Dual-protein system composed of soy protein and β-lactoglobulin: effect of transglutaminase-mediated crosslinking on its allergenicity and conformation.

IF 3.3 2区农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY Journal of the Science of Food and Agriculture Pub Date : 2025-01-15 DOI:10.1002/jsfa.14125

Guangliang Xing, Jia Liu, Ruyi Tang, Tianran Hui

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Abstract

Background: The escalating global prevalence of food allergies has intensified the need for hypoallergenic food products. Transglutaminase (TGase)-mediated crosslinking has garnered significant attention for its potential to reduce the allergenicity of food proteins. This study aimed to investigate the effects of TGase crosslinking on the potential allergenicity and conformational changes in a dual-protein system composed of β-lactoglobulin (β-LG) and soy protein isolate (SPI) at varying mass ratios (10:0, 7:3, 5:5, 3:7 and 0:10 (w/w)).

Results: TGase preferentially crosslinked the 7S and 11S subunits of soy protein, rather than β-LG. Crosslinking treatment reduced the allergenic potential of both soy protein and β-LG, with the degree of reduction depending on the protein ratio. The β-LG5:SPI5 and β-LG7:SPI3 mixtures showed the most significant reduction in antibody reactivity towards soy protein and β-LG, respectively. Additionally, TGase-mediated crosslinking significantly reduced the binding capacity of all dual-protein samples to serum immunoglobulin E from allergic patients, compared to the control group (P < 0.05). The allergenicity reduction was accompanied by structural modifications, including a decrease in β-sheet content, an increase in β-turn and random coil structures, enhanced ultraviolet absorption and intrinsic fluorescence, reduced free sulfhydryl levels and altered intermolecular forces. These changes suggest that TGase-induced crosslinking may disrupt or mask allergenic epitopes, thus lowering allergenicity.

Conclusion: TGase crosslinking effectively reduced the allergenic potential of the dual-protein system by inducing structural changes. These findings underscore the potential of TGase in developing hypoallergenic dual-protein food products and provide a scientific foundation for future research and application in the food industry. © 2025 Society of Chemical Industry.

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大豆蛋白与β-乳球蛋白组成的双蛋白体系：转谷氨酰胺酶介导的交联对其致敏性和构象的影响。

背景：食物过敏的全球流行率不断上升，加强了对低过敏性食品的需求。转谷氨酰胺酶（TGase）介导的交联因其降低食物蛋白质致敏性的潜力而引起了极大的关注。本研究旨在探讨TGase交联对β-乳球蛋白（β-LG）和大豆分离蛋白（SPI）在不同质量比（10:0,7:3,5:5,3:7和0:10 (w/w)）组成的双蛋白体系的潜在致敏性和构象变化的影响。结果：TGase优先交联大豆蛋白的7S和11S亚基，而不是β-LG。交联处理降低了大豆蛋白和β-LG的致敏潜力，其降低程度取决于蛋白质的比例。β-LG5:SPI5和β-LG7:SPI3分别对大豆蛋白和β-LG的抗体反应性降低最为显著。此外，与对照组相比，TGase介导的交联显著降低了所有双蛋白样品对过敏患者血清免疫球蛋白E的结合能力(P)。结论：TGase交联通过诱导结构变化有效降低了双蛋白系统的致敏潜力。这些发现强调了TGase在开发低过敏性双蛋白食品中的潜力，为今后在食品工业中的研究和应用提供了科学基础。©2025化学工业协会。

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来源期刊

Journal of the Science of Food and Agriculture 工程技术-农业综合

CiteScore

8.10

自引率

4.90%

发文量

634

审稿时长

3.1 months

期刊介绍： The Journal of the Science of Food and Agriculture publishes peer-reviewed original research, reviews, mini-reviews, perspectives and spotlights in these areas, with particular emphasis on interdisciplinary studies at the agriculture/ food interface. Published for SCI by John Wiley & Sons Ltd. SCI (Society of Chemical Industry) is a unique international forum where science meets business on independent, impartial ground. Anyone can join and current Members include consumers, business people, environmentalists, industrialists, farmers, and researchers. The Society offers a chance to share information between sectors as diverse as food and agriculture, pharmaceuticals, biotechnology, materials, chemicals, environmental science and safety. As well as organising educational events, SCI awards a number of prestigious honours and scholarships each year, publishes peer-reviewed journals, and provides Members with news from their sectors in the respected magazine, Chemistry & Industry . Originally established in London in 1881 and in New York in 1894, SCI is a registered charity with Members in over 70 countries.