文献类型： 外文期刊

作者： Qi, Jun ¹ ; Li, Yu-cong ¹ ; Yan, Hui-min ¹ ; Zeng, Li-ting ¹ ; Lv, Ao-jing ¹ ; Dong, Rui-ling ¹ ; Li, Xue-qing ¹ ; Lin, Zhou ¹ ; Shao, Le-le ¹ ; Zhang, Lang ¹ ; Duan, Guo-qing ² ; Zhang, Chun-hui ³ ; Xiong, Guo-yuan ⁴ ;

作者机构： 1.Anhui Agr Univ, Anhui Engn Res Ctr High Value Utilizat Characteris, Key Lab Jianghuai Agr Prod Fine Proc & Resource Ut, Minist Agr & Rural Affairs,Sch Food & Nutr, Hefei 230036, Peoples R China

2.Anhui Acad Agr Sci, Inst Fisheries Sci, Hefei 230031, Peoples R China

3.Chinese Acad Agr Sci, Inst Food Sci & Technol, Beijing 100193, Peoples R China

4.Anhui Sci & Technol Univ, Sch Food Engn, Chuzhou 233100, Peoples R China

关键词： Gelatin; Low-energy emulsification; Thermal stability of emulsion; Secondary structure; Surface tension

期刊名称：FOOD RESEARCH INTERNATIONAL （ 影响因子：8.0； 五年影响因子：8.5 ）

ISSN： 0963-9969

年卷期： 2025 年 218 卷

页码：

收录情况： SCI

摘要： The impact of low-energy stirring temperatures (30 degrees C, 50 degrees C, 70 degrees C, 90 degrees C) on the stability of gelatin emulsions was investigated when stirring with a magnetic stirrer at 1600 rpm for 3.5 hat an arginine (Arg) concentration of 1.2 % (w/v). The results indicated that as the stirring temperature increased, the appearance of the emulsions became more transparent and clearer, and their particle sizes and the absolute zeta potential values decreased significantly (P < 0.05). Moreover, the addition of Arg significantly enhanced the stability of the emulsions, with those prepared at 30 degrees C exhibiting the highest stability. These findings could be attributed to the fact that under the stirring temperature of 30 degrees C and in the presence of Arg, the depolymerization of gelatin increased, leading to a significant increase in the hydrophobic beta-sheet structures (P < 0.05), which in turn resulted in a significant increase in the exposure of hydrophobic amino acids and negatively charged residues on the gelatin surface (P < 0.05). Ultimately, the stability of gelatin emulsions (phi = 5 %), prepared via this one-step stirring method, was significantly improved. The information gathered could provide guidance on preparing protein-stabilized emulsions with low oil phase volume fractions using low-energy emulsification techniques.