that the recombinant, monocomponent endocellulase from T. reeseiis a suitable biocatalyst for the depolymerization of cellulose in [BMIM][Cl] and it therefore opens theway to a possible one-pot process based on a homogeneous phase, enzyme-catalyzed depolymerizationof cellulose.