Insighting the effect of lard-based diacylglycerol on the thermal gelation and rheological properties of myofibrillar protein influenced by soy protein isolate

被引:1
|
作者
Zhao, Xinxin [1 ]
Sun, Xiankun [1 ]
Lai, Bangcheng [1 ]
Wu, Mangang [1 ]
Ge, Qingfeng [1 ]
Peng, Xinyan [3 ]
Kong, Baohua [2 ]
Yu, Hai [1 ]
机构
[1] Yangzhou Univ, Coll Food Sci & Engn, Yangzhou 225127, Jiangsu, Peoples R China
[2] Northeast Agr Univ, Coll Food Sci, Harbin 150030, Heilongjiang, Peoples R China
[3] Yantai Univ, Coll Life Sci, Yantai 264005, Shandong, Peoples R China
基金
中国国家自然科学基金;
关键词
Soy protein isolate; Lard-based diacylglycerol; Myofibrillar protein; Molecular docking; Thermal gelation; Rheological property; HEAT-INDUCED GELATION; COMPOSITE GELS; ULTRASONIC PRETREATMENT; PORK FAT; OIL; EMULSIONS; MYOSIN; MICROSTRUCTURE; FUNCTIONALITY; REPLACEMENT;
D O I
10.1016/j.foodhyd.2024.110082
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
The objective of this study was to investigate the role of the replacing animal fat in the meat gel system with lardbased diacylglycerol (DG), which has health benefits and similar characteristics (such as taste, smell, and usability) to lard triacylglycerol (TG, the major component of pork fat). The impact of lard -based DG on the thermal gelation and rheological properties of myofibrillar protein (MP) as influenced by the incorporation of soy protein isolate (SPI, 0 -0.75% protein) was investigated, and the interaction mechanism was also explored. The gel structure became more continuous and compact with the incorporation of DG or purified DG (PDG) and the decrease of SPI content, as reflected by the change of secondary structures, which was beneficial to restrict the mobility of immobilized water. With the incorporation of DG or PDG and the decrease in the amount of SPI, the gel strength, G ' , and G '' were increased. Molecular docking results further revealed that the DG interacted with SPI mainly through van der Waals forces and hydrogen bonds, and interacted with MP mainly through van der Waals forces, hydrogen bonds, and hydrophobic interactions. More importantly, the negative binding energies of the DG -protein complexes were lower than those of the TG -protein complexes, indicating that the interaction was spontaneous and that DG is more likely to interact with proteins than TG. In conclusion, this study provides a vital theoretical basis at the molecular level for the development of desired quality meat products containing DG with health benefits.
引用
收藏
页数:14
相关论文
共 50 条
  • [31] Effect of Interaction between Mealworm Protein and Myofibrillar Protein on the Rheological Properties and Thermal Stability of the Prepared Emulsion Systems
    Kim, Tae-Kyung
    Lee, Min Hyeock
    Yong, Hae In
    Jung, Samooel
    Paik, Hyun-Dong
    Jang, Hae Won
    Choi, Yun-Sang
    FOODS, 2020, 9 (10)
  • [32] Improvement of kefir fermentation on rheological and microstructural properties of soy protein isolate gels
    Luo, Jiaqi
    Liu, Siyu
    Lu, Hongyun
    Wang, Yuxi
    Chen, Qihe
    Shi, Ying
    FOOD RESEARCH INTERNATIONAL, 2023, 174
  • [33] Effect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate
    Yan Yan Liu
    Xin An Zeng
    Zhiping Deng
    Shu Juan Yu
    Shinji Yamasaki
    European Food Research and Technology, 2011, 233 : 841 - 850
  • [34] Improvement of gelation properties of soy protein isolate emulsion induced by calcium cooperated with magnesium
    Wang, Xufeng
    Luo, Kaiyun
    Liu, Shutao
    Adhikari, Benu
    Chen, Jie
    JOURNAL OF FOOD ENGINEERING, 2019, 244 : 32 - 39
  • [35] Effect of pulsed electric field on the secondary structure and thermal properties of soy protein isolate
    Liu, Yan Yan
    Zeng, Xin An
    Deng, Zhiping
    Yu, Shu Juan
    Yamasaki, Shinji
    EUROPEAN FOOD RESEARCH AND TECHNOLOGY, 2011, 233 (05) : 841 - 850
  • [36] Barley protein isolate: Thermal, functional, rheological, and surface properties
    Mohamed, Abdellatif
    Hojilla-Evangelista, Mila P.
    Peterson, Steve C.
    Biresaw, Girma
    JOURNAL OF THE AMERICAN OIL CHEMISTS SOCIETY, 2007, 84 (03) : 281 - 288
  • [37] Oats protein isolate: Thermal, rheological, surface and functional properties
    Mohamed, Abdellatif
    Biresaw, Girma
    Xu, Jingyuan
    Hojilla-Evangelista, Mila P.
    Rayas-Duarte, Patricia
    FOOD RESEARCH INTERNATIONAL, 2009, 42 (01) : 107 - 114
  • [38] Barley protein isolate: Thermal, functional, rheological, and surface properties
    Mohamed, Abdellatif
    Hojilla-Evangelista, Mila P.
    Peterson, Steve C.
    Biresaw, Girma
    JAOCS, Journal of the American Oil Chemists' Society, 2007, 84 (03): : 281 - 288
  • [39] Effects of β-conglycinin and glycinin on thermal gelation and gel properties of soy protein
    Kang, IJ
    Lee, YS
    FOOD SCIENCE AND BIOTECHNOLOGY, 2005, 14 (01) : 11 - 15
  • [40] Gelation and rheological properties of myofibrillar proteins influenced by the addition of soybean protein isolates subjected to an acidic pH treatment combined with a mild heating
    Niu, Haili
    Li, Yue
    Han, Jianchun
    Liu, Qian
    Kong, Baohua
    FOOD HYDROCOLLOIDS, 2017, 70 : 269 - 276