By Cotor V., Alfonso I., Garcia-Urdiales E. (eds.)
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Extra resources for Asymmetric Organic Synthesis with Enzymes
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 Fischers hypothesis of lock-and-key or Koshlands model of induced ﬁt . 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 . 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 , in other cases improved enantioselectivity was observed [47,49–56]. In the following text, the latter cases will be examined in some detail.