文摘
We studied the performance of Fusarium solani pisi cutinase, immobilized on a zeolite, insupercritical fluids. The catalytic activity of the enzyme was strongly dependent on wateractivity, was unaffected by pressure up to 300 bar, and was higher in supercritical ethylenethan in supercritical carbon dioxide. The enzyme was very selective toward one of the isomersof 1-phenylethanol, with an enantiomeric excess of virtually 100%, regardless of water activity,pressure, solvent, and temperature. We used the X-ray crystal structure of the enzyme and dida computer modeling of the structures of the transition states formed by the two enantiomers.The differences between these structures helped elucidate the preference for the (R)-enantiomer.