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Interactions of lipases with lipid monolayers: Facts and questions by G. Piéroni; Y. Gargouri; L. Sarda; R. Verger is a Materials Science article available to read on EtoBox.

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Among the proteins, lipolytic enzymes provide a valuable model for studying proteinlipid interactions. Lipases having a catalytic action which is strictly dependent upon the presence of a lipid interface were used in the present study in order to gain better insight into protein-lipid interactions. Most of the data presented here were obtained using the monolayer technique, by recording (either independently or simultaneously) the lipolytic activity, the amount of protein adsorbed to the lipid monolayer, and the surface pressure variations following protein adsorption. Several non-enzymatic proteins were used as controls in order to determine how lipase behaviour differs from that of other proteins. At all initial surface pressures tested, with zwitterionic monolayers, a good correlation was observed between the amount of lipase bound to the monolayer and the surface pressure increase, in agreement with previous studies. Conversely, with neutral lipid monolayer-s the amount of lipase bound to the monolayer was not found to be surface pressure dependent. This latter behaviour observed with lipases on neutral films is not specific to lipases, since it was also observed with bovine se

Who reads Interactions of lipases with lipid monolayers: Facts and questions?

Author

G. Piéroni; Y. Gargouri; L. Sarda; R. Verger

Publisher

Elsevier Science; Elsevier ; Elsevier BV (ISSN 0001-8686)

Published

1990

Language

EN

Field

Materials Science (Physical Sciences)