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- W3088390848 abstract "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." @default.
- W3088390848 created "2020-10-01" @default.
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- W3088390848 date "2020-10-07" @default.
- W3088390848 modified "2023-09-23" @default.
- W3088390848 title "Inhibitory effect of lignin from <scp> <i>Canna edulis</i> </scp> Ker residues on trypsin: kinetics and molecular docking studies" @default.
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- W3088390848 doi "https://doi.org/10.1002/jsfa.10831" @default.
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