Phenolic acids are known to bind with and inhibit digestive enzymes in vitro. In particular, their action on pancreatic lipase at physiological pH is not well understood. Therefore, this study evaluated the inhibitory potential of phenolic acids from potato (caffeic acid CA, chlorogenic acid ChA, p-coumaric acid pCA, ferulic acid FA) towards lipase. All the phenolic acids were weak inhibitors of lipase and ChA was the weakest of all. Binding energy between phenolic acids and lipase obtained by molecular docking and solubility of the phenolic acids seemed to correlate well with inhibition data obtained at pH 6.9. Additionally, phenolic acids can form complexes with polysaccharides. In food such as potato, the presence of significant amount starch could therefore prevent phenolic acids to modulate pancreatic lipase. Consequently, we evaluated the effect of potato starch (up to 1 % w/w) on the ability to inhibit the activity of pancreatic lipase. The results showed that the presence of starch had essentially no effect on the inhibition of lipase by FA and pCA, that it led to decreased CA's inhibitory activity and to increased ChA's inhibitory activity. These contradictory observations could be explained by starch-phenolic acid complexation although they may be modulated by physical effects due to starch (microphase separation, decreased diffusion), and potentially amplified by the limited solubility of the phenolic acids.