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

IF 3.3 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

{"title":"Stability and molecular interactions in cold-induced hazelnut protein-chlorogenic acid gel.","authors":"Xuemei Wang, Jiarong Wang, Ligang Zhang, Wenqi Wang, Lai Jiang, Yuhua Yang, Yuhong Zhao","doi":"10.1002/jsfa.14192","DOIUrl":null,"url":null,"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.","PeriodicalId":17725,"journal":{"name":"Journal of the Science of Food and Agriculture","volume":" ","pages":""},"PeriodicalIF":3.3000,"publicationDate":"2025-03-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"0","resultStr":null,"platform":"Semanticscholar","paperid":null,"PeriodicalName":"Journal of the Science of Food and Agriculture","FirstCategoryId":"97","ListUrlMain":"https://doi.org/10.1002/jsfa.14192","RegionNum":2,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"AGRICULTURE, MULTIDISCIPLINARY","Score":null,"Total":0}

引用次数: 0

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.

查看原文

微信好友朋友圈 QQ好友复制链接

本刊更多论文

求助全文

约1分钟内获得全文去求助

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.