Description of the Kinetics and Enantioselectivity of Lipases in Various Media

摘要

Originally, the aim of the project was to provide knowledge for enzymaticallycatalyzed kinetic resolution processes. It was soon realized that in order to make reliable predictions, new concepts had to be introduced to describe porcine pancreas lipase (PPL) catalyzed resolution of racemic glycidyl butyrate. A logical step was to extend this to the enzymology of lipases in organic solvents. After further elaboration of the correction for solvent-substrate interaction, experimental verification was performed with PPL and Pseudomonas cepacia lipase (PcL) in several organic solvents. Since extensive measurements on emulsions with PcL had been carried out at DSM, it was attempted in a joint effort to model the data with the equations derived. Enantioselectivity is generally regarded as a very sensitive probe for changes in enzyme performance. Thus, to study effects of organic solvents by another approach, experiments were carried out with PPL and racemic glycidyl in transesterification reactions. Finally, it was realized that the approach developed could contribute also to better insight into classical enzymology in water. For that purpose, binding as well as kinetic properties were modeled for porcine liver esterase, PcL and horse liver alcohol dehydrogenase.