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The modulation of pancreatic lipase activity by alginates
- Wilcox, Matthew D., Brownlee, Iain A., Richardson, J. Craig, Dettmar, Peter W., Pearson, Jeffrey P.
- Food chemistry 2014 v.146 pp. 479-484
- Laminaria, alginates, biopolymers, enzyme activity, food industry, foods, macroalgae, triacylglycerol lipase, triacylglycerols, weight control
- Alginates are comprised of mannuronic (M) and guluronic acid (G) and have been shown to inhibit enzyme activity. Pancreatic lipase is important in dietary triacylglycerol breakdown; reducing pancreatic lipase activity would reduce triacylglycerol breakdown resulting in lower amounts being absorbed by the body.Lipase activity in the presence of biopolymers was assessed by enzymatic assay using natural and synthetic substrates. Alginate inhibited pancreatic lipase by a maximum of 72.2% (±4.1) with synthetic substrate (DGGR) and 58.0% (±9.7) with natural substrate. High-G alginates from Laminaria hyperborea seaweed inhibited pancreatic lipase to a significantly higher degree than High-M alginates from Lessonia nigrescens, showing that inhibition was related to alginate structure.High-G alginates are effective inhibitors of pancreatic lipase and are used in the food industry at low levels. They could be included at higher levels in foods without altering organoleptic qualities, potentially reduce the uptake of dietary triacylglycerol aiding in weight management.