Comparative analysis of β-lactoglobulin complexes with different catechins: formation, structure, functionality, and emulsion stability

IF 6 1区农林科学 Q1 FOOD SCIENCE & TECHNOLOGY

LWT - Food Science and Technology Pub Date : 2025-05-05 DOI:10.1016/j.lwt.2025.117881

Tinglan Yuan , Ting Ye , Haitao Guo , Yaoruixi Yang , Gongshuai Song , Danli Wang , Ling Li , Yong Cheng , Jinyan Gong

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引用次数: 0

Abstract

Complexes formed between polyphenols and proteins could be used as a good alternative to improve the phytochemical stability in food matrices. While interactions between tea catechins and milk proteins are prevalent in food systems, the effects of different structures of catechins on these interactions, and the resulting alterations in structural and functional properties of covalent complexes formed remain poorly understood. This study investigated the effect of different catechin structures on covalent interactions with β-lactoglobulin (β-Lg). (+)-Catechin (C), (−)-epicatechin (EC), (−)-epigallocatechin (EGC), (−)-epicatechin gallate (ECG), (−)-gallocatechin gallate (GCG), and (−)-epigallocatechin gallate (EGCG) were covalently bound to β-Lg through the alkaline method. β-Lg-catechin complexes had lower fluorescence intensity, hydrophobicity, α-helix content, free amino groups, and sulfhydryl groups than native β-Lg. Binding to catechins (especially ECG, GCG, and EGCG) significantly enhanced β-Lg antioxidant activity, emulsification activity, and stability. Furthermore, β-Lg-catechin complexes substantially enhance emulsion freeze-thaw, thermal stability, storage stability, and oxidative stability. Galloylated catechins exhibited the greatest graft affinity towards β-Lg, and their complexes demonstrated far superior antioxidant activity and stability than non-galloylated catechins. In conclusion, customized β-Lg-catechin conjugates have considerable potential as carriers in food that can enhance emulsion phytochemical stability.

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不同儿茶素β-乳球蛋白复合物的形成、结构、功能和乳状稳定性的比较分析

多酚和蛋白质之间形成的络合物可以作为一种很好的替代品来提高食物基质中的植物化学稳定性。虽然茶儿茶素和牛奶蛋白之间的相互作用在食物系统中很普遍，但儿茶素的不同结构对这些相互作用的影响，以及由此形成的共价复合物的结构和功能特性的改变，仍然知之甚少。本研究探讨了不同儿茶素结构对其与β-乳球蛋白（β-Lg）共价相互作用的影响。（+）-儿茶素(C)、(−)-表儿茶素（EC）、(−)-没食子儿茶素（EGC）、(−)-没食子儿茶素没食子酸酯（ECG）、(−)-没食子儿茶素没食子酸酯（GCG）和(−)-没食子儿茶素没食子酸酯（EGCG）通过碱性法与β-Lg共价结合。与天然的β-Lg相比，β-Lg-儿茶素配合物具有更低的荧光强度、疏水性、α-螺旋含量、游离氨基和巯基。结合儿茶素（特别是ECG、GCG和EGCG）可显著提高β-Lg的抗氧化活性、乳化活性和稳定性。此外，β- l -儿茶素配合物显著提高乳液的冻融稳定性、热稳定性、储存稳定性和氧化稳定性。没食子酸儿茶素对β-Lg的接枝亲和力最大，其配合物的抗氧化活性和稳定性远优于非没食子酸儿茶素。综上所述，定制的β- l -儿茶素缀合物作为食品中的载体具有很大的潜力，可以提高乳化液的植物化学稳定性。

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来源期刊

LWT - Food Science and Technology 工程技术-食品科技

CiteScore

11.80

自引率

6.70%

发文量

1724

审稿时长

65 days

期刊介绍： LWT - Food Science and Technology is an international journal that publishes innovative papers in the fields of food chemistry, biochemistry, microbiology, technology and nutrition. The work described should be innovative either in the approach or in the methods used. The significance of the results either for the science community or for the food industry must also be specified. Contributions written in English are welcomed in the form of review articles, short reviews, research papers, and research notes. Papers featuring animal trials and cell cultures are outside the scope of the journal and will not be considered for publication.