Modification of functional, rheological and structural characteristics of myofibrillar proteins by high-intensity ultrasonic and papain treatment

被引:52
作者
Amiri, Amir [1 ]
Sharifian, Parisa [1 ]
Morakabati, Naghmeh [2 ]
Mousakhani-Ganjeh, Alireza [1 ]
Mirtaheri, Maryamalsaddat [3 ]
Nilghaz, Azadeh [4 ]
Guo, Yi-gong [5 ]
Pratap-Singh, Anubhav [5 ]
机构
[1] Isfahan Univ Technol, Dept Food Sci & Technol, Coll Agr, Esfahan 8415683111, Iran
[2] Islamic Azad Univ, Dept Food Sci & Technol, Nour Branch, Mazandaran, Iran
[3] Islamic Azad Univ, Dept Chem, North Tehran Branch, Tehran, Iran
[4] Deakin Univ, Inst Frontier Mat, Geelong, Vic 3216, Australia
[5] Univ British Columbia, Food Nutr & Hlth, Fac Land & Food Syst, 2205 East Mall, Vancouver, BC V6T 1Z4, Canada
关键词
Enzyme; Emulsification; Foaming properties; Sonication; Solubility; PHYSICAL-PROPERTIES; POWER ULTRASOUND; INDUCED GELATION; WATER; PRETREATMENT; SOLUBILITY; ISOLATE;
D O I
10.1016/j.ifset.2021.102748
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
The effects of sonication duration (15 and 30 min) and papain enzyme treatments on the conformational, physicochemical and functional traits of myofibrillar proteins (MPs) were addressed in this study. As the ultrasound duration was increased, the water holding capacity (WHC), solubility, foaming and emulsifying properties were improved as a result of the changes in the particles size distribution and zeta potential. Our results indicated that the turbulence force caused increments in the surface hydrophobicity and significant changes in the secondary structure. Also, the rheological properties were influenced by both cavitation force and papain treatment. According to the observations, the samples treated with sonication (for 15 and 30 min) and enzyme were more elastic with higher viscosity, as compared to the control. Compared with the control, enzymolyzed samples indicated better functionality. Moreover, papain treatment led to the increase of the hydrophobicity groups on the surface of proteins and the decrease of the amount of alpha-helix and beta-sheet structures. It was noteworthy that the most changes in the structure and techno-functionality of myofibrillar proteins were observed for the sample affected by the simultaneous application of papain treatment and 15 min sonication. The highest values in the surface hydrophobicity, specific surface area, net charge, storage modulus, solubility and WHC belonged to this sample. However, enzyme-modified samples exposed to the longer sonication time (30 min) demonstrated reductions in solubility, WHC and surface hydrophobicity, as well as increases in the particle size distribution and protein turbidity.
引用
收藏
页数:9
相关论文
共 50 条
  • [31] Modification of rapeseed protein by ultrasound-assisted pH shift treatment: Ultrasonic mode and frequency screening, changes in protein solubility and structural characteristics
    Li, Yihe
    Cheng, Yu
    Zhang, Zhaoli
    Wang, Yang
    Mintah, Benjamin Kumah
    Dabbour, Mokhtar
    Jiang, Hui
    He, Ronghai
    Ma, Haile
    [J]. ULTRASONICS SONOCHEMISTRY, 2020, 69
  • [32] Cellulose Hollow Annular Nanoparticles Prepared from High-Intensity Ultrasonic Treatment
    Xu, Yongjian
    Gao, Minlan
    Zhang, Yongqi
    Ning, Lulu
    Zhao, Deqing
    Ni, Yonghao
    [J]. ACS NANO, 2022, 16 (06) : 8928 - 8938
  • [33] High-intensity ultrasound modified the functional properties of Neosalanx taihuensis myofibrillar protein and improved its emulsion stability
    Deng, Xiao-hong
    Ni, Xiang-xiang
    Han, Jia-hui
    Yao, Wen-hua
    Fang, Ya-jie
    Zhu, Qin
    Xu, Ming-feng
    [J]. ULTRASONICS SONOCHEMISTRY, 2023, 97
  • [34] High-pressure induced structural modification of porcine myofibrillar protein and its relation to rheological and emulsifying properties
    Lee, Min Hyeock
    Yong, Hae In
    Kim, Yun Jeong
    Choi, Yun-Sang
    [J]. MEAT SCIENCE, 2023, 196
  • [35] Solubilization strategy of myofibrillar proteins in low-ionic media (prototype soup): The effect of high-intensity ultrasound combined with non-covalent or covalent modification of polyphenols on myosin molecular assembly
    Zhang, Chao
    Wang, Ziyi
    Liu, Qian
    Chen, Qian
    Sun, Fangda
    Liu, Haotian
    Kong, Baohua
    [J]. FOOD CHEMISTRY, 2024, 436
  • [36] High-Intensity Ultrasound Treatment on Soy Protein after Selectively Proteolyzing Glycinin Component: Physical, Structural, and Aggregation Properties
    Xia, Wenjie
    Pan, Siyi
    Cheng, Zhe
    Tian, Yan
    Huang, Xingjian
    [J]. FOODS, 2020, 9 (06)
  • [37] Effect of high-intensity ultrasonic time on structural, mechanical, and physicochemical properties of β-conglycinin (7S)- Transglutaminase (TGase) composite edible films
    Zhang, Lan
    Zhang, Jixin
    Wen, Pingping
    Xu, Huiqing
    Cui, Guiyou
    Wang, Jun
    [J]. ULTRASONICS SONOCHEMISTRY, 2023, 98
  • [38] High-intensity ultrasound treatment of shiitake mushroom protein isolate: effects on physicochemical, structural properties, and functional performance
    Cao, Qinghui
    Du, Hongying
    [J]. JOURNAL OF THE SCIENCE OF FOOD AND AGRICULTURE, 2024,
  • [39] Solubilization and stable dispersion of myofibrillar proteins in water through the destruction and inhibition of the assembly of filaments using high-intensity ultrasound
    Liu, Haotian
    Zhang, Huan
    Liu, Qian
    Chen, Qian
    Kong, Baohua
    [J]. ULTRASONICS SONOCHEMISTRY, 2020, 67
  • [40] Effect of high-intensity ultrasound on the structural, rheological, emulsifying and gelling properties of insoluble potato protein isolates
    Zhao, Ruixuan
    Liu, Xinshuo
    Liu, Wei
    Liu, Qiannan
    Zhang, Liang
    Hu, Honghai
    [J]. ULTRASONICS SONOCHEMISTRY, 2022, 85