Additional file 1 of Computational design of highly stable and soluble alcohol dehydrogenase for NADPH regeneration

Additional file 1: Table S1. Information of NADPH-dependent alcohol dehydrogenase. Table S2. Information of selected alcohol dehydrogenase. Table S3. The mutation sites of the PROSS mutants. Table S4. Thermal stability of the recombinant LkADH. Table S5. Activity half-life of the recombinant CbADH-6M. Figure S1. Multiple sequence alignment of alcohol dehydrogenases. Figure S2. SDS-PAGE analysis of the protein expression of the alcohol dehydrogenases. Figure S3. SDS-PAGE analysis of the protein expression at different inducing temperatures. Figure S4. SDS-PAGE analysis of the protein expression at different IPTG concentration. Figure S5. CbADH activity of molecular chaperones co-expression strains. Fig S6. SDS-PAGE analysis of protein expression of molecular chaperones co-expression strains. Fig S7. Multiple sequence alignment of CbADH mutant. Fig S8. SDS-PAGE analysis of protein expression of PROSS mutants. Fig S9. Protein purification of PROSS mutants. Fig S10 HPLC spectrum of (S)-1-phenylethanol. Fig S11. HPLC spectrum of (S)-1-(4-methylphenyl)ethanol. Fig S12. HPLC spectrum of (S)-1-(4-fluorophenyl)ethanol. Fig S13. HPLC spectrum of (S)-1-(4-chlorophenyl)ethanol. Fig S14. HPLC spectrum of (S)-1-(3,4,5-trifluorophenyl)ethanol.