GUO Peifeng, ZENG Jiayan, QIAN Ruiqi, et al. Effect of Combination of Pulsed Electric Field and pH Shifting on Structure and Functional Properties of Soybean Protein Isolates[J]. Science and Technology of Food Industry, 2025, 46(7): 112−122. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024050128.
Citation: GUO Peifeng, ZENG Jiayan, QIAN Ruiqi, et al. Effect of Combination of Pulsed Electric Field and pH Shifting on Structure and Functional Properties of Soybean Protein Isolates[J]. Science and Technology of Food Industry, 2025, 46(7): 112−122. (in Chinese with English abstract). doi: 10.13386/j.issn1002-0306.2024050128.

Effect of Combination of Pulsed Electric Field and pH Shifting on Structure and Functional Properties of Soybean Protein Isolates

More Information
  • Received Date: May 14, 2024
  • Available Online: February 07, 2025
  • Soybean protein isolate (SPI) is an important vegetable protein source used in the food industry. Its functional properties are negatively impacted by its dense spherical aggregate structure, which reduces its molecular flexibility. In this study, pulsed electric field (PEF) and pH shifting techniques were applied to modify SPI structure. The effects of three different treatment strategies combining pulsed electric field and pH shifting (PEF first followed by pH shifting, pH shifting first followed by PEF, and simultaneous PEF and pH shifting) on the structure and functional properties of SPI were investigated. Among the three methods, simultaneous PEF and pH shifting achieved the most obvious effect on the aggregated structure of SPI. This treated SPI exhibited the highest solubility (90.23%), smallest turbidity (0.074), largest absolute ζ-potential value (44.4 mV), and smallest particle size (63.5 nm). Simultaneous PEF and pH shifting could induce partial unfolding of secondary and tertiary structures in SPI, converting the spherical aggregates into a "molten globule state" that exhibited lower α-helix and β-sheet content and higher random coil content. The overall treated protein structure was loose and disordered. Modified SPI using different methods showed better functional properties. The order of improvement in SPI functional properties was as follows: Simultaneous PEF and pH shifting>pH shifting first followed by PEF>PEF first followed by pH shifting. Compared with untreated SPI, simultaneous PEF and pH shifting treatment of SPI increased the emulsifying activity, emulsifying stability, foaming activity, and lutein binding constant by 119.24%, 39.33%, 59.03%, and 245.81%, respectively. In conclusion, different treatments combining pulsed electric field and pH shifting can significantly affect the structural and functional properties of SPI. Simultaneous PEF and pH shifting treatment can induce the greatest degree of unfolding of the advanced structure of SPI and most strongly improve its functional properties.
  • [1]
    谭孟娜. 超高压协同pH偏移处理对大豆分离蛋白及其糖基化产物乳化性质影响研[D]. 合肥:合肥工业大学, 2021. [TAN M N. Effects of combined high hydrostatic pressure and pH shifting pretreatment on the emulsifying properties of soy protein isolates and its glycosylation products[D]. Hefei:Hefei University of Technology, 2021.]

    TAN M N. Effects of combined high hydrostatic pressure and pH shifting pretreatment on the emulsifying properties of soy protein isolates and its glycosylation products[D]. Hefei: Hefei University of Technology, 2021.
    [2]
    丁小娜. 超声协同离子液体调控大豆分离蛋白聚集结构及乳化性能研究[D]. 镇江:江苏大学, 2019. [DIN X N. The aggregation, structures and emulsifying properties of soybean protein isolate induced by synergism between ultrasound and ionic liquids[D]. Zhenjiang:Jiangsu University, 2019.]

    DIN X N. The aggregation, structures and emulsifying properties of soybean protein isolate induced by synergism between ultrasound and ionic liquids[D]. Zhenjiang: Jiangsu University, 2019.
    [3]
    刘紫薇, 朱明明, 王凤新, 等. 高温湿热处理对大豆分离蛋白的结构及其功能特性的影响[J]. 食品与发酵工业,2021,47(15):157−164. [LIU Z W, ZHU M M, WANG F X, et al. Effect of high temperature hydrothermal treatment on structure and functional properties of soybean protein isolate[J]. Food and Fermentation Industries,2021,47(15):157−164.]

    LIU Z W, ZHU M M, WANG F X, et al. Effect of high temperature hydrothermal treatment on structure and functional properties of soybean protein isolate[J]. Food and Fermentation Industries, 2021, 47(15): 157−164.
    [4]
    王硕, 王俊平, 张燕, 等. 非热加工技术对食品中蛋白质结构和功能特性的影响[J]. 中国农业科技导报,2015,17(5):114−120. [WANG S, WANG J P, ZHANG Y, et al. Effect of non-thermal processing technology on the structure and function of protein in food[J]. Journal of Agricultural Science and Technology,2015,17(5):114−120.]

    WANG S, WANG J P, ZHANG Y, et al. Effect of non-thermal processing technology on the structure and function of protein in food[J]. Journal of Agricultural Science and Technology, 2015, 17(5): 114−120.
    [5]
    曾新安. 脉冲电场食品非热加工技术[M]. 北京:科学出版社, 2019:24−26. [ZENG X A. Pulsed electric field food non-thermal processing technology[M]. Beijing:Science Press, 2019:24−26.]

    ZENG X A. Pulsed electric field food non-thermal processing technology[M]. Beijing: Science Press, 2019: 24−26.
    [6]
    卢姗, 王文敏, 罗丹, 等. 探析脉冲电场对食品蛋白质改性作用的研究进展[J]. 现代食品,2020(21):73−76. [LU S, WANG W M, LUO D, et al. Research progress on effects of pulse electric field on food protein modification[J]. Modern Food,2020(21):73−76.]

    LU S, WANG W M, LUO D, et al. Research progress on effects of pulse electric field on food protein modification[J]. Modern Food, 2020(21): 73−76.
    [7]
    李迎秋. 脉冲电场对大豆蛋白理化性质和脂肪氧化酶的影响[D]. 无锡:江南大学, 2007. [LI Y Q. Effects of pulsed electric fields on physicochemical properties of soybean protein and lipoxygenase[D]. Wuxi:Jiangnan University, 2007.]

    LI Y Q. Effects of pulsed electric fields on physicochemical properties of soybean protein and lipoxygenase[D]. Wuxi: Jiangnan University, 2007.
    [8]
    WANG R, WANG L H, WEN Q H, et al. Combination of pulsed electric field and pH shifting improves the solubility, emulsifying, foaming of commercial soy protein isolate[J]. Food Hydrocolloids,2023,134:108049. doi: 10.1016/j.foodhyd.2022.108049
    [9]
    HUANG L, DING X, LI Y, et al. The aggregation, structures and emulsifying properties of soybean protein isolate induced by ultrasound and acid[J]. Food Chemistry,2019,279:114−119. doi: 10.1016/j.foodchem.2018.11.147
    [10]
    HUANG L, ZHANG W, DING X, et al. Effects of dual-frequency ultrasound with different energy irradiation modes on the structural and emulsifying properties of soy protein isolate[J]. Food and Bioproducts Processing,2020,123:419−426. doi: 10.1016/j.fbp.2020.07.021
    [11]
    SUN P, ZHANG Q, ZHAO Y, et al. Improving gel properties of soy protein isolate through alkaline pH-shifting, mild heat treatment, and TGase cross-linking[J]. Food Hydrocolloids,2023,144:108924. doi: 10.1016/j.foodhyd.2023.108924
    [12]
    林凤岩, 黄永娜, 褚洪俊, 等. 我国大豆蛋白加工产业现状及发展趋势[J]. 中国油脂,2023,48(11):33−37. [LIN F Y, HUANG Y N, CHU H J, et al. Current situation san development trend of Chinese soybean protein processing industry[J]. China Oils and Fats,2023,48(11):33−37.]

    LIN F Y, HUANG Y N, CHU H J, et al. Current situation san development trend of Chinese soybean protein processing industry[J]. China Oils and Fats, 2023, 48(11): 33−37.
    [13]
    齐宝坤, 李杨, 王中江, 等. 不同品种大豆分离蛋白Zeta电位和粒径分布与表面疏水性的关系[J]. 食品科学,2017,38(3):114−118. [QI B K, LI Y, WANG Z J, et al. Relationship between surface hydrophobicity and zeta potential as well as particle size distribution of soybean protein isolates from different varieties[J]. Food Science,2017,38(3):114−118.]

    QI B K, LI Y, WANG Z J, et al. Relationship between surface hydrophobicity and zeta potential as well as particle size distribution of soybean protein isolates from different varieties[J]. Food Science, 2017, 38(3): 114−118.
    [14]
    SMITH P K, KROHN R I, HERMANSON G T, et al. Measurement of protein using bicinchoninic acid[J]. Analytical Biochemistry,1985,150(1):76−85. doi: 10.1016/0003-2697(85)90442-7
    [15]
    KATO A, NAKAI S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins[J]. Biochimica et Biophysica Acta (BBA)-Protein Structure,1980,624(1):13−20. doi: 10.1016/0005-2795(80)90220-2
    [16]
    TAN M, XU J, GAO H, et al. Effects of combined high hydrostatic pressure and pH-shifting pretreatment on the structure and emulsifying properties of soy protein isolates[J]. Journal of Food Engineering,2021,306:110622. doi: 10.1016/j.jfoodeng.2021.110622
    [17]
    WANG R, LIU Y, HU X, et al. New insights into the binding mechanism between osthole and β-lactoglobulin:Spectroscopic, chemometrics and docking studies[J]. Food Research International,2019,120:226−234. doi: 10.1016/j.foodres.2019.02.042
    [18]
    唐永欣, 彭松林, 郭晨晨, 等. 温和热辅助pH值碱性偏移处理对猪肝蛋白结构和功能特性的影响[J]. 食品科学,2023,44(24):88−96. [TANG Y X, PENG S L, GUO C C, et al. Effect of mild heating assisted alkaline pH shift treatment on the structural and functional properties of porcine liver protein[J]. Food Science,2023,44(24):88−96.] doi: 10.7506/spkx1002-6630-20230407-059

    TANG Y X, PENG S L, GUO C C, et al. Effect of mild heating assisted alkaline pH shift treatment on the structural and functional properties of porcine liver protein[J]. Food Science, 2023, 44(24): 88−96. doi: 10.7506/spkx1002-6630-20230407-059
    [19]
    源博恩. 亚基解离与重聚集对大豆蛋白结构和功能特性的影响[D]. 广州:华南理工大学, 2012. [YUAN B E. Effect of subunits dissociation and aggregation on structure and functional properties of soy protein[D]. Guangzhou:South China University of Technology, 2012.]

    YUAN B E. Effect of subunits dissociation and aggregation on structure and functional properties of soy protein[D]. Guangzhou: South China University of Technology, 2012.
    [20]
    LI Y, MAO L W, WANG L F, et al. Physicochemical and foam properties of ovalbumin-carboxymethylcellulose mixtures after mild heat treatment:Comparison of electrostatic repulsion and attraction[J]. Food Hydrocolloids,2024,153:110042. doi: 10.1016/j.foodhyd.2024.110042
    [21]
    RODRIGUES R M, AVELAR Z, VICENTE A A, et al. Influence of moderate electric fields in β-lactoglobulin thermal unfolding and interactions[J]. Food Chemistry,2020,304:125442. doi: 10.1016/j.foodchem.2019.125442
    [22]
    YU Y, GUAN Y, LIU J, et al. Molecular structural modification of egg white protein by pH-shifting for improving emulsifying capacity and stability[J]. Food Hydrocolloids,2021,121:107071. doi: 10.1016/j.foodhyd.2021.107071
    [23]
    RAJNI V, SUNEELA P, CONNAGH E. R, et al. Detection and identification of amino acids and proteins using their intrinsic fluorescence in the visible light spectrum[J]. Analytica Chimica Acta,2023,1282:341925. doi: 10.1016/j.aca.2023.341925
    [24]
    DJAMILA B. Molecular dynamics simulations at high temperatures of the Aeropyrum pernix L7Ae thermostable protein:Insight into the unfolding pathway[J]. Journal of Molecular Graphics and Modelling,2024,127:108700. doi: 10.1016/j.jmgm.2023.108700
    [25]
    YANG J, DUAN Y, GENG F, et al. Ultrasonic-assisted pH shift-induced interfacial remodeling for enhancing the emulsifying and foaming properties of perilla protein isolate[J]. Ultrasonics Sonochemistry,2022,89:106108. doi: 10.1016/j.ultsonch.2022.106108
    [26]
    安然. 大豆分离蛋白可溶性热聚集行为及其超声调控研究[D]. 哈尔滨:东北农业大学, 2019. [AN R. Study on soluble thermal aggregates of soybean protein isolate and its ultrasonic regulation[D]. Harbin:Northeast Agricultural University, 2019.]

    AN R. Study on soluble thermal aggregates of soybean protein isolate and its ultrasonic regulation[D]. Harbin: Northeast Agricultural University, 2019.
    [27]
    CAO W, GAO R, WAN X, et al. Effects of globular and flexible structures on the emulsifying and interfacial properties of mixed soy proteins[J]. Food Hydrocolloids,2022,127:107539. doi: 10.1016/j.foodhyd.2022.107539
    [28]
    LUCA A L, JULIANA V C S, MAXIME S, et al. On the foaming properties of plant proteins:Current status and future opportunities[J]. Trends in Food Science & Technology,2021,118(A):261−272.
    [29]
    XIONG W, WANG Y, ZHANG C, et al. High intensity ultrasound modified ovalbumin:Structure, interface and gelation properties[J]. Ultrasonics Sonochemistry,2016,31:302−309. doi: 10.1016/j.ultsonch.2016.01.014
    [30]
    WANG Y, WANG S, LI R, et al. Effects of combined treatment with ultrasound and pH shifting on foaming properties of chickpea protein isolate[J]. Food Hydrocolloids,2022,124:107351. doi: 10.1016/j.foodhyd.2021.107351
    [31]
    SRUTEE R, PREM P S. Modification of soy protein isolate and pea protein isolate by high voltage dielectric barrier discharge (DBD) atmospheric cold plasma:Comparative study on structural, rheological and techno-functional characteristics[J]. Food Chemistry,2024,447:138914. doi: 10.1016/j.foodchem.2024.138914
    [32]
    YANG H, LI L, XIE C, et al. Characteristics and structure of a soy protein isolate-lutein nanocomplex produced via high-pressure homogenization[J]. Journal of the Science of Food and Agriculture,2022,102(12):5411−5421. doi: 10.1002/jsfa.11894
    [33]
    LI H J, ZHANG Y M, LIU T T, et al. Transglutaminase, glucono-δ-lactone, and citric acid-induced whey protein isolation-milk fat emulsion gel embedding lutein and its application in processed cheese[J]. Journal of Dairy Science,2023,106(10):6635−6645. doi: 10.3168/jds.2022-23097
    [34]
    YI J, FAN Y, YOKOYAMA W, et al. Characterization of milk proteins-lutein complexes and the impact on lutein chemical stability[J]. Food Chemistry,2016,200:91−97. doi: 10.1016/j.foodchem.2016.01.035
    [35]
    崔宁. 叶黄素异构体抗氧化应激、抗炎活性、蛋白转运及应用研究[D]. 无锡:江南大学, 2023. [CUI N. Study on the anti-oxidative stress, anti-inflammatory effects, protein transport and application of lutein isomers[D]. Wuxi:Jiangnan University, 2023.]

    CUI N. Study on the anti-oxidative stress, anti-inflammatory effects, protein transport and application of lutein isomers[D]. Wuxi: Jiangnan University, 2023.
    [36]
    WANG R, WEN Q H, ZENG X A, et al. Binding affinity of curcumin to bovine serum albumin enhanced by pulsed electric field pretreatment[J]. Food Chemistry,2022,377:131945. doi: 10.1016/j.foodchem.2021.131945
    [37]
    ZHANG S, LI Y, BAO Z, et al. Internal cavity amplification of shell-like ferritin regulated with the change of the secondary and tertiary structure induced by PEF technology[J]. International Journal of Biological Macromolecules,2021,182:849−857. doi: 10.1016/j.ijbiomac.2021.04.072

Catalog

    Article Metrics

    Article views (35) PDF downloads (12) Cited by()

    /

    DownLoad:  Full-Size Img  PowerPoint
    Return
    Return