Investigating the impact of ultrasound on the structural, physicochemical, and emulsifying characteristics of Dioscorin: Insights from experimental data and molecular dynamics simulation.

Autor: Gao Q; College of Light Industry, Liaoning University, Shenyang 110036, China; Department of Regional Economic Development, Party School of Liaoning Provincial Party Committee, Shenyang 110161, China., Yang YQ; College of Light Industry, Liaoning University, Shenyang 110036, China., Nie HN; College of Light Industry, Liaoning University, Shenyang 110036, China., Wang BQ; College of Light Industry, Liaoning University, Shenyang 110036, China., Peng X; College of Light Industry, Liaoning University, Shenyang 110036, China., Wang N; College of Light Industry, Liaoning University, Shenyang 110036, China., Li JK; Tianjin Key Laboratory of Postharvest Physiology and Storage of Agricultural Products, National Engineering and Technology Research Center for Preservation of Agricultural Products, Tianjin 300384, China., Rao JJ; Department of Plant Sciences, North Dakota State University, Fargo, ND 58108, USA., Xue YL; College of Light Industry, Liaoning University, Shenyang 110036, China. Electronic address: xueyoulin@lnu.edu.cn.
Jazyk: angličtina
Zdroj: Food chemistry [Food Chem] 2024 Sep 30; Vol. 453, pp. 139581. Date of Electronic Publication: 2024 May 10.
DOI: 10.1016/j.foodchem.2024.139581
Abstrakt: This study investigated the impact of ultrasound treatment on dioscorin, the primary storage protein found in yam tubers. Three key factors, namely ultrasound power, duration, and frequency, were focused on. The research revealed that ultrasound-induced cavitation effects disrupted non-covalent bonds, resulting in a reduction in α-helix and β-sheet contents, decreased thermal stability, and a decrease in the apparent hydrodynamic diameter (Dh) of dioscorin. Additionally, previously hidden amino acid groups within the molecule became exposed on its surface, resulting in increased surface hydrophobicity (Ho) and zeta-potential. Under specific ultrasound conditions (200 W, 25 kHz, 30 min), Dh decreased while Ho increased, facilitating the adsorption of dioscorin molecules onto the oil-water interface. Molecular dynamics (MD) simulations showed that at lower frequencies and pressures, the structural flexibility of dioscorin's main chain atoms increased, leading to more significant fluctuations between amino acid residues. This transformation improved dioscorin's emulsifying properties and its oil-water interface affinity.
Competing Interests: 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.
(Copyright © 2023. Published by Elsevier Ltd.)
Databáze: MEDLINE
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