@article{Itabaiana Jr. I._Gonçalves K.M._Cordeiro Y.M.L._ Zoumpanioti M._Leal I.C.R._Miranda L.S.M._De Souza R.O.M.A._ Xenakis A._2013, title={Kinetics and mechanism of lipase catalyzed monoacylglycerols synthesis}, volume={96}, ISSN={1381-1177}, archiveLocation={Ινστιτούτο Χημικής Βιολογίας - Επιστημονικό έργο}, url={https://hdl.handle.net/10442/17673}, DOI={10.1016/j.molcatb.2013.06.008}, abstractNote={Monoacylglycerols are increasingly used in several industrial applications as effective and cheap emulsifiers. In the present work monostearin synthesis has been studied, using lipase as a biocatalyst of the esterification reaction of stearic acid with (R,S)-1,2-O-iso-propylidene glycerol (solketal). The lipase from Candida antarctica (CaL B) was immobilized in AOT/isooctane water in oil microemulsions. Optimization of the reaction conditions have shown that the highest production (80% in 30 min) could be achieved at 40 °C, in microemulsions with relatively low water content (wo = 8). Kinetic studies have shown that the esterification reaction of stearic acid with solketal catalyzed by CaL B occurs via the ordered bi-bi mechanism, in which inhibition by the acid was identified. Moreover, at high fixed solketal concentrations a negative cooperativity is pronounced, which means that binding of the alcohol lowers the affinity of the enzyme for binding of the acid. Values of all kinetic parameters have been determined.}, journal={Journal of Molecular Catalysis B: Enzymatic}, publisher={Elsevier B.V.}, author={Itabaiana Jr. I. and Gonçalves K.M. and Cordeiro Y.M.L. and Zoumpanioti M. and Leal I.C.R. and Miranda L.S.M. and De Souza R.O.M.A. and Xenakis A.}, year={2013}, pages={34–39} }