Science and Technology of Food Industry

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Volume 42 Issue 12
Jun.  2021
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DAI Yiqiang, LIU Xiaoli, WU Han, et al. Effects of Different Coagulants on Intermolecular Forces and Secondary Structure of Soybean Protein Isolate[J]. Science and Technology of Food Industry, 2021, 42(12): 89−94. (in Chinese with English abstract). doi: 10.13386/ j.issn1002-0306.2020110009.
Citation: DAI Yiqiang, LIU Xiaoli, WU Han, et al. Effects of Different Coagulants on Intermolecular Forces and Secondary Structure of Soybean Protein Isolate[J]. Science and Technology of Food Industry, 2021, 42(12): 89−94. (in Chinese with English abstract). doi: 10.13386/ j.issn1002-0306.2020110009.
shu

Effects of Different Coagulants on Intermolecular Forces and Secondary Structure of Soybean Protein Isolate

  • 1.

    Institute of Agricultural Product Processing, Jiangsu Academy of Agricultural Sciences, Nanjing 210014, China

  • 2.

    College of Food Science and Technology, Nanjing Agricultural University, Nanjing 210095, China

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  • Received Date: November 02, 2020
  • Available Online: April 12, 2021
    Graphical Abstract
    • Abstract
  • To study the changes of intermolecular forces and secondary structure of soy protein induced by MgCl2, CaSO4, lactic acid, acetic acid, GDL and fermented soy whey, the effects of different coagulants on the pH value, surface hydrophobicity, free sulfhydryl group (SH), Zeta potential, α-helix, β-sheet, β-turn and random coil during SPI tofu processing were analyzed, while the SPI was used as the research object. Both salt coagulants and acid coagulants could reduce the pH values of SPI solution, and the final pH value was 6.08~6.14 and 5.25~5.58, respectively. Compared with heated SPI solution without coagulant, the addition of coagulants caused increases in the surface hydrophobicity and free SH content, and a decrease in Zeta potential in SPI solution. The surface hydrophobicity of SPI induced by coagulants increased first and then decreased, and free SH content decreased at 0~45 min. The Zeta potential of SPI solution added with fermented soy whey was significantly higher than that of other coagulants (P<0.05), ranging from 9.19 mV to 9.90 mV. In addition, salt coagulants induced a shift of α-helix and β-turn into β-sheet of soy proteins, and acid coagulants destroyed β-sheet of SPI. In particular, the SPI added with fermented soy whey had α-helix ratio between lactic acid and salt coagulants, and β-turn ratio between lactic acid and acetic acid.
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    • References (32)
  • [1]
    贺云. 豆腐酸浆中乳酸菌的分离鉴定及其在酸浆豆腐中的应用[D]. 无锡: 江南大学, 2018: 1−2.
    [2]
    Chang K L B, Lin Y S, Chen R H. The effect of chitosan on the gel properties of tofu (soybean curd)[J]. Journal of Food Engineering,2003,57(4):315−319. doi: 10.1016/S0260-8774(02)00345-X
    [3]
    Lee C H, Rha C. Microstructure of soybean aggregates and its relation to the physical and textural properties of the curd[J]. Journal of Food Science,1978,43(6):79−84. doi: 10.1111/j.1365-2621.1978.tb09740.x
    [4]
    Lu X, Lu Z, Yin L, et al. Effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel[J]. Food Research International,2010,43:1673−1683. doi: 10.1016/j.foodres.2010.05.011
    [5]
    王旭峰. CaSO4诱导大豆分离蛋白乳状液凝胶性质影响因素的研究[D]. 无锡: 江南大学, 2017: 4−5.
    [6]
    王宸之, 陈宇, 万重, 等. 豆腐凝胶成型机理研究进展[J]. 东北农业大学学报,2017,48(10):88−96. doi: 10.3969/j.issn.1005-9369.2017.10.011
    [7]
    Schuldt S, Raak N, Jaros D, et al. Acid-induced formation of soy protein gels in the presence of NaCl[J]. LWT - Food Science and Technology,2014,57(2):634−639. doi: 10.1016/j.lwt.2014.02.013
    [8]
    Chen N, Zhao M, Sun W, et al. Effect of oxidation on the emulsifying properties of soy protein isolate[J]. Food research international,2013,52(1):26−32. doi: 10.1016/j.foodres.2013.02.028
    [9]
    Shigeru H, Shuryo N. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins[J]. Journal of Food Science,1985,50:486−491.
    [10]
    Zhang M, Wang P, Zou M, et al. Microbial transglutaminase-modified protein network and its importance in enhancing the quality of high-fiber tofu with okara[J]. Food Chemistry,2019,289:169−176. doi: 10.1016/j.foodchem.2019.03.038
    [11]
    Liang X, Ma C, Yan X, et al. Structure, rheology and functionality of whey protein emulsion gels: Effects of double cross-linking with transglutaminase and calcium ions[J]. Food Hydrocolloids,2020,102:105569. doi: 10.1016/j.foodhyd.2019.105569
    [12]
    Cao F, Li X, Luo S, et al. Effects of organic acid coagulants on the physical properties of and chemical interactions in tofu[J]. LWT - Food Science and Technology,2017,85:58−65. doi: 10.1016/j.lwt.2017.07.005
    [13]
    Liu Z, Chang S. Effect of soy milk characteristics and cooking conditions on coagulant requirements for making filled tofu[J]. Journal of Agricultural and Food Chemistry, 2004, 52(11): 3405−3411.
    [14]
    Hsia S, Hsiao Y, Li W, et al. Aggregation of soy protein isoflavone complexes and gel formation induced by glucono-δ-lactone in soymilk[J]. Scientific Reports,2016,6(1):35718. doi: 10.1038/srep35718
    [15]
    赵海波. 硫酸钙诱导热变性大豆蛋白凝胶的影响因素及应用研究[D]. 无锡: 江南大学, 2017: 1−6.
    [16]
    Hu H, Li-Chen E C Y, Wan L, et al. The effect of high intensity ultrasonic pre-treatment on the properties of soybean protein isolate gel induced by calcium sulfate[J]. Food Hydrocolloids,2013,32(2):303−311. doi: 10.1016/j.foodhyd.2013.01.016
    [17]
    Chen J, Sun Y. Modeling of the salt effects on hydrophobic adsorption equilibrium of protein[J]. Journal of Chromatography A,2003,992(1-2):29−40. doi: 10.1016/S0021-9673(03)00277-2
    [18]
    Haskard C A, Li-Chen E C Y. Hydrophobicity of bovine serum albumin and ovalbumin determined using uncharged (PRODAN) and anionic (ANS-) fluorescent probes[J]. Journal of Agricultural and Food Chemistry,1998,46(7):2671−2677. doi: 10.1021/jf970876y
    [19]
    Greene F C. Interactions of anionic and cationic fluorescent probes with proteins: The effect of charge[J]. Journal of Protein Chemistry,1984,3:167−180. doi: 10.1007/BF01040498
    [20]
    Zhao J, Dong F, Li Y, et al. Effect of freeze–thaw cycles on the emulsion activity and structural characteristics of soy protein isolate[J]. Process Biochemistry,2015,50(2):1607−1613. doi: 10.1016/j.procbio.2015.06.021
    [21]
    Kohyama K, Sano Y, Doi E. Rheological characteristics and gelation mechanism of tofu (Soybean Curd)[J]. Journal of Agricultural and Food Chemistry,1995,43(10):1808−1812. doi: 10.1021/jf00055a011
    [22]
    李传运. 酶处理对大豆蛋白凝胶性的影响研究[D]. 合肥: 合肥工业大学, 2019: 1-2.
    [23]
    左锋. 微压煮浆对豆乳蛋白粒子形成及其加工特性的影响机制研究[D]. 北京: 中国农业大学, 2016: 17-18.
    [24]
    Ryan K N, Zhong Q, Foegeding E A. Use of whey protein soluble aggregates for thermal stability-a hypothesis paper[J]. Journal of Food Science,2013,78(8):R1105−1115. doi: 10.1111/1750-3841.12207
    [25]
    Akbari A, Wu J. Cruciferin nanoparticles: Preparation, characterization and their potential application in delivery of bioactive compounds[J]. Food Hydrocolloids,2016,54:107−118. doi: 10.1016/j.foodhyd.2015.09.017
    [26]
    Li C, Rui X, Zhang Y, et al. Production of tofu by lactic acid bacteria isolated from naturally fermented soy whey and evaluation of its quality[J]. LWT-Food Science and Technology,2017,82:227−234. doi: 10.1016/j.lwt.2017.04.054
    [27]
    杨芳. 豆腐凝胶形成机理及水分状态与品质关系研究[D]. 武汉: 华中农业大学, 2009: 34-37.
    [28]
    Qiao Z, Chen X, Cheng Y, et al. Microbiological and chemical changes during the production of acidic whey, a traditional chinese tofu-coagulant[J]. International Journal of Food Properties, 2010, 13(1): 90−104.
    [29]
    Liu R, Zhao S M, Xiong S B, et al. Role of secondary structures in the gelation of porcine myosin at different pH values[J]. Meat Science,2008,80(3):632−639. doi: 10.1016/j.meatsci.2008.02.014
    [30]
    杨岚. 热处理强度对大豆蛋白凝胶性质的影响及机制初探[D]. 无锡: 江南大学, 2018: 18-23.
    [31]
    Utsumi S, Damodaran S, Kinsella J. Heat-induced interactions between soybean proteins: Preferential association of 11S basic subunits and. beta. subunits of 7S[J]. Journal of Agricultural and Food Chemistry, 1984, 32(6): 1406-1412.
    [32]
    HerreroA, Jiménez-Colmenero F, Carmona P. Elucidation of structural changes in soy protein isolate upon heating by Raman spectroscopy[J]. International Journal of Food Science & Technology, 2009, 44: 711−717.
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