Change in thermal stability and molecular structure characteristics of whey protein beta-lactoglobulin upon the interaction with levamisole hydrochloride.

The interaction between beta-lactoglobulin (BLG) and anthelmintic compounds including levamisole (LEV) is a matter of great concern as it not only poses potential health and environmental risks but also has significant implications for food processing and production. The mechanisms of LEV-BLG interaction were investigated through spectral and molecular modeling approaches. Fluorescence and UV-Visible investigations indicated the formation of a spontaneous and stable LEV-BLG complex. Structural changes of BLG were revealed by circular dichroism and Fourier transform infrared studies. The thermal stability of BLG increased in the presence of LEV. Molecular docking studies indicated the best mode of LEV-BLG interaction and molecular dynamics simulation confirmed the stability of the LEV-BLG complex. In conclusion, our study sheds light on the potential of BLG to interact with deleterious substances such as anthelmintic agents, thus highlighting the necessity of further research in this field to assure food safety and prevent any health hazards.

Informations de copyright

Copyright © 2023 Elsevier Ltd. All rights reserved.

Déclaration de conflit d'intérêts

Declaration of Competing Interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.