Kinetics and Molecular Docking Studies of Activating Effect of Canna edulis Ker Residue Lignin on the Activity of Lipase
2021
Xie, Fan | Gong, Shengxiang | Zhang, Wei | Wang, Zhengwu
In a previous study, abundant lignin is found in the residues of Canna edulis (C. edulis) ker and showed a strong inhibitory effect on α‐glucosidase and a promoting effect on α‐amylase. In this study, the interaction kinetics, thermodynamic parameters, secondary structure, reaction site, and molecular docking are analyzed. C. edulis residues lignin present an activity promotion effect on pancreatic lipase (promoted 90% of lipase activity) through hydrogen bonding and hydrophobic interaction. The temperature increase from 298 to 310 K promotes the reaction between lignin and pancreatic lipase. The isolated lignin forms a 1:1 complex with the pancreatic lipase to quench its fluorescence. The presence of lignin changes the β‐turn structure of the pancreatic lipase molecule to influence its activity. Further, the binding site of the lignin molecule on the pancreatic lipase molecule is the phenolic hydroxyl group on the guaiacyl group. The lignin molecule binds closely to the active site of the pancreatic lipase molecule. These results provide new insight into the effect of C. edulis residues lignin on fat metabolism.
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