Comparative study of binding interactions between different fatty acids and β-lactoglobulin:Impact on conformation and physicochemical properties of the protein

IF 8.5 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Chemistry Pub Date : 2025-03-31 DOI:10.1016/j.foodchem.2025.144116

Hui Yang, Jie Xue, Yinuo Xiao, Endian Guo, Jiayang Wu, Yanli Ji, Chenxi Fan

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Abstract

A comparative study was conducted to investigate the binding mechanisms and interactions between four different lengths of saturated fatty acids (C12:0 to C18:0) and two types of C18 unsaturated fatty acids (C18:1 and C18:2) with β-lactoglobulin (β-Lg). The quenching mechanism for these six fatty acids — lauric acid (LUA), myristic acid (MA), palmitic acid (PAL), stearic acid (SA), oleic acid (OA), and linoleic acid (LA) — with β-Lg were found to be static, and the interactions were predominantly driven by hydrophobic forces. The binding affinity was increased with the increase of carbon chain. While, an increase in the number of CC double bonds resulted in a decreased in binding affinity. The binding of fatty acids interfered with the micro-environment around the tyrosine (Tyr) and tryptophan (Trp) residues in protein, subsequently altering the secondary structures of β-Lg. This study will help to improve our understanding of nutrient interactions in food.

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不同脂肪酸与β-乳球蛋白结合相互作用的比较研究：对蛋白质构象和理化性质的影响

对比研究了四种不同长度的饱和脂肪酸（C12:0 ~ C18:0）和两种C18不饱和脂肪酸（C18:1和C18:2）与β-乳球蛋白（β-Lg）的结合机制和相互作用。结果表明，月桂酸（LUA）、肉豆酱酸（MA）、棕榈酸（PAL）、硬脂酸（SA）、油酸（OA）和亚油酸（LA）等6种脂肪酸与β-Lg的猝灭机制是静态的，且主要由疏水力驱动。结合亲合力随碳链的增加而增加。而随着CC双键数的增加，其结合亲和力降低。脂肪酸的结合干扰了蛋白质中酪氨酸（Tyr）和色氨酸（Trp）残基周围的微环境，随后改变了β-Lg的二级结构。这项研究将有助于提高我们对食物中营养相互作用的理解。

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来源期刊

Food Chemistry 工程技术-食品科技

CiteScore

16.30

自引率

10.20%

发文量

3130

审稿时长

122 days

期刊介绍： Food Chemistry publishes original research papers dealing with the advancement of the chemistry and biochemistry of foods or the analytical methods/ approach used. All papers should focus on the novelty of the research carried out.