<br/>Lignocellulosic materials are of the most promising renewable feedstocks available for human exploitation. Its biological conversion with enzymes offers producing a range of sugar residues in an ecofriendly way (low energy and water consumption). Enzymatic hydrolysis at high solid loadings (≥15% w/w) would render the conversion process more economically feasible. However, this remains a challenge given the poor understanding we have of enzyme activity in a dense medium, limited diffusion of the enzyme and changed mode of action. We prepared a low volume and highly organized model platform to mimic enzymatic activity. It is known that highly concentrated suspensions of rod-like cellulose nanocrystals (CNCs) (200 nm long x 10 nm section) self-assemble to form stable cholesteric liquid crystalline (LC) phases with pitches of few tens of microns. We thus prepared droplets of such highly concentrated suspension resulting in 100 to 200 µm diameter droplets in LC form presenting concentric organization. Using deep-UV synchrotron radiation, the localization of proteins is probed either in organized and disordered areas using their autofluorescence. Two proteins are compared, an economically significant enzyme (glucanase GH7) and a control protein, bovine serum albumine (BSA). We will highlight the different technical challenges of such investigation and describe the influence of the proteins on CNC organization and vice versa.

Dense and organized cellulose nancrystals emulsion droplets as model to study enzyme action

ACS Spring Meeting 2021

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