Enzymes in organic synthesis. 42. Investigation of the effects of the isozymal composition of pig liver esterase on its stereoselectivity in preparative-scale ester hydrolyses of asymmetric synthetic value

The stereospecificities of the isozyme components of commercially available pig liver esterase have been shown to be essentially the same toward representative monocyclic and acyclic diester substrates. This removes previous concerns that the isozymal composition of pig liver esterase, a widely used catalyst for chiral synthon production, might result in its not behaving consistently when applied as a catalyst for asymmetric synthetic purposes. The results establish that commercial pig liver esterase can be exploited synthetically as a chiral catalyst with confidence that it will behave as if it were a single protein. © 1988, American Chemical Society. All rights reserved.

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Author Eric John Toone Chemistry