Highly Retained Enzymatic Activities of Two Different Cellulases Immobilized on Non-porous and Porous Silica Particles

다국어 초록 (Multilingual Abstract)

Efficient biological degradation of lignocellulosicbiomass is a key step towards developing sustainablebiorefineries. One potential approach to improve processefficiency is the use of enzyme immobilization to facilitatereuse of the enzymes. Two different commercial cellulasecontaining enzyme preparations, termed Cellulases 1 (C1)and Cellulases 2 (C2) for the purposes of this manuscript,were separately immobilized on non-porous silica (S1) andporous silica (S2). The effect of pH, ionic strength andenzyme loading on enzyme stability and activity were allinvestigated. Immobilized cellulases on S1 showed equivalentenzyme activity as free cellulases, and those on S2 retained60% enzyme activity. Dissociation of the cellulases fromthe support after immobilization and during hydrolysis wasfound to be minimal, suggesting strong enzyme-supportinteractions. Further, Scanning Electron Microscopy imagesrevealed that S1 and S2 containing immobilized cellulasesdifferentially interact with cellulose, which likely contributesto the observed differences in hydrolysis.

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