CHED 391 |
| Many fragrances, flavors, insect pheromones, and building blocks for important pharmaceuticals are single enantiomers of lactones. Our investigations look at synthesizing these optically active lactones under mild conditions according to the reaction diagrammed below. The nitrilase enzyme hydrolyzes the g-hydroxynitrile to the corresponding g-hydroxyacid, which spontaneously esterifies to the lactone. In the past, straight side chains with various numbers of carbons have been tested with six different nitrilases. To better understand the active site of the enzymes and the reaction, different reaction conditions and substrates were studied. These investigations include branched side chains, decreased reaction temperatures, and b-hydroxynitriles. Currently, we are synthesizing the prochiral substrate, 4-hydroxyheptane-1,7-dinitrile. This may prove to be the optimal substrate if the enzyme performs mononitrile hydrolysis to yield 100% of one enantiomer. This project will add to our understanding of the nitrilases used, which in turn can be applied to the production of important chiral lactones.
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Undergraduate Research Poster Session: Organic Chemistry
11:00 AM-1:00 PM, Monday, 27 March 2006 Georgia World Congress Center -- Ex. Hall B4, Poster
Division of Chemical Education |
