不同酚类化合物对鲤鱼肌原纤维蛋白的交联修饰

IF 8.3 2区 材料科学 Q1 MATERIALS SCIENCE, MULTIDISCIPLINARY
Chong Tan, Qian-Da Xu, Nan Chen, Qiang He, Wei-Cai Zeng
{"title":"不同酚类化合物对鲤鱼肌原纤维蛋白的交联修饰","authors":"Chong Tan,&nbsp;Qian-Da Xu,&nbsp;Nan Chen,&nbsp;Qiang He,&nbsp;Wei-Cai Zeng","doi":"10.1007/s11947-022-02958-2","DOIUrl":null,"url":null,"abstract":"<div><p>Common carp (<i>Cyprinus carpio</i>) is an important and popular fish in Asia, but due to the short length and low cross-linking degree, fish myofibrillar protein is easy to break and deteriorate, which shows some negative impacts on the quality of fish meat. In present study, the cross-linking modifications of different phenolic compounds on myofibrillar protein of common carp were investigated, and their action mechanism was further explored. Phenolic compounds including gallic acid (GA), chlorogenic acid (CA), epigallocatechin (EGC), epigallocatechin gallate (EGCG), and tannic acid (TA) could increase the average particle size of myofibrillar protein from 61 to 65, 102, 97, 118, and 127 μm individually, and the solubility decreased by 7.7, 16.1, 13.6, 21.1, and 19.2%. The increased particle size and decreased solubility could promote the aggregation of myofibrillar protein, which indicated phenolic compounds exhibited the cross-linking effects on fish myofibrillar protein. Then, hydrogen bonds were found to be the main molecular force for the cross-linking effects. Meanwhile, the contents of sulfhydryl decreased by 13.5, 18.9, 29.7, 35.1, and 40.5%, and the disulfide bonds in myofibrillar protein decreased by 12.9, 11.9, 14.4, 22.3, and 26.7% when treated with GA, CA, EGC, EGCG, and TA, respectively. In addition, the secondary and tertiary structures of myofibrillar protein were both changed with phenolic compounds, which indicated that its spatial structure was changed to be loose. Furthermore, the thermal stability and gel properties of myofibrillar protein were improved with phenolic compounds. Different phenolic compounds showed various cross-linking effects on fish myofibrillar protein, which was due to the content and reactivity of hydroxyl groups in phenolic compounds. All results suggested that phenolic compounds had potential value to modify the length and cross-linking degree of fish myofibrillar protein, so as to improve the quality of fish meat in the food industry.</p></div>","PeriodicalId":5,"journal":{"name":"ACS Applied Materials & Interfaces","volume":null,"pages":null},"PeriodicalIF":8.3000,"publicationDate":"2022-12-06","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":"4","resultStr":"{\"title\":\"Cross-Linking Modifications of Different Phenolic Compounds on Myofibrillar Protein of Common Carp\",\"authors\":\"Chong Tan,&nbsp;Qian-Da Xu,&nbsp;Nan Chen,&nbsp;Qiang He,&nbsp;Wei-Cai Zeng\",\"doi\":\"10.1007/s11947-022-02958-2\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Common carp (<i>Cyprinus carpio</i>) is an important and popular fish in Asia, but due to the short length and low cross-linking degree, fish myofibrillar protein is easy to break and deteriorate, which shows some negative impacts on the quality of fish meat. In present study, the cross-linking modifications of different phenolic compounds on myofibrillar protein of common carp were investigated, and their action mechanism was further explored. Phenolic compounds including gallic acid (GA), chlorogenic acid (CA), epigallocatechin (EGC), epigallocatechin gallate (EGCG), and tannic acid (TA) could increase the average particle size of myofibrillar protein from 61 to 65, 102, 97, 118, and 127 μm individually, and the solubility decreased by 7.7, 16.1, 13.6, 21.1, and 19.2%. The increased particle size and decreased solubility could promote the aggregation of myofibrillar protein, which indicated phenolic compounds exhibited the cross-linking effects on fish myofibrillar protein. Then, hydrogen bonds were found to be the main molecular force for the cross-linking effects. Meanwhile, the contents of sulfhydryl decreased by 13.5, 18.9, 29.7, 35.1, and 40.5%, and the disulfide bonds in myofibrillar protein decreased by 12.9, 11.9, 14.4, 22.3, and 26.7% when treated with GA, CA, EGC, EGCG, and TA, respectively. In addition, the secondary and tertiary structures of myofibrillar protein were both changed with phenolic compounds, which indicated that its spatial structure was changed to be loose. Furthermore, the thermal stability and gel properties of myofibrillar protein were improved with phenolic compounds. Different phenolic compounds showed various cross-linking effects on fish myofibrillar protein, which was due to the content and reactivity of hydroxyl groups in phenolic compounds. All results suggested that phenolic compounds had potential value to modify the length and cross-linking degree of fish myofibrillar protein, so as to improve the quality of fish meat in the food industry.</p></div>\",\"PeriodicalId\":5,\"journal\":{\"name\":\"ACS Applied Materials & Interfaces\",\"volume\":null,\"pages\":null},\"PeriodicalIF\":8.3000,\"publicationDate\":\"2022-12-06\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"\",\"citationCount\":\"4\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"ACS Applied Materials & Interfaces\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://link.springer.com/article/10.1007/s11947-022-02958-2\",\"RegionNum\":2,\"RegionCategory\":\"材料科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"MATERIALS SCIENCE, MULTIDISCIPLINARY\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"ACS Applied Materials & Interfaces","FirstCategoryId":"97","ListUrlMain":"https://link.springer.com/article/10.1007/s11947-022-02958-2","RegionNum":2,"RegionCategory":"材料科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"MATERIALS SCIENCE, MULTIDISCIPLINARY","Score":null,"Total":0}
引用次数: 4

摘要

鲤鱼(Cyprinus carpio)是亚洲重要的流行鱼类,但由于其体长短,交联度低,鱼肌原纤维蛋白容易断裂变质,对鱼肉品质有一定的负面影响。本研究研究了不同酚类化合物对鲤鱼肌原纤维蛋白的交联修饰,并进一步探讨了其作用机制。未食子酸(GA)、绿原酸(CA)、没食子儿茶素(EGC)、没食子儿茶素没食子酸酯(EGCG)和单宁酸(TA)等酚类化合物可使肌原纤维蛋白的平均粒径分别从61 μm增大到65 μm、102 μm、97 μm、118 μm和127 μm,溶解度分别降低7.7、16.1%、13.6%、21.1和19.2%。增大的粒径和降低的溶解度可以促进肌原纤维蛋白的聚集,说明酚类化合物对鱼类肌原纤维蛋白具有交联作用。然后,发现氢键是交联效应的主要分子力。GA、CA、EGC、EGCG和TA处理后,肌纤维蛋白中巯基含量分别降低了13.5、18.9、29.7、35.1和40.5%,二硫键含量分别降低了12.9、11.9、14.4、22.3和26.7%。此外,肌纤维蛋白的二级和三级结构都被酚类化合物改变,表明其空间结构变得松散。此外,酚类化合物还改善了肌原纤维蛋白的热稳定性和凝胶性能。不同酚类化合物对鱼肌原纤维蛋白表现出不同的交联作用,这与酚类化合物中羟基的含量和反应活性有关。这些结果表明,酚类化合物在改变鱼类肌原纤维蛋白的长度和交联度,从而改善食品工业中鱼肉的品质方面具有潜在的价值。
本文章由计算机程序翻译,如有差异,请以英文原文为准。

Cross-Linking Modifications of Different Phenolic Compounds on Myofibrillar Protein of Common Carp

Cross-Linking Modifications of Different Phenolic Compounds on Myofibrillar Protein of Common Carp

Common carp (Cyprinus carpio) is an important and popular fish in Asia, but due to the short length and low cross-linking degree, fish myofibrillar protein is easy to break and deteriorate, which shows some negative impacts on the quality of fish meat. In present study, the cross-linking modifications of different phenolic compounds on myofibrillar protein of common carp were investigated, and their action mechanism was further explored. Phenolic compounds including gallic acid (GA), chlorogenic acid (CA), epigallocatechin (EGC), epigallocatechin gallate (EGCG), and tannic acid (TA) could increase the average particle size of myofibrillar protein from 61 to 65, 102, 97, 118, and 127 μm individually, and the solubility decreased by 7.7, 16.1, 13.6, 21.1, and 19.2%. The increased particle size and decreased solubility could promote the aggregation of myofibrillar protein, which indicated phenolic compounds exhibited the cross-linking effects on fish myofibrillar protein. Then, hydrogen bonds were found to be the main molecular force for the cross-linking effects. Meanwhile, the contents of sulfhydryl decreased by 13.5, 18.9, 29.7, 35.1, and 40.5%, and the disulfide bonds in myofibrillar protein decreased by 12.9, 11.9, 14.4, 22.3, and 26.7% when treated with GA, CA, EGC, EGCG, and TA, respectively. In addition, the secondary and tertiary structures of myofibrillar protein were both changed with phenolic compounds, which indicated that its spatial structure was changed to be loose. Furthermore, the thermal stability and gel properties of myofibrillar protein were improved with phenolic compounds. Different phenolic compounds showed various cross-linking effects on fish myofibrillar protein, which was due to the content and reactivity of hydroxyl groups in phenolic compounds. All results suggested that phenolic compounds had potential value to modify the length and cross-linking degree of fish myofibrillar protein, so as to improve the quality of fish meat in the food industry.

求助全文
通过发布文献求助,成功后即可免费获取论文全文。 去求助
来源期刊
ACS Applied Materials & Interfaces
ACS Applied Materials & Interfaces 工程技术-材料科学:综合
CiteScore
16.00
自引率
6.30%
发文量
4978
审稿时长
1.8 months
期刊介绍: ACS Applied Materials & Interfaces is a leading interdisciplinary journal that brings together chemists, engineers, physicists, and biologists to explore the development and utilization of newly-discovered materials and interfacial processes for specific applications. Our journal has experienced remarkable growth since its establishment in 2009, both in terms of the number of articles published and the impact of the research showcased. We are proud to foster a truly global community, with the majority of published articles originating from outside the United States, reflecting the rapid growth of applied research worldwide.
×
引用
GB/T 7714-2015
复制
MLA
复制
APA
复制
导出至
BibTeX EndNote RefMan NoteFirst NoteExpress
×
提示
您的信息不完整,为了账户安全,请先补充。
现在去补充
×
提示
您因"违规操作"
具体请查看互助需知
我知道了
×
提示
确定
请完成安全验证×
copy
已复制链接
快去分享给好友吧!
我知道了
右上角分享
点击右上角分享
0
联系我们:info@booksci.cn Book学术提供免费学术资源搜索服务,方便国内外学者检索中英文文献。致力于提供最便捷和优质的服务体验。 Copyright © 2023 布克学术 All rights reserved.
京ICP备2023020795号-1
ghs 京公网安备 11010802042870号
Book学术文献互助
Book学术文献互助群
群 号:481959085
Book学术官方微信