Effects of enantiomeric solvents on the activity, thermostability and activation energy of lipoprotein lipase |
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Authors: | Gianluca Ottolina Francesca Gianinetti Sergio Riva Giacomo Carrea |
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Affiliation: | Istituto di Chimica degli Ormoni, CNR Via Mario Bianco 9, Milano 20131, Italy |
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Abstract: | The kinetic parameters (Km and Vmax) of lipoprotein lipase (LPL)-catalyzed transesterification were determined in (R)- and (S)-carvone, and in mixtures of the two. It was found that only Vmax was significantly affected by solvent chirality. LPL thermostability was not influenced by solvent config- uration, whereas activation energy was twice as high in (R)-carvone as in (S)-carvone. |
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