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Unlocking sesame protein potential: Production and functional characteristics of sesame protein via cold plasma-assisted extraction

文献类型： 外文期刊

作者： Hou, Ying 1 ; Wang, Xuan 1 ; Zheng, Xuechao 1 ; Hao, Jianxiong 1 ; Peng, Yu 2 ; Zhao, Dandan 1 ;

作者机构： 1.Hebei Univ Sci & Technol, Coll Food Sci & Biol, Shijiazhuang 050018, Peoples R China

2.Beijing Acad Agr & Forestry Sci, Inst Agrifood Proc & Nutr, 50 Zhanghua Rd, Beijing 100097, Peoples R China

关键词： Sesame protein fractions; Dielectric barrier discharge atmospheric cold plasma; Protein extraction; Protein functional properties

期刊名称：FOOD HYDROCOLLOIDS （ 影响因子：12.4； 五年影响因子：13.3 ）

ISSN： 0268-005X

年卷期： 2025 年 167 卷

页码：

收录情况： SCI

摘要： Sesame seeds are among the oldest oilseed crops in the food industry; however, the by-product of sesame oil production, known as sesame cake, has limited applications. Enhancing protein extraction from sesame cake is crucial for fully exploiting the potential of sesame proteins. This research studied the effects of dielectric barrier discharge atmospheric cold plasma (DBD-ACP) treatment at different voltages on the extraction efficacy, structural characteristics, and functional properties of sesame protein fractions (SPFs). Notably, treatment at DBD-ACP 45 V resulted in a maximum extraction rate of approximately 16.92 %, whereas the highest protein content, approximately 85.40 %, was attained at 35 V. At this voltage, structural analysis revealed increased porosity and significant structural refolding of SPFs, accompanied by reduced surface hydrophobicity and sulfhydryl contents. Additionally, treatment at 35 V led to a decrease in average particle size and an increase in intermolecular electrostatic repulsion among SPFs. While solubility improved under these conditions, there were concomitant reductions in oil-holding capacity, emulsifying properties, and foaming ability. These findings indicated that moderate DBD-ACP treatment enhanced the interaction between protein particles and water molecules by promoting structural refolding that buries hydrophobic groups within the core of the protein structure. In conclusion, this study provided novel insights into how varying intensities of DBD-ACP treatment influence SPF extraction efficiency, structure, and functional properties.

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