文献类型： 外文期刊

作者： Yan, Hui-min ¹ ; Song, Yu ² ; Yao, Xiu-ning ¹ ; Zhang, Wen-wen ³ ; Xu, Ying ⁴ ; Li, Xue-qing ¹ ; Xu, Yu-qin ¹ ; Fang, Shun ¹ ; Qi, Jun ¹ ; Xiong, Guo-yuan ¹ ; Li, Chao ⁶ ; Jia, Jing-min ⁷ ; Hu, Yong ⁸ ;

作者机构： 1.Anhui Agr Univ, Coll Tea & Food Sci & Technol, Key Lab Jianghuai Agr Prod Fine Proc & Resource Ut, Anhui Engn Lab Agroprod Proc,Minist Agr & Rural Af, Hefei 230036, Peoples R China

2.Anhui Acad Agr Sci, Agr Prod Proc Res Inst, Hefei 230031, Peoples R China

3.Anhui Qingsong Food Co Ltd, Hefei 230088, Peoples R China

4.Chinese Acad Agr Sci, Key Lab Agroprod Proc, Minist Agr & Rural Affairs, Inst Food Sci & Technol, Beijing 100193, Peoples R China

5.Dalian Polytech Univ, Natl Engn Res Ctr Seafood, Sch Food Sci & Technol, Dalian 116034, Peoples R China

6.Yurun Grp, Natl Key Lab Meat Qual Control & New Resource Crea, Nanjing 210041, Peoples R China

7.Suzhou Fuliji Liulaoer Roast Chicken Co Ltd, Suzhou 234101, Peoples R China

8.Anhui Youzhi Youwei Food Co Ltd, Maanshan 238253, Peoples R China

关键词： Low-energy emulsification; Thermal stability; Aspartic acid and arginine complexes; Secondary structure; Intermolecular force

期刊名称：JOURNAL OF FOOD ENGINEERING （ 影响因子：5.5； 五年影响因子：5.7 ）

ISSN： 0260-8774

年卷期： 2024 年 361 卷

页码：

收录情况： SCI

摘要： The purpose of this study was to use the complexes of gelatin (GA), positively charged arginine (Arg), and negatively charged aspartic acid (Asp) to produce a stable o/w emulsion using a low-energy stirring method. The thermal stability mechanism of this emulsion was investigated by evaluating its particle size, microstructure, differential scanning calorimetry (DSC), rheology, and zeta potential, as well as the secondary structure, surface hydrophobicity, and interaction force of gelatin-amino acid complexes. The results showed that adding Arg and/ or Asp significantly decreased the particle size of the emulsion (P < 0.05). Particularly, the emulsion stabilized by gelatin-Arg-Asp showed the smallest particle size of 0.9 mu m (D3.2), the highest absolute zeta potential (21.58 mV), the greatest viscosity, and the highest thermal stability. Even after heating at 121 C-degrees for 20 min, this emulsion still had smaller particles than the unheated emulsion with or without Arg or Asp. Asp and Arg enhanced the triple helix content of gelatin through intramolecular hydrogen bonds and protected the surface hydrophobic groups of gelatins through intermolecular hydrophobic interactions of guanidine groups, increasing the depolymerization and ordered structure of gelatin and thus prolonging the temperature corresponding to the endothermic peak from 24.16 C-degrees to 84.35 C-degrees. These findings should contribute to the high thermal stability of the gelatin-Arg-Asp-stabilized emulsion. This study suggested that macromolecular protein-stabilized oil-in-water emulsions with a low oil phase content could be prepared by low-energy emulsification.