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Inhibitory effect of lignin from Canna edulis Ker residues on trypsin: kinetics and molecular docking studies
Fan Xie1, Wei Zhang2, Shengxiang Gong2
1Shanghai Engineering Research Center of Food Microbiology, School of Medical Instrument and Food Engineering, University of Shanghai for Science and Technology, Shanghai, China.
Background:
Lignin extracted from Canna edulis Ker residues shows a strong inhibitory effect on α-glucosidase and a promoting effect on α-amylase. Protease activity inhibition may play a key role in disease processes, such as metastasis, tumor invasion and bacterial colonization. Hence, in the present study, the inhibitory mechanism of lignin on trypsin was examined, including the interaction type, thermodynamic parameters, structure, reaction site and molecular docking.
Results:
The isolated lignin presented an inhibitory effect on trypsin activity with an IC50 value of 1.35 μmol L-1 . This inhibition was a mixed linear type with a constant Ki of 3.92 μmol L-1 . The lignin could bind with the key amino acid residue Ser195 on the active site of the trypsin molecule to inhibit its activity, and the phenolic hydroxyl group and -OH on the β-O-4 structure of the lignin molecule were the major groups bound with trypsin.
Conclusion:
These results illustrate the inhibitory effects of Canna edulis residue lignin on protease, which helps with respect to understanding the possible application of lignin in the food industry in functional foods. © 2020 Society of Chemical Industry.
