Stability of pancreatic lipase inhibitory activity of peptide derived from crucian

The effects of different conditions on stability of pancreatic lipase inhibitory activity of peptide hydrolyzed by crucian protein were studied.It was shown that the pancreatic lipase inhibitory peptide remained at high active stability below 60 ℃,under neutral condition.Based on evaluation of pancreatic lipase inhibitory activity,freeze drying was better than spray drying.Na+,Mg2+promoted the pancreatic lipase inhibitory activity,while Zn2+and Mn2+inhibited the pancreatic lipase inhibitory activity.Peptide hydrolyzed by pepsin exhibited lower pancreatic lipase inhibitory activity,but the inhibitory activity was stable after further hydrolyzed by trypsin.