Summary
Noncovalent complexes were formed by lyophilization of aqueous solutions containing horse liver alcohol dehydrogenase, NAD+ and a polymer [ethyl cellulose or poly(vinyl butyral)]. The complexes expressed higher specific catalytic activity in organic solvents as compared to a corresponding amount of enzyme deposited on to Celite or lyophilized enzyme powder. The noncovalent complexes were soluble in toluene. In butyl acetate and methyl t-butyl ether, suspensions of fine particles were formed.
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Virto, C., Svensson, I., Adlercreutz, P. et al. Catalytic activity of noncovalent complexes of horse liver alcohol dehydrogenase, NAD+ and polymers, dissolved or suspended in organic solvents. Biotechnol Lett 17, 877–882 (1995). https://doi.org/10.1007/BF00129022
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DOI: https://doi.org/10.1007/BF00129022