@ARTICLE{Zniszczoł_Aurelia_Kinetics_2017,
 author={Zniszczoł, Aurelia and Szymańska, Katarzyna and Kocurek, Jacek and Bryjak, Jolanta and Walczak, Krzysztof and Jarzębski, Andrzej},
 volume={vol. 38},
 number={No 2},
 journal={Chemical and Process Engineering},
 pages={209-215},
 howpublished={online},
 year={2017},
 publisher={Polish Academy of Sciences Committee of Chemical and Process Engineering},
 abstract={The studies showed that alkaline lipase from Pseudomonas fluorescens enables an irreversible transesterification of vinyl esters to give enantiomeric excess (eeR) of about 80% using vinyl butyrate as acyl donor and diisopropyl ether as a solvent, at partially optimized conditions. For the native lipase the process was adequately described by a five-parameter Ping-Pong Bi Bi model for both enantiomers plus expression accounting for the formation of enzyme-acyl donor complex, but for the same lipase supported on mesoporous materials of SBA-15-Oc type, R-product inhibition also had to be taken into account. The use of hydrophobic support increased by more than two-fold the rate of the S-solketal conversion but even more that of R-solketal. Thus the immobilization of lipase had very positive effect on the process kinetics but decreased its enantioselectivity.},
 type={Artykuły / Articles},
 title={Kinetics of Enantiomerically Enriched Synthesis of Solketal Esters Using Native and SBA-15 supported P. Fluorescens Lipase},
 URL={http://journals.pan.pl/Content/107725/PDF-MASTER/02-paper.pdf},
 doi={10.1515/cpe-2017-0016},
 keywords={bioenantioselectivity, solketal, ping-pong kinetics, transesterification},
}