{"title":"作为二硫键形成阻断剂的 N-乙基马来酰亚胺对不同蛋白质-乳液-MP 复合凝胶特性的影响","authors":"Yuyu Xu , Jingjing Yang , Mangang Wu, Shumin Lei, Peipei Yin, Qing Yin, Tianhao Zhu, Qingling Wang, Xinxin Zhao, Duxin Jin, Rui Liu, Qingfeng Ge, Hai Yu","doi":"10.1016/j.fochx.2024.101831","DOIUrl":null,"url":null,"abstract":"<div><p>Three different emulsions of myofibrillar protein (MP), soy protein isolate (SPI) and egg white protein isolate (EPI) were individually mixed with MP sol to form composite gels. N-ethylmaleimide (NEM) was used as a sulfhydryl group blocker to evaluate the effects of sulfhydryl and disulfide bonds on the properties of different protein–emulsion composite gels. The results show that the disulfide bond contents in the MP (SPI, EPI) emulsion composite gel decreased from the initial 2.4 ± 0.1, (2.3 ± 0.2, 1.8 ± 0.4) mol/kg to 0.6 ± 0.1, (0.5 ± 0.3, 0.7 ± 0.1) mol/kg with the NEM content increased. In addition, the microstructure showed that the interfacial protein membrane of the emulsion globules were broken in different degrees, indicating that the interaction between the emulsion and the gel matrix was weakened. Meanwhile, gel strength, water distribution and elastic modulus of the composite gels were reduced with NEM contents increased.</p></div>","PeriodicalId":12334,"journal":{"name":"Food Chemistry: X","volume":"24 ","pages":"Article 101831"},"PeriodicalIF":6.5000,"publicationDate":"2024-09-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590157524007193/pdfft?md5=16f7df07b8dd549dd82a942a85d1b85c&pid=1-s2.0-S2590157524007193-main.pdf","citationCount":"0","resultStr":"{\"title\":\"Effect of N-ethylmaleimide as a blocker of disulfide bonds formation on the properties of different protein-emulsion MP composite gels\",\"authors\":\"Yuyu Xu , Jingjing Yang , Mangang Wu, Shumin Lei, Peipei Yin, Qing Yin, Tianhao Zhu, Qingling Wang, Xinxin Zhao, Duxin Jin, Rui Liu, Qingfeng Ge, Hai Yu\",\"doi\":\"10.1016/j.fochx.2024.101831\",\"DOIUrl\":null,\"url\":null,\"abstract\":\"<div><p>Three different emulsions of myofibrillar protein (MP), soy protein isolate (SPI) and egg white protein isolate (EPI) were individually mixed with MP sol to form composite gels. N-ethylmaleimide (NEM) was used as a sulfhydryl group blocker to evaluate the effects of sulfhydryl and disulfide bonds on the properties of different protein–emulsion composite gels. The results show that the disulfide bond contents in the MP (SPI, EPI) emulsion composite gel decreased from the initial 2.4 ± 0.1, (2.3 ± 0.2, 1.8 ± 0.4) mol/kg to 0.6 ± 0.1, (0.5 ± 0.3, 0.7 ± 0.1) mol/kg with the NEM content increased. In addition, the microstructure showed that the interfacial protein membrane of the emulsion globules were broken in different degrees, indicating that the interaction between the emulsion and the gel matrix was weakened. Meanwhile, gel strength, water distribution and elastic modulus of the composite gels were reduced with NEM contents increased.</p></div>\",\"PeriodicalId\":12334,\"journal\":{\"name\":\"Food Chemistry: X\",\"volume\":\"24 \",\"pages\":\"Article 101831\"},\"PeriodicalIF\":6.5000,\"publicationDate\":\"2024-09-12\",\"publicationTypes\":\"Journal Article\",\"fieldsOfStudy\":null,\"isOpenAccess\":false,\"openAccessPdf\":\"https://www.sciencedirect.com/science/article/pii/S2590157524007193/pdfft?md5=16f7df07b8dd549dd82a942a85d1b85c&pid=1-s2.0-S2590157524007193-main.pdf\",\"citationCount\":\"0\",\"resultStr\":null,\"platform\":\"Semanticscholar\",\"paperid\":null,\"PeriodicalName\":\"Food Chemistry: X\",\"FirstCategoryId\":\"97\",\"ListUrlMain\":\"https://www.sciencedirect.com/science/article/pii/S2590157524007193\",\"RegionNum\":1,\"RegionCategory\":\"农林科学\",\"ArticlePicture\":[],\"TitleCN\":null,\"AbstractTextCN\":null,\"PMCID\":null,\"EPubDate\":\"\",\"PubModel\":\"\",\"JCR\":\"Q1\",\"JCRName\":\"CHEMISTRY, APPLIED\",\"Score\":null,\"Total\":0}","platform":"Semanticscholar","paperid":null,"PeriodicalName":"Food Chemistry: X","FirstCategoryId":"97","ListUrlMain":"https://www.sciencedirect.com/science/article/pii/S2590157524007193","RegionNum":1,"RegionCategory":"农林科学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":null,"EPubDate":"","PubModel":"","JCR":"Q1","JCRName":"CHEMISTRY, APPLIED","Score":null,"Total":0}
Effect of N-ethylmaleimide as a blocker of disulfide bonds formation on the properties of different protein-emulsion MP composite gels
Three different emulsions of myofibrillar protein (MP), soy protein isolate (SPI) and egg white protein isolate (EPI) were individually mixed with MP sol to form composite gels. N-ethylmaleimide (NEM) was used as a sulfhydryl group blocker to evaluate the effects of sulfhydryl and disulfide bonds on the properties of different protein–emulsion composite gels. The results show that the disulfide bond contents in the MP (SPI, EPI) emulsion composite gel decreased from the initial 2.4 ± 0.1, (2.3 ± 0.2, 1.8 ± 0.4) mol/kg to 0.6 ± 0.1, (0.5 ± 0.3, 0.7 ± 0.1) mol/kg with the NEM content increased. In addition, the microstructure showed that the interfacial protein membrane of the emulsion globules were broken in different degrees, indicating that the interaction between the emulsion and the gel matrix was weakened. Meanwhile, gel strength, water distribution and elastic modulus of the composite gels were reduced with NEM contents increased.
期刊介绍：
Food Chemistry: X, one of three Open Access companion journals to Food Chemistry, follows the same aims, scope, and peer-review process. It focuses on papers advancing food and biochemistry or analytical methods, prioritizing research novelty. Manuscript evaluation considers novelty, scientific rigor, field advancement, and reader interest. Excluded are studies on food molecular sciences or disease cure/prevention. Topics include food component chemistry, bioactives, processing effects, additives, contaminants, and analytical methods. The journal welcome Analytical Papers addressing food microbiology, sensory aspects, and more, emphasizing new methods with robust validation and applicability to diverse foods or regions.
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