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Caption : figure s1.  ft-ir spectra of sarcoine-, ectoine-, tmao-, and betaine-based des.

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Caption : figure s2. ft-ir spectra of proline- and dmsp-based des, together with spectra of multicomponent bioinspired des tmao:bet:tau:u and bet:sor:tau:gpc:u.

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Caption : figure s3. time-dependent optical density (λ= 600 nm) of lysozyme solution (c<sub>lys</sub> = 5 mg ml<sup>-1</sup>) at 80°c in 50 mm potassium phosphate buffer solution (ph 6.4), tmao:u (40% of water, w/w), and bioinspired multicomponent des bet:sor:tau:gpc:u (40% of water, w/w).

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Caption : figure s4. first derivations of melting curves of thermal cd scans of lysozyme in 50 mm potassium phosphate buffer solution (ph 6.4) and des solvents (c<sub>lys</sub> = 0.3-0.4 mg ml<sup>-1</sup>; λ=227±5 nm).

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Caption : figure s5. near uv cd spectra of lysozyme (clys = 0.2 mg ml<sup>-1</sup>) dissolved in (a) pro:gly (40% of water, w/w)  and (b) bet:gly (40% of water, w/w) before thermal treatment (black line), at 80°c (red line), 95°c (green line), and 20°c after cooling (blue dotted line).

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Caption : figure s6. residual lysozyme activity (a<sub>r</sub>) after incubation in des (containing 40% of water, w/w) and 50 mm potassium phosphate buffer solution (ph 6.4) after each freeze/thaw cycle at -20°c (c<sub>lys</sub> = 5 mg ml<sup>-1</sup>). the relative activity (%) was calculated from the initial reaction rate obtained by the enzyme after incubation, compared to the one obtained without previous exposure.

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Caption : figure s7. residual lysozyme activity (a<sub>r</sub>) after incubation in des (containing 40% of water, w/w) and 50 mm potassium phosphate buffer solution (ph 6.4) after each freeze/thaw cycle at -80°c (c<sub>lys</sub> = 5 mg ml<sup>-1</sup>). the relative activity (%) was calculated from the initial reaction rate obtained by the enzyme after incubation, compared to the one obtained without previous exposure.

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Caption : figure s8. relative lysozyme activity (a<sub>a</sub>) in des (40% of water, w/w; c<sub>lys</sub> = 5 mg ml<sup>-1</sup>). the relative lysozyme activity (a<sub>a</sub>) was calculated from the initial reaction rate obtained by the enzyme after incubation, compared to the one obtained without previous exposure.

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Caption : figure s9. first derivations of melting curves of thermal cd scans of lysozyme in 50 mm potassium phosphate buffer solution (ph 6.4) and bet:sor:tau:gpc:u at different water shares (20, 40, 60 and 80%, w/w) (c<sub>lys</sub> = 0.4 mg ml<sup>-1</sup> λ=225 nm).

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Caption : figure s10. (a) far uv cd spectra of lysozyme dissolved in 50 mm potassium phosphate buffer (ph 6.4) (clys = 0.2 mg ml<sup>-1</sup>) and hydrated lysozyme (dilution of lysozyme solution pre-incubated in bet:sor:tau:gpc:u (40% of water, w/w)) into the buffer, resulting in a final concentration of bet:sor:tau:gpc:u in the buffer of 0.5% (v/v).