caa a22 4500 445313595 CHVBK 20180317142638.0 cr unu---uuuuu 170323e20110801xx s 000 0 eng 10.1007/s11095-010-0362-9 doi (NATIONALLICENCE)springer-10.1007/s11095-010-0362-9 Effects of Surfactants on Lipase Structure, Activity, and Inhibition [Elektronische Daten] [Vincent Delorme, Rabeb Dhouib, Stéphane Canaan, Frédéric Fotiadu, Frédéric Carrière, Jean-François Cavalier] ABSTRACT: Lipase inhibitors are the main anti-obesity drugs prescribed these days, but the complexity of their mechanism of action is making it difficult to develop new molecules for this purpose. The efficacy of these drugs is known to depend closely on the physico-chemistry of the lipid-water interfaces involved and on the unconventional behavior of the lipases which are their target enzymes. The lipolysis reaction which occurs at an oil-water interface involves complex equilibria between adsorption-desorption processes, conformational changes and catalytic mechanisms. In this context, surfactants can induce significant changes in the partitioning of the enzyme and the inhibitor between the water phase and lipid-water interfaces. Surfactants can be found at the oil-water interface where they compete with lipases for adsorption, but also in solution in the form of micellar aggregates and monomers that may interact with hydrophobic parts of lipases in solution. These various interactions, combined with the emulsification and dispersion of insoluble substrates and inhibitors, can either promote or decrease the activity and the inhibition of lipases. Here, we review some examples of the various effects of surfactants on lipase structure, activity and inhibition, which show how complex the various equilibria involved in the lipolysis reaction tend to be. Springer Science+Business Media, LLC, 2011 inhibitor nationallicence interfacial enzymology nationallicence lipase nationallicence lipid-protein interaction nationallicence surfactant nationallicence β-OG : β-octyl glucoside nationallicence BSA : bovine serum albumin nationallicence CMC : critical micellar concentration nationallicence DGL : dog gastric lipase nationallicence EPR : electron paramagnetic resonance nationallicence E600 : diethyl p-nitrophenyl phosphate nationallicence GPLRP2 : guinea pig pancreatic lipase-related protein 2 nationallicence HPL : human pancreatic lipase nationallicence NaTDC : sodium taurodeoxycholate nationallicence PPL : porcine pancreatic lipase nationallicence SDS : sodium dodecyl sulphate nationallicence SDSL : site-directed spin labeling nationallicence TAG : triacylglycerol nationallicence TGME : tetraethylene glycol monooctyl ether nationallicence THL : tetrahydrolipstatin (Orlistat) nationallicence TLL : Thermomyces lanuginosus lipase nationallicence YLLip2 : Yarrowia lipolytica Lip2 nationallicence Delorme Vincent CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut Dhouib Rabeb CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut Canaan Stéphane CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut Fotiadu Frédéric UMR 6263 CNRS-École Centrale Marseille-Université Paul Cézanne, Equipe Chirosciences, Avenue Escadrille Normandie-Niemen, 13397, Marseille Cedex 20, France aut Carrière Frédéric CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut Cavalier Jean-François CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut Pharmaceutical Research Springer US; http://www.springer-ny.com 28/8(2011-08-01), 1831-1842 0724-8741 28:8<1831 2011 28 11095 https://doi.org/10.1007/s11095-010-0362-9 text/html Onlinezugriff via DOI 1 review-article jats NATIONALLICENCE 856 40 https://doi.org/10.1007/s11095-010-0362-9 text/html Onlinezugriff via DOI NATIONALLICENCE 700 1- Delorme Vincent CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut NATIONALLICENCE 700 1- Dhouib Rabeb CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut NATIONALLICENCE 700 1- Canaan Stéphane CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut NATIONALLICENCE 700 1- Fotiadu Frédéric UMR 6263 CNRS-École Centrale Marseille-Université Paul Cézanne, Equipe Chirosciences, Avenue Escadrille Normandie-Niemen, 13397, Marseille Cedex 20, France aut NATIONALLICENCE 700 1- Carrière Frédéric CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut NATIONALLICENCE 700 1- Cavalier Jean-François CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la Lipolyse, UPR 9025, 31 chemin Joseph Aiguier, 13402, Marseille cedex 20, France aut NATIONALLICENCE 773 0- Pharmaceutical Research Springer US; http://www.springer-ny.com 28/8(2011-08-01), 1831-1842 0724-8741 28:8<1831 2011 28 11095 Metadata rights reserved Springer special CC-BY-NC licence nationallicence BK010053 XK010053 XK010000 NATIONALLICENCE NATIONALLICENCE NL-springer