Investigation on the Effect of Temperature on the Structure of β-Lactoglobulin Based on Molecular Dynamics Simulation

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摘要

In this study, the structural changes of β-lactoglobulin, the core component of whey protein, in different temperatures (303.15 K, 348.15 K, 373.15 K and 423.15 K) were investigated from a molecular perspective employing the molecular dynamics (MD) simulation method. By analyzing structural parameters such as root-mean-square deviation (RMSD), root-mean-square fluctuation (RMSF), radius of gyration (Rg), and solvent-accessible surface area (SASA), the influence of temperature on the structure of β-lactoglobulin was explored. The results show that within the temperature range of 303.15 K to 373.15 K, the molecular conformation of β-lactoglobulin is relatively stable. However, the relative high temperature (e.g., 423.15 K) might significantly affect the structure of β-lactoglobulin, causing significant aggregation and denaturation, which may subsequently affect the gel properties and nutritional functions of the β-lactoglobulin. Furthermore, based on the visualization results, high temperatures might lead to the protein denaturation.

文献引用

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