Pharmaceutical Research

, Volume 28, Issue 8, pp 1831–1842

Effects of Surfactants on Lipase Structure, Activity, and Inhibition

  • Vincent Delorme
  • Rabeb Dhouib
  • Stéphane Canaan
  • Frédéric Fotiadu
  • Frédéric Carrière
  • Jean-François Cavalier
Expert Review

DOI: 10.1007/s11095-010-0362-9

Cite this article as:
Delorme, V., Dhouib, R., Canaan, S. et al. Pharm Res (2011) 28: 1831. doi:10.1007/s11095-010-0362-9

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.

KEY WORDS

inhibitor interfacial enzymology lipase lipid-protein interaction surfactant 

ABBREVIATIONS

β-OG

β-octyl glucoside

BSA

bovine serum albumin

CMC

critical micellar concentration

DGL

dog gastric lipase

EPR

electron paramagnetic resonance

E600

diethyl p-nitrophenyl phosphate

GPLRP2

guinea pig pancreatic lipase-related protein 2

HPL

human pancreatic lipase

NaTDC

sodium taurodeoxycholate

PPL

porcine pancreatic lipase

SDS

sodium dodecyl sulphate

SDSL

site-directed spin labeling

TAG

triacylglycerol

TGME

tetraethylene glycol monooctyl ether

THL

tetrahydrolipstatin (Orlistat)

TLL

Thermomyces lanuginosus lipase

YLLip2

Yarrowia lipolytica Lip2

Copyright information

© Springer Science+Business Media, LLC 2011

Authors and Affiliations

  • Vincent Delorme
    • 1
    • 2
  • Rabeb Dhouib
    • 1
  • Stéphane Canaan
    • 1
  • Frédéric Fotiadu
    • 2
  • Frédéric Carrière
    • 1
  • Jean-François Cavalier
    • 1
  1. 1.CNRS - Aix-Marseille Université - Enzymologie Interfaciale et Physiologie de la LipolyseMarseille cedex 20France
  2. 2.UMR 6263 CNRS-École Centrale Marseille-Université Paul Cézanne, Equipe ChirosciencesMarseille Cedex 20France

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