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Characterization of the aggregation behavior of sea bass (Lateolabrax japonicus) myofibrillar proteins mediated by different ionic strengths: Protein structures, gel properties, and emulsion stabilities

文献类型： 外文期刊

作者： Wu, Yamei 1 ; Xiang, Huan 1 ; Chen, Shengjun 1 ; Zhao, Yongqiang 1 ; Cai, Qiuxing 2 ; Lin, Wanling 1 ; Wu, Yanyan 1 ; Wang, Yueqi 1 ;

作者机构： 1.Chinese Acad Fishery Sci, South China Sea Fisheries Res Inst, Natl R&D Ctr Aquat Prod Proc, Key Lab Aquat Prod Proc Minist Agr & Rural Affairs, Guangzhou 510300, Peoples R China

2.Beibu Gulf Univ, Guangxi Coll, Qinzhou 535000, Guangxi, Peoples R China

3.Beibu Gulf Univ, Univ Key Lab Dev & High value Utilizat Beibu Gulf, Coll Food Engn, Qinzhou 535000, Guangxi, Peoples R China

4.Jiangsu Ocean Univ, Coinnovat Ctr Jiangsu Marine Bioind Technol, Lianyungang 222005, Peoples R China

5.Ocean Univ China, Coll Food Sci & Engn, Qingdao 266000, Peoples R China

6.Sanya Trop Fisheries Res Inst, Key Lab Efficient Utilizat & Proc Marine Fishery R, Sanya 572018, Peoples R China

关键词： Lateolabrax japonicus; Emulsifying properties; Gelation; Structural properties; Functional properties

期刊名称：LWT-FOOD SCIENCE AND TECHNOLOGY （ 影响因子：6.0； 五年影响因子：6.0 ）

ISSN： 0023-6438

年卷期： 2023 年 189 卷

页码：

收录情况： SCI

摘要： Ionic strength affects the aggregation behavior and function of myofibrillar proteins (MPs). This study investigated changes in the aggregation behavior and function of sea bass MPs under ion induction to determine the mechanism of its impact. The ionic strength increased the solubility of proteins (up to 90% at 0.6 mol/L), facilitated the transition from alpha-helices to beta-sheets and increased the reactive sulfhydryl groups from 3.12 mu mol/g to 3.93 mu mol/g. The unfolding of MPs ultimately changed their functional properties. Scanning electron microscopy images showed that a gel network structure began to form at an ionic strength of 0.4 mol/L. Furthermore, the water holding capacity and cooking yield of the gel increased from 51.40% to 28.97%-69.01% and 46.16%, respectively, with an increasing ionic strength. The distribution of droplets in the field of view was relatively uniform at an ionic strength of 0.6 mol/L with a minimum value of CI (20.66%). However, the droplets aggregated at higher ionic strengths (>0.8 mol/L), which also decreased the emulsification properties and gel properties. It is hoped that these results will broaden the potential applications of myofibrillar proteins in emulsions and provide guidance for the processing of surimi products.

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