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Modulation of gastric lipolysis by the phospholipid specie: link to specific lipase-phospholipid interaction at the lipid/water interface?

Lookup NU author(s): Dr Gaelle Fave


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Triglycerides lipolysis by gastric lipase (HGL) is dependent of the lipid/water interface properties. Our objective was to research strategies to increase lipase action by optimizing the interface quality. Several radiolabeled triolein emulsions containing different phospholipid species (PL) were prepared by sonication and characterized (lipid-droplet size and zeta potential). Specific interaction between HGL and PL was researched using BIAcore and monolayer technique. Emulsions hydrolysis were conducted in vitro in physiological conditions with purified HGL or gastric juice from different subjects. Lipolysis rates were determined after free fatty acids extraction and quantitation ([3H] counting). The data shown that PL type influences emulsion droplet-size and stability over time and markedly affects HGL activity (SM diminished lipolysis by 80%, whereas other PL increased it by 25 to 191%). The lipolysis increase was linked to compressibility and electrokinetic value (–18mV) of the PL, higher binding rate of HGL to PL, and involved HGL sources as integrity of HGL N-terminal sequence. In conclusion, the activatory effect of certain PL on HGL activity could be applied in enteral nutrition field to formulate a new type of enteral lipid emulsion whose physicochemical properties optimize lipid digestion and absorption in subjects with pancreatic insufficiency. Supported by ISL.

Publication metadata

Author(s): Favé G, Lévêque C, Peyrot J, Pieroni G, Coste TC, Armand M

Publication type: Conference Proceedings (inc. Abstract)

Publication status: Published

Conference Name: FASEB Journal: Experimental Biology annual meeting

Year of Conference: 2007

Pages: 800.1

ISSN: 0892-6638

Publisher: Federation of American Societies for Experimental Biology


Library holdings: Search Newcastle University Library for this item

ISBN: 15306860