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Structural properties and emulsification of myofibrillar proteins from hairtail (Trichiurus haumela) at different salt ions

文献类型： 外文期刊

作者： Huang, Xianglan 1 ; Cui, Yaqing 1 ; Shi, Linfan 1 ; Yang, Shen 1 ; Qiu, Xujian 1 ; Hao, Gengxin 1 ; Zhao, Yongqiang 3 ; Liu, Shuji 4 ; Liu, Zhiyu 4 ; Weng, Wuyin 1 ; Ren, Zhongyang 1 ;

作者机构： 1.Jimei Univ, Coll Ocean Food & Biol Engn, Xiamen 361021, Peoples R China

2.Minist Educ, Engn Res Ctr Modern Technol Eel Ind, Xiamen, Peoples R China

3.Chinese Acad Fishery Sci, Natl R&D Ctr Aquat Prod Proc, Minist Agr & Rural Affairs Peoples Republ China, Key Lab Aquat Prod Proc,South China Fisheries Res, Guangzhou 510300, Peoples R China

4.Fujian Collaborat Innovat Ctr Exploitat & Utilizat, Fisheries Res Inst Fujian, Key Lab Cultivat & High value Utilizat Marine Orga, Xiamen 361013, Peoples R China

关键词： Salt ions; Trichiurus haumela; Myofibrillar proteins

期刊名称：INTERNATIONAL JOURNAL OF BIOLOGICAL MACROMOLECULES （ 影响因子：8.2； 五年影响因子：7.8 ）

ISSN： 0141-8130

年卷期： 2023 年 253 卷

页码：

收录情况： SCI

摘要： The structural properties and emulsification of myofibrillar proteins (MPs) are susceptibly affected by salt ions. The effect of different salt ions on the structural properties and emulsification of MPs from hairtail (Trichiurus haumela) remains unclear. Hairtail MPs were analyzed under different ion treatments of Na+, K+, Ca2+ and Mg2+. MPs at K+ and Na+ treatment showed a similar trend on salt effect due to the unfolding of proteins under salt ions. However, the excessive electrostatic effect of divalent ions could enhance protein aggregation, especially at Ca2+ and Mg2+. The beta-sheet of MPs at different salt ions interconverted with alpha-helix and random coil at ionic strengths from 0.1 mol/L to 1.0 mol/L. The surface hydrophobicity and active sulfhydryl content of MPs increased with the improvement of ionic strengths at 0-0.8 mol/L. Under Ca2+ and Mg2+ treatments, the turbidity of MPs was low compared to that under the treatment of Na+ and K+. Additionally, the emulsification of hairtail MPs treated with different ions was improved at an ionic strength of 0.6 mol/L. This study can contribute to using salts in constructing fish protein-based emulsions for manufacturing emulsified surimi products and promoting the development and utilization of hairtail proteins.

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