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By Cotor V., Alfonso I., Garcia-Urdiales E. (eds.)

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In contrast, enantioselectivity is a parameter that chemists, biochemists, and enzymologists traditionally associate with the active center and the binding pocket, in the tradition of Emil Fischer’s hypothesis of lock-and-key or Koshland’s model of induced fit [45]. Indeed, all previous attempts to influence the enantioselectivity of an enzyme based on site-specific mutagenesis as suggested by rational design focused on the binding pocket [9]. The initial results of the MM/QM study regarding the source of enhanced enantioselectivity led to several plausible conclusions [36a].

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Antarctica and esterase from Bacillus stearothermophilus were found to be 17, 3, and 30 times more stable in ionic liquids than in organic solvents [47b]. Several reports deal also with the effects of ionic liquids on enzyme enantioselectivity, which is the subject of this chapter. Although in several cases there was no change or even a decrease in enantioselectivity compared to organic solvents [47], in other cases improved enantioselectivity was observed [47,49–56]. In the following text, the latter cases will be examined in some detail.

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