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Pancreatic lipase–colipase binds strongly to the thylakoid membrane surface
Author(s) -
Emek Sinan Cem,
Åkerlund HansErik,
ErlansonAlbertsson Charlotte,
Albertsson PerÅke
Publication year - 2013
Publication title -
journal of the science of food and agriculture
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.782
H-Index - 142
eISSN - 1097-0010
pISSN - 0022-5142
DOI - 10.1002/jsfa.6034
Subject(s) - thylakoid , colipase , lipase , biochemistry , chemistry , trypsin , dissociation constant , triacylglycerol lipase , enzyme , chloroplast , receptor , gene
Background Isolated thylakoid membranes, i.e. the photosynthetic membranes of green leaves, inhibit the activity of pancreatic lipase and colipase during hydrolysis of fat in vitro . This inhibition has been demonstrated to cause reduced food intake and improved hormonal and lipid profile in vivo . One of the reasons suggested for the inhibiting effect is binding of lipase–colipase to the thylakoid membrane surface. This prompted a study of the binding of lipase and colipase to thylakoids . Results The results showed that lipase and colipase strongly bind to the thylakoid membrane surface. The dissociation constant was determined at 1.2 × 10 −8 mol L −1 ; binding decreased after treatment of thylakoids with pepsin/trypsin to 1.0 × 10 −7 and to 0.6 × 10 −7 mol L −1 after treatment with pancreatic juice. Similarly, delipidation of thylakoids caused a decrease in binding, the dissociation constant being 2.0 × 10 −7 mol L −1 . Conclusion The binding of pancreatic lipase–colipase to the thylakoid membrane is strong and may explain the inhibition of lipase–colipase activity by thylakoids. After treatment with proteases to mimic intestinal digestion binding is decreased, but is still high enough to explain the observed metabolic effects of thylakoids in vivo . © 2013 Society of Chemical Industry