Gargouri_1986_Biochemistry_25_1733

We previously reported that the inhibition of pancreatic and Rhizopus delemar lipases by proteins is due to the protein associated with lipid and is not caused by direct protein-enzyme interaction in the aqueous phase [Gargouri, Y., Pieroni, G., Riviere, C., Sugihara, A., Sarda, L., & Verger, R. (1985) J. Biol. Chem. 260, 2268-2273]. In this study, using radiolabeled lipases, serum albumin, and beta-lactoglobulin A, we investigated their respective binding with respect to lipolysis of dicaprin monolayers. Lipase inhibition was found to be correlated with a lack of lipase binding to mixed protein-dicaprin films or to a desorption of lipase from the interface when inhibitory protein was added later. Since a large proportion of the lipid film remained potentially accessible to the enzyme in the presence of inhibitory protein, it was concluded that the observed decrease in lipase binding to the interface was due to a variation of the physiochemical properties of the lipid-water interface following binding of inhibitory protein. On the basis of the results presented here, it is proposed that mixed protein-glyceride films could be used to characterize the interaction of various lipases with lipid substrates and to classify these enzymes according to their penetration power.