Interaction mechanism between soybean protein isolate and citrus pectin.
citrus pectin
fluorescence spectrum
interaction
soybean protein isolate
Journal
Journal of food science
ISSN: 1750-3841
Titre abrégé: J Food Sci
Pays: United States
ID NLM: 0014052
Informations de publication
Date de publication:
Jun 2022
Jun 2022
Historique:
revised:
06
02
2022
received:
10
08
2021
accepted:
11
02
2022
pubmed:
6
5
2022
medline:
24
6
2022
entrez:
5
5
2022
Statut:
ppublish
Résumé
In this study, citrus pectin (CP) and soybean protein isolate (SPI) were used as raw materials to prepare a complex. The interaction mechanism and structural changes between SPI and CP were deeply studied by fluorescence spectroscopy and Fourier infrared spectroscopy. The results show that CP has a strong quenching effect on SPI's endogenous fluorescence, and with the addition of CP, the endogenous fluorescence intensity of SPI decreased from 13,565.2 to 6067.3. The CP quenching of SPI is static quenching, and the number of combined bits is 1.26. The results of three-dimensional fluorescence spectra showed that the addition of CP reduced the polarity of SPI amino acid residue microenvironment and changed the protein structure. Hydrophobic interaction exists between CP and SPI. The results of three-dimensional fluorescence spectra showed that the addition of CP reduced the polarity of the amino acid residue microenvironment of SPI and changed the protein structure. Fourier transform infrared spectroscopy shows that CP could change the secondary structure of SPI by decreasing the α-helix and β-sheet, increasing β-rotation and irregular curl, destroying the ordered structure of SPI and increasing the polarity of the amino acids exposed to the solution. The microstructure analysis shows that SPI-CP composite system has honeycomb structure and dense pores. From the perspective of reaction thermodynamics, it was found that the addition of CP could improve the thermal stability of SPI and increase the denaturation temperature of SPI from 119.73 to 132.97°C. This study can provide a theoretical basis for the preparation of protein-pectin complexes and provides reference for their application in food grade gels and Pickering emulsions.
Identifiants
pubmed: 35510685
doi: 10.1111/1750-3841.16108
doi:
Substances chimiques
Amino Acids
0
Emulsions
0
Soybean Proteins
0
citrus pectin
47EQO8LE7H
Pectins
89NA02M4RX
Types de publication
Journal Article
Langues
eng
Sous-ensembles de citation
IM
Pagination
2538-2548Informations de copyright
© 2022 Institute of Food Technologists®.
Références
Arroyo-Maya, I. J., Campos-Terán, J., Hernández-Arana, A., & McClements, D. J. (2016). Characterization of flavonoid-protein interactions using fluorescence spectroscopy: Binding of pelargonidin to dairy proteins. Food Chemistry, 223, 431-439. https://doi.org/10.1016/j.foodchem.2016.06.105
Chanphai, & Tajmir-Riahi. (2019). Tea polyphenols bind serum albumins: A potential application for polyphenol delivery. Food Hydrocolloids, 89, 461-467. https://doi.org/10.1016/j.foodhyd.2018.11.008
Chen, C., Sun-Waterhouse, D., & Zhao, J. (2021). Soybean protein isolate hydrolysates-liposomes interactions under oxidation: Mechanistic insights into system stability. Food Hydrocolloids, 112, 106336. https://doi.org/10.1016/j.foodhyd.2020.106336
Coloma, A., Del Pozo, M., Martínez-Moro, R., Blanco, E., Atienzar, P., Sánchez, L., Petit-Domínguez, M. D., Casero, E., & Quintana, C. (2021). MoS2 quantum dots for on-line fluorescence determination of the food additive allura red in beverage. Food Chemistry, 345, 128628. https://doi.org/10.1016/j.foodchem.2020.128628
Condict, L., Hung, A., Ashton, J., & Kasapis, S. (2021). High-temperature binding parameters and molecular dynamics of 4-hydroxybenzoic acid and β-casein complexes, determined via the method of continuous variation and fluorescence spectroscopy. Food Hydrocolloids, 114, 106567. https://doi.org/10.1016/j.foodhyd.2020.106567
Dai, L., Sun, C., Wei, Y., Zhan, X., Mao, L., & Gao, Y. (2018). Formation and characterization of zein-propylene glycol alginate-surfactant ternary complexes: Effect of surfactant type. Food Chemistry, 258, 321-330. https://doi.org/10.1016/j.foodchem.2018.03.077
Fan, C., Chen, X., & He, J. (2020). Effect of calcium chloride on emulsion stability of methyl-esterified citrus pectin. Food Chemistry, 332, 127366. https://doi.org/10.1016/j.foodchem.2020.127366
Guo, Q., Shu, X., Hu, Y., Su, J., Chen, S., Decker, E. A., & Gao, Y. (2021). Formulated protein-polysaccharide-surfactant ternary complexes for co-encapsulation of curcumin and resveratrol: Characterization, stability and in vitro digestibility. Food Hydrocolloids, 111, 106265. https://doi.org/10.1016/j.foodhyd.2020.106265
Guo, Q., Su, J., Shu, X., Shu, X., Yuan, F., Mao, L., & Gao, Y. (2020). Development of high methoxyl pectin-surfactant-pea protein isolate ternary complexes: Fabrication, characterization and delivery of resveratrol. Food Chemistry, 321, 126706. https://doi.org/10.1016/j.foodchem.2020.126706
Guo, Y., Bao, Y.-H., Chang, C., & Liu, W.-F. (2021). Effects of covalent interactions and gel characteristics on soy protein-tannic acid conjugates prepared under alkaline conditions. Food Hydrocolloids, 112, 106293. https://doi.org/10.1016/j.foodhyd.2020.106293
Hua, X., Jinran, L., Shuyi, G., Tian , J., Wang , M., & Yang , R. (2020). Surface activity of ultrahigh methoxylated pectin of different size. Food Hydrocolloids, 113, 106495. https://doi.org/10.1016/j.foodhyd.2020.106495
Khairul, A. B., & Feroz, S. R. (2019). A critical view on the analysis of fluorescence quenching data for determining ligand-protein binding affinity. Spectrochimica Acta Part A: Molecular and Biomolecular Spectroscopy, 223, https://doi.org/10.1016/j.saa.2019.117337
Li, J., Li, Y., & Guo, S. (2014). The binding mechanism of lecithin to soybean 11S and 7S globulins using fluorescence spectroscopy. Food Science and Biotechnology, 23(6), 1785-1791. https://doi.org/10.1007/s10068-014-0244-8
Li, Y., Liu, B., Jiang, L., Regenstein, J. M., Jiang, N., Poias, V., Zhang, X., Qi, B., Li, A., & Wang, Z. (2019). Interaction of soybean protein isolate and phosphatidylcholine in nanoemulsions: A fluorescence analysis. Food Hydrocolloids, 87, 814-829. https://doi.org/10.1016/j.foodhyd.2018.09.006
Luo, Y., Shen, H., Pan, D., & Bu, G. (2008). Gel properties of surimi from silver carp (Hypophthalmichthys molitrix) as affected by heat treatment and soy protein isolate. Food Hydrocolloids, 22(8), 1513-1519. https://doi.org/10.1016/j.foodhyd.2007.10.003
Ma, X., Chen, W., Yan, T., Wang, D., Hou, F., Miao, S., & Liu, D. (2020). Comparison of citrus pectin and apple pectin in conjugation with soy protein isolate (SPI) under controlled dry-heating conditions. Food Chemistry, 309, 125501. https://doi.org/10.1016/j.foodchem.2019.125501
Ma, X., Yan, T., Hou, F., Chen, W., Miao, S., & Liu, D. (2019). Formation of soy protein isolate (SPI)-citrus pectin (CP) electrostatic complexes under a high-intensity ultrasonic field: Linking the enhanced emulsifying properties to physicochemical and structural properties. Ultrasonics Sonochemistry, 59, 104748. https://doi.org/10.1016/j.ultsonch.2019.104748
Miriani, M., Keerati-U-Rai, M., Corredig, M., Iametti, S., & Bonomi, F. (2010). Denaturation of soy proteins in solution and at the oil-water interface: A fluorescence study. Food Hydrocolloids, 25(4), 620-626. https://doi.org/10.1016/j.foodhyd.2010.07.020
Miwa, N., Yokoyama, K., Nio, N., & Sonomoto , K. (2013). Effect of enzymatic deamidation on the heat-induced conformational changes in whey protein isolate and its relation to gel properties. Journal of Agricultural and Food Chemistry, 61(9), 2205-2212. https://doi.org/10.1021/jf3047626
Molina Ortiz, S. E., Puppo, M. C., & Wagner, J. R. (2004). Relationship between structural changes and functional properties of soy protein isolates-carrageenan systems. Food Hydrocolloids, 18(6), 1045-1053. https://doi.org/10.1016/j.foodhyd.2004.04.011
Nawrocka, A., Szymańska-Chargot, M., Miś, A., Wilczewska, A. Z., & Markiewicz, K. H. (2017). Effect of dietary fibre polysaccharides on structure and thermal properties of gluten proteins-A study on gluten dough with application of FT-Raman spectroscopy, TGA and DSC. Food Hydrocolloids, 69, 410-421. https://doi.org/10.1016/j.foodhyd.2017.03.012
Ningtyas, D. W., Tam, B., Bhandari, B., & Prakash, S. (2020). Effect of different types and concentrations of fat on the physico-chemical properties of soy protein isolate gel. Food Hydrocolloids, 111, 106226. https://doi.org/10.1016/j.foodhyd.2020.106226
Ozde, Z. G., Cansu, C., & Banu, A. K. (2018). Theophylline-loaded pectin-based hydrogels. I. Effect of medium pH and preparation conditions on drug release profile. Journal of Applied Polymer Science, 135(38), 274-285. https://doi.org/10.1002/app.46731
Pillai, P. K. S., Stone, A. K., Guo, Q., Guo, Q., Wang, Q., & Nickerson, M. T. (2019). Effect of alkaline de-esterified pectin on the complex coacervation with pea protein isolate under different mixing conditions. Food Chemistry, 284, 227-235. https://doi.org/10.1016/j.foodchem.2019.01.122
Porras-Saavedra, J., Palacios-González, E., Lartundo-Rojas, L., Garibay-Febles, V., Yáñez-Fernández, J., Hernández-Sánchez, H., Gutiérrez-López, G., & Alamilla-Beltrán, L. (2015). Microstructural properties and distribution of components in microparticles obtained by spray-drying. Journal of Food Engineering, 152, 105-112. https://doi.org/10.1016/j.jfoodeng.2014.11.014
Raei, M., Shahidi, F., Farhoodi, M., Jafari, S. M., & Rafe, A. (2017). Application of whey protein-pectin nano-complex carriers for loading of lactoferrin. International Journal of Biological Macromolecules, 105, 281-291. https://doi.org/10.1016/j.ijbiomac.2017.07.037
Romdhane, M. H., Beltifa, A., Mzoughi, Z., Rihouey, C., Ben Mansour, H., Majdoub, H., & Le Cerf, D. (2020). Optimization of extraction with salicylic acid, rheological behavior and antiproliferative activity of pectin from Citrus sinensis peels. International Journal of Biological Macromolecules, 159, 547-556. https://doi.org/10.1016/j.ijbiomac.2020.05.125
Sharma, P., Dube, D., Singh, A., Mishra, B., Singh, N., Sinha, M., Dey, S., Kaur, P., Mitra, D. K., Sharma, S., & Singh, T. P. (2011). Structural basis of recognition of pathogen-associated molecular patterns and inhibition of proinflammatory cytokines by camel peptidoglycan recognition protein. Journal of Biological Chemistry, 286(18), P16208-16217. https://doi.org/10.1074/jbc.M111.228163
Song, Y., & Sang-Ho, Y. (2017). Quality improvement of a rice-substituted fried noodle by utilizing the protein-polyphenol interaction between a pea protein isolate and green tea (Camellia sinensis) extract. Food Chemistry, 235, 181-187. https://doi.org/10.1016/j.foodchem.2s017.05.052
Souza, A. C. P., Gurak, P. D., & Marczak, L. D. F. (2017). Maltodextrin, pectin and soy protein isolate as carrier agents in the encapsulation of anthocyanins-rich extract from jaboticaba pomace. Food and Bioproducts Processing, 102, 186-194. https://doi.org/10.1016/j.fbp.2016.12.012
Svilenov, H. L., & Winter, G. (2020). Formulations that suppress aggregation during long-term storage of a bispecific antibody are characterized by high refoldability and colloidal stability. Journal of Pharmaceutical Sciences, 109(6), P2048-2058. https://doi.org/10.1016/j.xphs.2020.03.011
Tamnak, S., Mirhosseini, H., Tan, C. P., Ghazali, H. M., & Muhammad, K. (2016). Physicochemical properties, rheological behavior and morphology of pectin-pea protein isolate mixtures and conjugates in aqueous system and oil in water emulsion. Food Hydrocolloids, 56, 405-416. https://doi.org/10.1016/j.foodhyd.2015.12.033
Wang, S., Lu, Y., Ouyang, X.-K., & Ling, J. (2020). Fabrication of soy protein isolate/cellulose nanocrystal composite nanoparticles for curcumin delivery. International Journal of Biological Macromolecules, 165, 1468-1474. https://doi.org/10.1016/j.ijbiomac.2020.10.046
Wang, X., Zhang, G., Yu, D., Wang, N., & Guan, Q. (2021). The interaction of folate-modified Bletilla striata polysaccharide-based micelle with bovine serum albumin. Glycoconjugate Journal, 38, 585-597. https://doi.org/10.1007/S10719-021-10022-Y
Xiang, Y., & Wu, F. (2010). Study of the interaction between a new Schiff-base complex and bovine serum albumin by fluorescence spectroscopy. Spectrochimica Acta Part A Molecular & Biomolecular Spectroscopy, 77(2), 430-436. https://doi.org/10.1016/j.saa.2010.06.010
Yan, J.-K., Wang, C., Qiu, W.-Y., Chen, T.-T., Yang, Y., Wang, W.-H., & Zhang, H.-N. (2021). Ultrasonic treatment at different pH values affects the macromolecular, structural, and rheological characteristics of citrus pectin. Food Chemistry, 341(01), 128216. https://doi.org/10.1016/j.foodchem.2020.128216
Yan, S., Xie, F., Zhang, S., Jiang, L., Qi, B., & Li, Y. (2020). Effects of soybean protein isolate-polyphenol conjugate formation on the protein structure and emulsifying properties: Protein-polyphenol emulsification performance in the presence of chitosan. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 609, 125641. https://doi.org/10.1016/j.colsurfa.2020.125641
Yan, W., Jia, X., Zhang, Q., Chen, H., Zhu, Q., & Yin, L. (2021). Interpenetrating polymer network hydrogels of soy protein isolate and sugar beet pectin as a potential carrier for probiotics. Food Hydrocolloids, 113, 106453. https://doi.org/10.1016/j.foodhyd.2020.106453
Yin, Z., Wu, Y., Chen, Y., Qie, X., Zeng, M., Wang, Z., Qin, F., Chen, J., & He, Z. (2021). Analysis of the interaction between cyanidin-3-O-glucoside and casein hydrolysates and its effect on the antioxidant ability of the complexes. Food Chemistry, 340, 127915. https://doi.org/10.1016/j.foodchem.2020.127915
Zhao, X., Chen, F., Xue, W., & Lee, L. (2007). FTIR spectra studies on the secondary structures of 7S and 11S globulins from soybean proteins using AOT reverse micellar extraction. Food Hydrocolloids, 22(4), 568-575. https://doi.org/10.1016/j.foodhyd.2007.01.019