Controlling lipase stereoselectivity via the surface pressure.
In the present study, the stereoselectivity of Rhizomucor miehei lipase, lipoprotein lipase, Candida antarctica B lipase, and human gastric lipase towards racemic dicaprin spread as a monolayer at the air-water interface was investigated. For this purpose we have developed a method with which the enantiomeric excess of the residual substrate can be measured in monomolecular films. The stereoselectivity, which is one of the main aspects of enzymic catalysis, was found to depend on the surface pressure of the substrate. With all four lipases tested, low surface pressures enhanced the stereoselectivity while decreasing the enzymes' catalytic activity.[1]References
- Controlling lipase stereoselectivity via the surface pressure. Rogalska, E., Ransac, S., Verger, R. J. Biol. Chem. (1993) [Pubmed]
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