Li_2025_Food.Chem_497_147031

The screening of enzyme inhibitors faces challenges such as low efficiency. In this study, a novel online HPLC-FLD/pancreatic lipase recognition system was developed for the first time. The optimal operating parameters were established as a flow rate of 1 mL/min, with excitation and emission wavelengths for pancreatic lipase set at 221 nm and 303 nm, respectively. The effectiveness of this system was validated using orlistat. Subsequently, this system was applied to Lycium ruthenicum, where two petunidin-based anthocyanins pancreatic lipase inhibitors were efficiently isolated using medium-pressure liquid chromatography. Molecular docking elucidated that compounds 1 and 2 interact with the serine residue of pancreatic lipase, exhibiting binding energies of -13.12 kcal/mol and -12.22 kcal/mol, respectively. Enzymatic assays showed that the half-maximal inhibitory concentrations of compounds 1 and 2 were 9.67 microM and 147.37 microM, respectively. These docking and inhibition results confirm the system for efficiently discovering pancreatic lipase inhibitors.