不同酚类化合物对鲤鱼肌原纤维蛋白的交联修饰

IF 5.3 2区 农林科学 Q1 FOOD SCIENCE & TECHNOLOGY Food and Bioprocess Technology Pub Date : 2022-12-06 DOI:10.1007/s11947-022-02958-2
Chong Tan, Qian-Da Xu, Nan Chen, Qiang He, Wei-Cai Zeng
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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。
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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.

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来源期刊
Food and Bioprocess Technology
Food and Bioprocess Technology 农林科学-食品科技
CiteScore
9.50
自引率
19.60%
发文量
200
审稿时长
2.8 months
期刊介绍: Food and Bioprocess Technology provides an effective and timely platform for cutting-edge high quality original papers in the engineering and science of all types of food processing technologies, from the original food supply source to the consumer’s dinner table. It aims to be a leading international journal for the multidisciplinary agri-food research community. The journal focuses especially on experimental or theoretical research findings that have the potential for helping the agri-food industry to improve process efficiency, enhance product quality and, extend shelf-life of fresh and processed agri-food products. The editors present critical reviews on new perspectives to established processes, innovative and emerging technologies, and trends and future research in food and bioproducts processing. The journal also publishes short communications for rapidly disseminating preliminary results, letters to the Editor on recent developments and controversy, and book reviews.
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