大豆蛋白-黄芩素的结合机制及蛋白构象和功能的变化

食品科学 ›› 0, Vol. ›› Issue (): 0-0.

• 食品化学 • 下一篇

大豆蛋白-黄芩素的结合机制及蛋白构象和功能的变化

闫馨月¹,贾亦佳¹,孙诗艳¹,张东蒙¹,耿梦洁¹,杨晋杰²,Stanislav Sukhikh³,Olga Babich⁴,李杨⁵,齐宝坤⁵

1. 东北农业大学
2. 渤海大学
3. 康德波罗的海联邦大学
4. 康德波罗的海大学
5. 东北农业大学食品学院

收稿日期:2022-05-20 修回日期:2022-12-19 出版日期:2023-02-25 发布日期:2023-02-25
通讯作者: 李杨 E-mail:yangli@neau.edu.cn
基金资助:
大豆产业技术体系岗位科学家项目

Exploring the Binding Mechanism of Soybean Protein-Baicalein Including Changes in Protein Conformation and Function

Xin-Yue YAN ², ², ², ²,Jinjie Yang ²,Babich Olga³,li yang ²

Received:2022-05-20 Revised:2022-12-19 Online:2023-02-25 Published:2023-02-25
Contact: li yang E-mail:yangli@neau.edu.cn
Supported by:
the Post System Scientist of Ministry of Agriculture

摘要/Abstract

摘要： 探索大豆蛋白组分中β-伴大豆蛋白（7S）/大豆蛋白（11S）与黄芩素的结合机制，考察复合物构象及功能特性的变化。傅里叶变换红外光谱表明黄芩素诱导蛋白的β-折叠转化为α-螺旋和无规卷曲。内源荧光光谱证实了黄芩素的加入使7S、11S结构变得更紧密。黄芩素与蛋白的反应自发进行，并通过静态方式淬灭蛋白荧光。7S、11S蛋白分别通过氢键和疏水相互作用与黄芩素结合。分子对接结果表明，黄芩素对11S的亲和力高于7S。扫描电子显微镜显示了7S、11S与复合物的微观结构差异。此外，与黄芩素结合后，7S、11S的表面疏水性下降，热稳定性及其他功能特性提升。

关键词: β-伴大豆蛋白（7S）, 大豆蛋白（11S）, 黄芩素, 结合机制, 构象变化, 功能特性

Abstract: To explore the binding mechanism of β-conglycinin (7S)/glycinin (11S) in soybean protein components with baicalein, and to investigate the changes of the conformation and functional properties of the complex. Fourier transform infrared spectroscopy indicated that baicalein induced the transformation of β-sheets into α-helices and random coils. Intrinsic fluorescence spectra confirmed that the addition of baicalein made the 7S、11S structure tighter. The reaction of baicalein with the protein proceeded spontaneously and quenched the protein fluorescence in a static manner. The 7S、11S proteins bound to baicalein by hydrogen bonds and hydrophobic interactions, respectively. The affinity of baicalein to 11S was higher than that of 7S by molecular docking. Scanning electron microscopy showed the microstructure difference between 7S、11S and complex. In addition, the surface hydrophobicity of 7S、11S decreased and the thermal stability and other functional properties of complex were improved after combining with baicalein.

Key words: β-conglycinin (7S), glycinin (11S), baicalein, binding mechanism, conformational change, functional properties

中图分类号:

TS.214.2

闫馨月贾亦佳孙诗艳张东蒙耿梦洁杨晋杰 Stanislav Sukhikh Olga Babich 李杨齐宝坤. 大豆蛋白-黄芩素的结合机制及蛋白构象和功能的变化[J]. 食品科学, 0, (): 0-0.

Xin-Yue YAN Jinjie Yang Babich Olga li yang. Exploring the Binding Mechanism of Soybean Protein-Baicalein Including Changes in Protein Conformation and Function[J]. FOOD SCIENCE, 0, (): 0-0.

参考文献

[1] Nishinari K, Fang Y, Guo S, et al.Soy proteins: A review on composition, aggregation and emulsification[J].Food hydrocolloids, 2014, 39:301-318
[2]Wu C, Hua Y, Chen Y, et al.Effect of 7S11S ratio on the network structure of heat-induced soy protein gels: A study of probe release[J].RSC advances, 2016, 6(104):101981-101987
[3] Wu C, Hua Y, Chen Y, et al.Effect of temperature, ionic strength and 11S ratio on the rheological properties of heat-induced soy protein gels in relation to network proteins content and aggregates size[J].Food Hydrocolloids, 2017, 66:389-395
[4] 张麒, 吴海波, 颜文文, 等.大豆7S与11S蛋白理化特性及其改性修饰的研究进展[J].2022, , :1-14
[5]邱爽, 牟佳佳, 邓雁如.黄芩素的结构修饰及其药理活性研究进展[J].中国药物化学杂志, 2021, 31(05):390-399
[6] Ojha H, Mishra K, Hassan M I, et al.Spectroscopic and isothermal titration calorimetry studies of binding interaction of ferulic acid with bovine serum albumin[J].Thermochimica Acta, 2012, 548:56-64
[7] Jiang J, Zhang Z, Zhao J, et al.The effect of non-covalent interaction of chlorogenic acid with whey protein and casein on physicochemical and radical-scavenging activity of in vitro protein digests[J].Food Chemistry, 2018, 268:334-341
[8] Ye J, Deng L, Wang Y, et al.Impact of rutin on the foaming properties of soybean protein: Formation and characterization of flavonoid-protein complexes[J].Food Chemistry, 2021, 362(130238):-
[9] Parolia S, Maley J, Sammynaiken R, et al.Structure–Functionality of lentil protein-polyphenol conjugates[J].Food Chemistry, 2022, 367(130603):-
[10]Yildirim-Elikoglu S, Erdem Y K.Interactions between milk proteins and polyphenols: Binding mechanisms,related changes,and the future trends in the dairy industry[J].Food Reviews International, 2018, 34(7):665-697
[11]Liu C, Wang H, Cui Z, et al.Optimization of extraction and isolation for 11S and 7S globulins of soybean seed storage protein[J].Food Chemistry, 2007, 102(4):1310-1316
[12]Surewicz W K, Mantsch H H.New insight into protein secondary structure from resolution-enhanced infrared spectra[J].Biochimica et biophysica acta, 1988, 952(2):115-130
[13]Liu Y, Zhao G, Zhao M, et al.Improvement of functional properties of peanut protein isolate by conjugation with dextran through Maillard reaction[J].Food Chemistry, 2012, 131(3):901-906
[14] He S, Zhao J, Cao X, et al.Low pH-shifting treatment would improve functional properties of black turtle bean (Phaseolus vulgaris L.) protein isolate with immunoreactivity reduction[J].Food Chemistry, 2020, 330(127217):-
[15]Li C, Huang X, Peng Q, et al.Physicochemical properties of peanut protein isolate–glucomannan conjugates prepared by ultrasonic treatment[J].Ultrasonics Sonochemistry, 2014, 21(5):1722-1727
[16]Pearce K N, Kinsella J E.Emulsifying properties of proteins: evaluation of a turbidimetric technique[J].Journal of Agricultural and Food Chemistry, 1978, 26(3):716-723
[17] Sui X, Sun H, Qi B, et al.Functional and conformational changes to soy proteins accompanying anthocyanins: Focus on covalent and non-covalent interactions[J].Food Chemistry, 2018, 245:871-878
[18] Sun Y, Zhang S, Xie F, et al.Effects of covalent modification with epigallocatechin-3-gallate on oleosin structure and ability to stabilize artificial oil body emulsions[J].Food Chemistry, 2021, 341(128272):-
[19]王启明, 唐瑜婉, 杨雅轩, 等.值对麦醇溶蛋白-槲皮素相互作用及其乳液特性的影响[J].食品科学, 2020, 41(20):27-34
[20] Liu X, Song Q, Li X, et al.Effects of different dietary polyphenols on conformational changes and functional properties of protein–polyphenol covalent complexes[J].Food Chemistry , 2021, 361(130071):-
[21]李春翼, 王启明, 唐瑜婉, 等.热诱导对麦醇溶蛋白芦丁相互作用及其乳液流变学特性的影响[J].食品科学, 2020, 41(18):27-34
[22] Li H, Zhang X, Zhao C, et al.Entrapment of curcumin in soy protein isolate using the pH-driven method: Nanoencapsulation and formation mechanism[J].LWT, 2022, 153(112480):-
[23] Qiao X, Yang L, Gu J, et al.Kinetic interactions of nanocomplexes between astaxanthin esters with different molecular structures and β-lactoglobulin[J].Food Chemistry, 2021, 335(127633):-
[24]Lakowicz J R, Weber G.Quenching of fluorescence by oxygenProbe for structural fluctuations in macromolecules[J].Biochemistry, 1973, 12(21):4161-4170
[25]Ross P D, Subramanian S.Thermodynamics of protein association reactions: forces contributing to stability[J].Biochemistry, 1981, 20(11):3096-3102
[26]唐瑜婉, 王启明, 杨雅轩, 等.玉米醇溶蛋白-多酚纳米颗粒对乳液稳定性的调控[J].食品与发酵工业, 2019, 45(11):6-
[27] Ren C, Xiong W, Li J, et al.Comparison of binding interactions of cyanidin-3-O-glucoside to β-conglycinin and glycinin using multi-spectroscopic and thermodynamic methods[J].Food Hydrocolloids, 2019, 92:155-162
[28]Cao Y, Xiong Y L.Binding of gallic acid and epigallocatechin gallate to heat-unfolded whey proteins at neutral pH alters radical scavenging activity of in vitro protein digests[J].Journal of Agricultural and Food Chemistry, 2017, 65(38):8443-8450
[29] ZHU X, LI L, LI S, et al.L-arginine/L-lysine improves emulsion stability of chicken sausage by increasing electrostatic repulsion of emulsion droplet and decreasing the interfacial tension of soybean oil-water [J].Food hydrocolloids, 2019, 89:492-502
[30]TANG C H.Emulsifying properties of soy proteins: A critical review with emphasis on the role of conformational flexibility[J].Critical Reviews in Food Science & Nutrition, 2017, 57(12):2636-2679
[31] 汪婷婷.大米蛋白-鳕鱼蛋白复合纳米结构的构建及乳液稳定性研究[D].江南大学, 2021. DOI: 10.27169/d.cnki.gwqgu.2021.000724.
[32] 吴凡.物理加工对牡蛎（Ostrea edulis）蛋白结构和功能性质的影响[D].大连工业大学, 2019. DOI: 10.26992/d.cnki.gdlqc.2019.000260.
[33]李杨, 闫世长, 齐宝坤, 等.绿原酸改性黑芸豆蛋白抗氧化活性与乳化性能研究[J].农业机械学报, 2020, 51(05):356-362

大豆蛋白-黄芩素的结合机制及蛋白构象和功能的变化

Exploring the Binding Mechanism of Soybean Protein-Baicalein Including Changes in Protein Conformation and Function

PDF (PC)

可视化

摘要/Abstract

引用本文

使用本文

参考文献

相关文章 15

编辑推荐

Metrics

本文评价

[1]	胡丽筠，马旭华，李亚蕾，罗瑞明. 牛HSPA6蛋白特性分析及蛋白互作网络构建[J]. 食品科学, 2024, 45(3): 1-8.
[2]	陈腊梅, 唐善虎, 李思宁, 李锦锦, 李巧艳, 赵佳莹. 丙二醛氧化对牦牛肉肌原纤维蛋白结构及功能特性的影响[J]. 食品科学, 2023, 44(8): 46-54.
[3]	闫洪波, 楚英珂, 李雯慧, 张德景, 杨青, 位正鹏, 王宗敏, 王彦波, 朱兰兰. 海洋生物活性肽生物学和功能特性的研究进展[J]. 食品科学, 2023, 44(7): 18-28.
[4]	樊润泽，祁苗，张新颖，彭三三，赵欣怡，李卓，许德晖. 冷等离子体对肉蛋白的影响及其在肉品保藏加工中的应用研究进展[J]. 食品科学, 2023, 44(7): 250-259.
[5]	李艾黎，刘串，马艺鸣，王雪莹，李春，孙铭爽. 山羊乳及其制品营养与功能特性的研究进展[J]. 食品科学, 2023, 44(5): 212-221.
[6]	王欣卉，宋雪健，张东杰，李志江. 脂质组学技术及其在食品科学领域应用研究进展[J]. 食品科学, 2023, 44(5): 290-297.
[7]	李红娟，李梦凡，袁玉京，陈紫阳，朱广潮，李丹，李洪波，于景华,. 再制干酪乳化过程中理化、功能特性及微观结构的变化[J]. 食品科学, 2023, 44(4): 78-84.
[8]	闫馨月，贾亦佳，孙诗艳，张东蒙，耿梦洁，杨晋杰，Stanislav Sukhikh, Olga Babich，齐宝坤，李杨. 大豆蛋白-黄芩素的结合机制及蛋白构象和功能变化[J]. 食品科学, 2023, 44(4): 91-98.
[9]	王甜甜，朱逸宸，谢勇，周凯，廖鲜艳，黄俊逸，徐宝才. 肌红蛋白在加工贮藏过程中结构与功能特性的变化及其对肉制品色泽的影响研究进展[J]. 食品科学, 2023, 44(3): 393-399.
[10]	唐永欣, 彭松林, 郭晨晨, 徐毅, 尚永彪. 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.
[11]	陈欣彤, 邱毓, 杨若婷, 高金燕, 李欣, 陈红兵. 糖基化对乳制品加工性能及致敏性影响的研究进展[J]. 食品科学, 2023, 44(23): 383-393.
[12]	赵宇楠, 贾丹丹, 蔡丹, 王泽贤, 高飞, 刘景圣. 食用菌发酵对人参不溶性膳食纤维结构及功能特性的影响[J]. 食品科学, 2023, 44(22): 80-88.
[13]	曹佳兴，朱海兰，王君荣，张健豪，张国治. 超声功率对小麦醇溶蛋白-膳食多酚共价复合物结构及功能性质的影响[J]. 食品科学, 2023, 44(19): 65-73.
[14]	陈贵婷，石凯欣，张珮珮，徐阳，潘思轶. 不同品种柑橘皮渣膳食纤维构效关系比较[J]. 食品科学, 2023, 44(17): 20-28.
[15]	吴寒，刘浩男，邸清茹，夏依旦·买买提，刘小莉，周剑忠. 高功率脉冲微波协同花色苷对大豆分离蛋白理化特性的影响及其在蛋糕中的应用[J]. 食品科学, 2023, 44(17): 60-66.