Mild alkalinity preheating treatment regulates the heat and ionic strength co-tolerance of whey protein aggregates

被引:1
作者
Zhang, Rui
Zhang, Junwei
Zou, Bowen
Ren, Chao
Na, Xiaokang
Xu, Xianbing
Du, Ming
Zhu, Beiwei
Wu, Chao [1 ]
机构
[1] Dalian Polytech Univ, Sch Food Sci & Technol, Dalian 116034, Peoples R China
关键词
Whey protein; Soluble aggregates; Thermostability; NaCl tolerance; Protein beverages; Preheating; BOVINE SERUM-ALBUMIN; BETA-LACTOGLOBULIN; CIRCULAR-DICHROISM; INDUCED GELATION; FLUID BALANCE; STABILITY; FLUORESCENCE; PH; SPECTROSCOPY; ISOLATE;
D O I
10.1016/j.foodres.2024.114845
中图分类号
TS2 [食品工业];
学科分类号
0832 ;
摘要
A major obstacle to the use of whey protein in protein-enriched sports beverages is the heat-induced gelation of the protein in the presence of salt. In this study, whey protein soluble aggregates (WPSAs) with high tolerance to NaCl and heat were successfully generated by preheating whey protein isolate (WPI) at a low concentration (1 % w/v) and pH 8.5. The suspension of WPSAs (5% w/v) with 100 mM NaCl maintained clarity, transparency, and good flowability even after 30 min of heating at 100 degrees C. However, suspensions prepared by untreated WPI turned into milky white gels. WPSAs had a reduced Zeta potential at pH 7 compared to WPI, making them more resistant to the electrostatic screening caused by NaCl. Additionally, WPSAs exhibited reduced sensitivity to heat treatment due to a more compact structure achieved through preheating modification. In light of these findings, a straightforward and effective method was presented for regulating the heat and ionic strength tolerance of whey protein aggregates.
引用
收藏
页数:10
相关论文
共 57 条
  • [1] Effect of ethanol on gelation and microstructure of whey protein gels in the presence of NaCl
    Andreadis, Marios
    Moschakis, Thomas
    [J]. FOOD HYDROCOLLOIDS, 2023, 134
  • [2] Trends in the food and sports nutrition industry: A review
    Arenas-Jal, Marta
    Sune-Negre, J. M.
    Perez-Lozano, Pilar
    Garcia-Montoya, Encarna
    [J]. CRITICAL REVIEWS IN FOOD SCIENCE AND NUTRITION, 2020, 60 (14) : 2405 - 2421
  • [3] Bovine beta-lactoglobulin at 1.8 angstrom resolution - Still an enigmatic lipocalin
    Brownlow, S
    Cabral, JHM
    Cooper, R
    Flower, DR
    Yewdall, SJ
    Polikarpov, I
    North, ACT
    Sawyer, L
    [J]. STRUCTURE, 1997, 5 (04) : 481 - 495
  • [4] FLUORESCENCE AND LOCATION OF TRYPTOPHAN RESIDUES IN PROTEIN MOLECULES
    BURSTEIN, EA
    VEDENKINA, NS
    IVKOVA, MN
    [J]. PHOTOCHEMISTRY AND PHOTOBIOLOGY, 1973, 18 (04) : 263 - 279
  • [5] Enhanced heat stability of high protein emulsion systems provided by microparticulated whey proteins
    Cakir-Fuller, Esra
    [J]. FOOD HYDROCOLLOIDS, 2015, 47 : 41 - 50
  • [6] Effect of Self-Association of Bovine Serum Albumin on the Stability of Surfactant-Induced Aggregates of Allylamine-Capped Silicon Quantum Dots
    Chatterjee, Surajit
    Mukherjee, Tushar Kanti
    [J]. JOURNAL OF PHYSICAL CHEMISTRY B, 2013, 117 (50) : 16110 - 16116
  • [7] pH and ionic strength responsive core-shell protein microgels fabricated via simple coacervation of soy globulins
    Chen, Nannan
    Nicolai, Taco
    Chassenieux, Christophe
    Wang, Yong
    [J]. FOOD HYDROCOLLOIDS, 2020, 105
  • [8] Effect of pH-shifting treatment on structural and functional properties of whey protein isolate and its interaction with (-)-epigallocatechin-3-gallate
    Chen, Weijun
    Wang, Wenjun
    Ma, Xiaobin
    Lv, Ruiling
    Watharkar, Ritesh Balaso
    Ding, Tian
    Ye, Xingqian
    Liu, Donghong
    [J]. FOOD CHEMISTRY, 2019, 274 : 234 - 241
  • [9] Proteomic Characterization of Native and Rearranged Disulfide Bonds in Proteins from Thermally Treated and Commercial Milk Samples
    Ciaravolo, Valentina
    Scaloni, Andrea
    Novi, Gianfranco
    Renzone, Giovanni
    Arena, Simona
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2023, 71 (26) : 10212 - 10225
  • [10] Investigating the synergistic effects of high-pressure homogenization and pH shifting on the formation of tryptophan-rich nanoparticles
    Dong, Hongmin
    Yang, Lixin
    Dadmohammadi, Younas
    Li, Peilong
    Lin, Tiantian
    He, Yanhong
    Zhou, Yufeng
    Li, Jieying
    Meletharayil, Gopinathan
    Kapoor, Rohit
    Abbaspourrad, Alireza
    [J]. FOOD CHEMISTRY, 2024, 434