Stability and molecular interactions in cold-induced hazelnut protein-chlorogenic acid gel

IF 3.5 2区农林科学 Q1 AGRICULTURE, MULTIDISCIPLINARY Journal of the Science of Food and Agriculture Pub Date : 2025-03-09 DOI:10.1002/jsfa.14192

Xuemei Wang, Jiarong Wang, Ligang Zhang, Wenqi Wang, Lai Jiang, Yuhua Yang, Yuhong Zhao

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Abstract

BACKGROUND

Phenols have been demonstrated to enhance protein gelation but their stability is often compromised in heat-induced gels. This has prompted the development of cold-induced gels. The objective of this study was to enhance the gel properties of hazelnut isolate protein (HPI) through the incorporation of transglutaminase (TGase), glucono-δ-lactone (GDL), and chlorogenic acid (CA). It also aimed to investigate the biofunctional role of CA.

RESULTS

In comparison with heat-induced gels, cold-induced gels exhibited a higher prevalence of disulfide (25.51%) and hydrogen bonds (35.88%). Transglutaminyl transferase also facilitated the formation of ε-(γ-glutamyl)lysine interpeptide bonds, enhancing the gel properties of cold-induced gels significantly. The gel strength increased by about 3.9 times, the water-holding capacity increased by approximately 2.8 times, and storage modulus increased by about 2.5 times. The resulting gels were more compact and stable, which reduced protein digestibility. It was observed that the interaction between HPI and CA in cold-induced gels was significantly enhanced, thereby enabling CA to improve the gelation capability of HPI more effectively, particularly in TGase-induced formulations. Chlorogenic acid displayed strong thermal stability in cold-induced gels; findings from in vitro digestion simulation also indicated that the CA present in HPI exhibited effective sustained release properties within the gastrointestinal tract.

CONCLUSION

The present study offers novel approaches to the utilization of HPI in food applications and presents innovative strategies for developing HPI gel foods characterized by enhanced gel properties and rich active compound content. © 2025 Society of Chemical Industry.

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冷诱导榛子蛋白-绿原酸凝胶的稳定性及分子相互作用。

背景：苯酚已被证明可以增强蛋白质凝胶，但它们的稳定性在热诱导凝胶中经常受到损害。这促进了冷诱导凝胶的发展。本研究的目的是通过谷氨酰胺转酶（TGase）、葡萄糖-δ-内酯（GDL）和绿原酸（CA）的掺入来提高榛子分离蛋白（HPI）的凝胶性能。结果：与热诱导凝胶相比，冷诱导凝胶具有更高的二硫化物（25.51%）和氢键（35.88%）。转谷氨酰基转移酶还促进ε-（γ-谷氨酰基）赖氨酸肽间键的形成，显著提高冷诱导凝胶的凝胶性能。凝胶强度提高约3.9倍，持水量提高约2.8倍，储存模量提高约2.5倍。所得凝胶更加致密和稳定，从而降低了蛋白质的消化率。观察到冷诱导凝胶中HPI和CA之间的相互作用显著增强，从而使CA能够更有效地提高HPI的凝胶化能力，特别是在tgase诱导的配方中。绿原酸在冷诱导凝胶中表现出较强的热稳定性；体外消化模拟的结果也表明，HPI中的CA在胃肠道内具有有效的缓释特性。结论：本研究为HPI在食品中的应用提供了新的途径，并提出了开发具有增强凝胶性能和丰富活性化合物含量的HPI凝胶食品的创新策略。©2025化学工业协会。

本文章由计算机程序翻译，如有差异，请以英文原文为准。

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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.