초록
<P>Class-I aldolases are known for efficiently catalyzing stereoselective aldol-addition reactions in bulk aqueous media, and considerable efforts are currently being devoted to engineer the enzyme in order to optimize its activity and stability, primarily by modulating the hydrophobicity of the catalytic active site. Here, we opt for a different strategy based on choosing a nanoconfined environment favorable to the enzyme. We report the observation of enhanced activity and stability of a class-I aldolase, <SMALL>D</SMALL>-fructose-6-phosphate aldolase from <I>E. coli</I> (FSA), when incorporated into lipidic cubic mesophases (LCMs), a class of biomimetic amphiphilic complex fluids employed in several nanotechnology applications. We infer that this improved in-meso performance is achieved by optimal location of the FSA in the LCMs, as a result of the known interaction between the residues of FSA and the glycerol moieties, which serve as the lipid head groups and thus locate along the amphiphilic interface encompassing the whole LCM. This continuous interface ensures increased accessibility of the catalytic reaction center to substrates and high activity in LCM.</P><BR>[FIG OMISSION]</BR>