Revealing the non-enzymatic covalent interaction between neo−/crypto-chlorogenic acid and beta-lactoglobulin under nonthermal process and potential delivery capability

IF 8.5 1区农林科学 Q1 CHEMISTRY, APPLIED

Food Chemistry Pub Date : 2025-02-10 DOI:10.1016/j.foodchem.2025.143325

Fang Li, Haina Hou, Tian Zhao, Gongshuai Song, Danli Wang, Tinglan Yuan, Ling Li, Jinyan Gong

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引用次数: 0

Abstract

Several studies have shown that the protein-chlorogenic acid covalent complex has better function and stability than the non-covalent. The degree of binding between the proteins and chlorogenic acids (CQA) can be enhanced by the ultrasound process. Herein, the effects of ultrasound-assisted non-enzymatic covalent binding (the free radical induction (Vc)-ultrasound combination and the alkali treatment (Alkali)-ultrasound combination) of two chlorogenic acids (neochlorogenic acid (3-CQA), cryptochlorogenic acid (4-CQA)) and β-lactoglobulin (β-LG) on proteins structure and properties were investigated. Results showed that ULG-Alkali-4CQA exhibited a 5.1 % reduction in α-helices, a 6.8 % increase in random curl and proteins structures becoming loose and disordered. The hydrophilicity and thermal stability of β-LG were effectively enhanced by the addition of 4-CQA and the effect of alkali treatment-ultrasound combination. Curcumin (CUR) and lycopene (LYC) were successfully delivered by the covalent complexes as delivery vehicles. The encapsulation efficiencies of the ULG-Vc/Alkali-4CQA + CUR and ULG-Vc/Alkali-4CQA + LYC complexes were 82.81 %, 84.16 %, 89.56 % and 90.51 %, respectively. The stabilities of CUR and LYC in the ULG-Vc/Alkali-4CQA + CUR/LYC ternary complexes were superior to those of all the measured complexes delivery systems. The study hopes to establish a theoretical foundation and serve as a reference for the advancement of a highly stable food-grade delivery system.

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揭示新−/隐绿原酸与β -乳球蛋白在非热过程下的非酶共价相互作用及其潜在的递送能力

多项研究表明，蛋白质-绿原酸共价复合物比非共价复合物具有更好的功能和稳定性。超声处理可提高蛋白质与绿原酸（CQA）的结合程度。本文研究了超声辅助下两种绿原酸(新绿原酸（3-CQA）、隐绿原酸（4-CQA）和β-乳球蛋白（β-LG）的非酶促共价结合(自由基诱导（Vc)-超声联合和碱处理（碱）-超声联合）对蛋白质结构和性质的影响。结果表明，ULG-Alkali-4CQA的α-螺旋减少了5.1% %，随机旋度增加了6.8% %，蛋白质结构变得松散和无序。4-CQA的加入和碱处理-超声联合作用可有效提高β-LG的亲水性和热稳定性。姜黄素（Curcumin， CUR）和番茄红素（LYC， LYC）以共价配合物为载体成功递送。ULG-Vc/碱- 4cqa + CUR和ULG-Vc/碱- 4cqa + LYC配合物的包封效率分别为82.81 %、84.16 %、89.56 %和90.51 %。ULG-Vc/Alkali-4CQA + 中CUR/LYC三元配合物的稳定性优于所有被测配合物递送体系。本研究希望为构建高度稳定的食品级外卖系统奠定理论基础，并提供参考。

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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.