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, Qian-Da Xu, Nan Chen, Qiang He, 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, Qian-Da Xu, Nan Chen, Qiang He, 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}
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.
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.