Inhibitory mechanism and molecular analysis of furoic acid and oxalic acid on lipase.

Lipase hydrolyzes fat to free fatty acid and monoacylglycerol, which can be absorbed. Lipase inhibitors reduce the absorption of fat by intestinal cells. In this paper, we explored a novel treatment for obesity. Lipase was strongly inhibited by furoic acid and oxalic acid (IC50 of 2.12 ± 0.04 and 15.05 ± 0.78 mM, respectively). The inhibition by furoic acid was non-competitive, while that of oxalic acid was competitive (inhibition constant 2.12 ± 0.04 and 10.6 ± 0.17 mM, respectively). Quenching was static. With increasing concentration of inhibitor, the peaks of enzyme fluorescence declined. Docking results suggested that furoic acid and oxalic acid could interact with the amino acid residues of the active center of lipase.