Improvement of heat-induced nanofibrils formation of soy protein isolate through NaCl and microwave

被引:22
作者
Afkhami, Rana [1 ]
Varidi, Mohammad Javad [1 ]
Varidi, Mehdi [1 ]
Hadizadeh, Farzin [2 ]
机构
[1] Ferdowsi Univ Mashhad FUM, Fac Agr, Dept Food Sci & Technol, Mashhad, Iran
[2] Mashhad Univ Med Sci, Sch Pharm, Med Chem Dept, Mashhad, Iran
关键词
Conventional heating; Microwave heating; Protein fibrils; Soy protein isolate; BETA-LACTOGLOBULIN NANOFIBRILS; AMYLOID-LIKE FIBRILS; PH; 2.0; GROWTH-KINETICS; IONIC-STRENGTH; CONGLYCININ; FUNCTIONALITY; AGGREGATION; TEMPERATURE; HYDROLYSATE;
D O I
10.1016/j.foodhyd.2022.108443
中图分类号
O69 [应用化学];
学科分类号
081704 ;
摘要
A novel method involving microwave heating (MH) at 85 degrees C can be applied to induce the self-assembly of soy protein isolate (SPI) into SPI-nanofibrils at low pH and in the presence of NaCl. The effect of heating type (MH and conventional heating (CH)), heating times (0, 30, 60, and 90 min), and NaCl (0 and 160 mM) on the for-mation and physicochemical properties of SPI-nanofibrils at pH 2.0 and 85 degrees C were investigated. The SPI-nanofibrils were characterized through thioflavin T (Th T) fluorescence, intrinsic fluorescence emission spec-troscopy, atomic force microscopy (AFM), transmission electron microscopy (TEM), surface charge density, sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE), and Fourier transform infrared spec-trometer (FTIR). The sample treated with MH for 30 min in the presence of NaCl had the highest potential to form SPI-nanofibrils as evidenced by Th T. The AFM (998 nm) and TEM (1573 nm) results demonstrated that the longest SPI-nanofibrils were formed in the sample treated with MH for 60 min in the presence of NaCl. MH and NaCl procedures had a significant effect on the level of 8-sheet and led to increasing its level (35.3%). The results of SDS-PAGE indicated that progressive polypeptide hydrolysis occurred upon heating, and the polypeptide hydrolysis for the samples treated with MH was much more severe than the samples treated with CH. From the surface charge density results, MH and NaCl led to decreasing electrostatic repulsion. Hence, these phenomena might increase the SPI-nanofibrils level by the electrostatic interaction. Finally, the data suggest that MH and NaCl not only can enhance the potential for SPI-nanofibrils formation but also increase the length of SPI-nanofibrils.
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页数:14
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共 67 条
  • [1] Micrometer-sized fibrillar protein aggregates from soy glycinin and soy protein isolate
    Akkermans, C.
    Van Der Goot, A. J.
    Venema, P.
    Gruppen, H.
    Vereijken, J. M.
    Van Der Linden, E.
    Boom, R. M.
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2007, 55 (24) : 9877 - 9882
  • [2] The Effect of Limited Proteolysis by Trypsin on the Formation of Soy Protein Isolate Nanofibrils
    An, Di
    Li, Liang
    [J]. JOURNAL OF CHEMISTRY, 2020, 2020
  • [3] Infrared spectroscopy of proteins
    Barth, Andreas
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-BIOENERGETICS, 2007, 1767 (09): : 1073 - 1101
  • [4] Molecular mechanism of Thioflavin-T binding to amyloid fibrils
    Biancalana, Matthew
    Koide, Shohei
    [J]. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS, 2010, 1804 (07): : 1405 - 1412
  • [5] Efficient microwave-assisted cyanation of aryl bromide
    Cai, LZ
    Liu, X
    Tao, XC
    Shen, D
    [J]. SYNTHETIC COMMUNICATIONS, 2004, 34 (07) : 1215 - 1221
  • [6] Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications
    Cao, Yiping
    Mezzenga, Raffaele
    [J]. ADVANCES IN COLLOID AND INTERFACE SCIENCE, 2019, 269 : 334 - 356
  • [7] Nanocomplexation between thymol and soy protein isolate and its improvements on stability and antibacterial properties of thymol
    Chen, Fei-ping
    Kong, Nian-qing
    Wang, Ling
    Luo, Zheng
    Yin, Juan
    Chen, Yulong
    [J]. FOOD CHEMISTRY, 2021, 334
  • [8] Modifications of soy protein isolates using combined extrusion pre-treatment and controlled enzymatic hydrolysis for improved emulsifying properties
    Chen, Lin
    Chen, Jianshe
    Ren, Jiaoyan
    Zhao, Mouming
    [J]. FOOD HYDROCOLLOIDS, 2011, 25 (05) : 887 - 897
  • [9] Modulating β-Lactoglobulin Nanofibril Self-Assembly at pH 2 Using Glycerol and Sorbitol
    Dave, Anant C.
    Loveday, Simon M.
    Anema, Skelte G.
    Jameson, Geoffrey B.
    Singh, Harjinder
    [J]. BIOMACROMOLECULES, 2014, 15 (01) : 95 - 103
  • [10] β-Lactoglobulin Self-Assembly: Structural Changes in Early Stages and Disulfide Bonding in Fibrils
    Dave, Anant C.
    Loveday, Simon M.
    Anema, Skelte G.
    Loo, Trevor S.
    Norris, Gillian E.
    Jameson, Geoffrey B.
    Singh, Harjinder
    [J]. JOURNAL OF AGRICULTURAL AND FOOD CHEMISTRY, 2013, 61 (32) : 7817 - 7828