RESUMEN
Using synthetic sulfobetaine library, the enzyme activation behavior has been investigated. Comparison of enzyme activation behavior revealed that sulfobetaines equally facilitate enzyme reactions, being consistent with that of carboxybetaines. The subsequent kinetic and solution property analyses clarified that both the kinetic parameter and hydration property changes are identical with those of carboxybetaines, indicating that the difference in the anionic functional group of the betaine structure scarcely affects the enzyme activation. On the other hand, comparison of carboxy- or sulfo-betaines with tetraalkylammonium salts, whose counteranion binds to the ammonium cation intermolecularly, revealed that the activation ability for enzymes of tetraalkylammonium salts is considerably smaller than that of carboxy- or sulfo-betaines. These findings give us a hint to design the useful betaine-type enzyme activators.