Abstract
This study investigated the effects of ultrasound-assisted thermo-alkali modification on the molecular structure of peanut protein. Further, the preparation conditions involved in embedding curcumin by the modified pea protein were also studied. It was found that within the pH range of 7 < pH < 11, with an increase in pH, the content of free sulfhydryl group in peanut protein isolate gradually increased from 10.35 ± 0.63 μmol/g (pH = 7) to 18.26 ± 0.93 μmol/g (pH = 10); and the content of disulfide bonds decreased from 44.62 ± 0.48 μmol/g (pH = 7) to 34.26 ± 2.03 μmol/g (pH = 11). In the ultrasonic power range (P < 300 W), with an increase in power, the content of free mercapto group in peanut protein isolate gradually increased from 12.44 ± 0.73 μmol/g to 19.46 ± 0.24 μmol/g (P = 250 W); and the content of disulfide bonds decreased from 42.29 ± 1.24 μmol/g to 33.28 ± 0.64 μmol/g (P = 300 W). Within the temperature range of 70 °C < T < 90 °C, with an increase in temperature, the content of free sulfhydryl group in peanut protein isolate gradually increased from 10.35 ± 0.94 μmol/g (T = 70 °C) to 19.67 ± 0.68 μmol/g (T = 90 °C), and the content of disulfide bonds decreased from 45.02 ± 2.84 μmol/g (T = 70 °C) to 34.26 ± 2.03 μmol/g (T = 90 °C). Response surface test was used to optimize the preparation conditions of nanoparticles from curcumin. The results showed that the optimum parameters of ultrasonic-assisted modification of peanut protein embedding curcumin were pH = 9.8, heating temperature T = 90 °C, ultrasonic power Q = 225 W, and heating time S = 21 min. Under these conditions, the embedding rate of curcumin reached 83.27 + 1.06%, the ABTS+ scavenging activity generally decreases with time over the 2 days period measured in PPI solution and PPI nanoparticles (PPN), the ABTS+ scavenging activity decreased from 40.8%, 52.2% and 67.3% to 27.1%, 39.0% and 60.5%, respectively. Compared with pure curcumin, the antioxidant activity was increased at presence of PPI.
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References
Beveridge T, Tomas J, Nakai S (1974) Determination of SH- and SS- groups in some food proteins using Ellman’s reagent. J Food Sci 39(2):49–51
Chang HM, Cheng-Fang T, Chin-Fung L (1999) Inhibition of lysinoalanine formation in alkali-pickled duck egg (Pidan). Food Res Int 32(2):559–563. https://doi.org/10.1016/s0963-9969(99)00131-3
Chen FP, Li BS, ChuanH T (2015) Nanocomplexation of soy protein isolate with curcumin: influence of ultrasonic treatment. Food Res Int 75:157–165. https://doi.org/10.1016/j.foodres.2015.06.009
Chen L, Ettelaie R, Akhtar M (2019) Improved enzymatic accessibility of peanut protein isolate pre-treated using thermosonication. Food Hydrocolloids 93:308–316. https://doi.org/10.1016/j.foodhyd.2019.02.050
Gómez-Mascaraque LG, Sipoli CC, de La Torre LG, López-Rubio A (2017) Microencapsulation structures based on protein-coated liposomes obtained through electrospraying for the stabilization and improved bioaccessibility of curcumin. Food Chem 233:343–350. https://doi.org/10.1016/j.foodchem.2017.04.133
Gong KJ, Shi AM, Liu HZ, Liu L, Hu H, Adhikari B, Wang Q (2016) Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate. J Food Eng 170:33–40. https://doi.org/10.1016/j.jfoodeng.2015.09.011
Gong K, Chen L, Xia H, Dai H, Li X, Sun L, Kong W, Liu K (2019) Driving forces of disaggregation and reaggregation of peanut protein isolates in aqueous dispersion induced by high-pressure microfluidization. Int J Biol Macromol 130:915–921. https://doi.org/10.1016/j.ijbiomac.2019.02.123
Guo CF, Zhang ZN, Liu Y (2019) Effects of radio frequency heating temperature on functional proteins and structure changes of soy preotein isolate. J Chin Inst Food Sci Technol 03(2):42–48
Horiuchi S, Winter G (2015) CMC determination of nonionic surfactants in protein formulations using ultrasonic resonance technology. Eur J Pharm Biopharm 92:8–14. https://doi.org/10.1016/j.ejpb.2015.02.005
Hu Y, Sun-Waterhouse D, Liu L, He W, Zhao M, Su G (2019) Modification of peanut protein isolate in glucose-containing solutions during simulated industrial thermal processes and gastric-duodenal sequential digestion. Food Chem 295:120–128. https://doi.org/10.1016/j.foodchem.2019.04.115
James H, Carlsson NG, Jönsson E, Sundell K, Undeland I (2019) Aquafeed ingredient production from herring (Clupea harengus) by-products using pH-shift processing: effect from by-product combinations, protein solubilization-pH and centrifugation force. Anim Feed Sci Technol 247:273–284. https://doi.org/10.1016/j.anifeedsci.2018.07.014
Kim HK, Kim YH, Kim YE, Jung SK, Lee NH, Song KM (2018) Effects of salts on ultrasonic extraction of protein from porcine myocardium. Food Bioprod Process 108:12–17. https://doi.org/10.1016/j.fbp.2017.12.002
Li W, Mengzhou Z, Ning X, Yong H, Chao W, Deyuan L, Liegang L, Dongsheng L (2016) Comparative analysis of protective effects of curcumin, curcumin-β-cyclodextrin nanoparticle and nanoliposomal curcumin on unsymmetrical dimethyl hydrazine poisoning in mice. Bioengineered 7(22):334–341. https://doi.org/10.1080/21655979.2016.1197029
Li W, Shugang L, Yong H, Mengzhou Z, Chao W, Li DS, Li DY (2019) Impact of hot alkali modification conditions on secondary structure of peanut protein and embedding rate of curcumin. Food Sci Human Wellness. https://doi.org/10.1016/j.fshw.2019.05.004
Liu Y, Liu D, Zhu L, Gan Q, Le X (2015) Temperature-dependent structure stability and in vitro release of chitosan-coated curcumin liposome. Food Res Int 74:97–105. https://doi.org/10.1016/j.foodres.2015.04.024
Ma T, Zhu H, Wang J, Wang Q, Yu LL, Sun B (2017) Influence of extraction and solubilizing treatments on the molecular structure and functional properties of peanut protein. LWT-Food Sci Technol 79:197–204. https://doi.org/10.1016/j.lwt.2017.01.037
María L, Prado-Audelo D, Caballero-Florán Isaac H, Meza-Toledo Jorge A, Mendoza-Muñoz Néstor, González-Torres Maykel, Florán Benjamín, Cortés Hernán, Leyva-Gómez Gerardo (2019) Formulations of curcumin nanoparticles for brain diseases. Biomolecules 9:56–57. https://doi.org/10.3390/biom9020056
Mehdi A, Masoud R, Ali J, Ingrid U (2017) Dynamic rheological, microstructural and physicochemical properties of blend fish protein recovered from kilka (Clupeonella cultriventris) and silver carp (Hypophthalmichthys molitrix) by the pH-shift process or washing-based technology. Food Chem 229(2):695–709. https://doi.org/10.1016/j.foodchem.2017.02.133
Ning F, Wang X, Zheng H, Zhang K, Bai C, Peng H, Huang Q, Xiong H (2019) Improving the bioaccessibility and in vitro absorption of 5-demethylnobiletin from chenpi by se-enriched peanut protein nanoparticles-stabilized pickering emulsion. J Funct Food 55:76–85. https://doi.org/10.1016/j.jff.2019.02.019
Patroklos V, Hultin Herbert O, Wesley RA (2008) Hemoglobin-mediated lipid oxidation of protein isolates obtained from cod and haddock white muscle as affected by citric acid, calcium chloride and pH. Food Chem 108(10):64–74. https://doi.org/10.1016/j.foodchem.2007.10.043
Paul MB, Ioana C, Adriana EB, Ioana CB, Raluca MP, Dan G, Sorana DB (2019) Effects of curcumin nanoparticles in isoproterenol-induced myocardial infarction. Oxid Med Cell Longev. https://doi.org/10.1155/2019/7847142
Sui X, Shuang B, Baokun Q, Zhongjiang W, Min Z, Yang L, Lianzhou J (2017) Impact of ultrasonic treatment on an emulsion system stabilized with soybean protein isolate and lecithin: its emulsifying property and emulsion stability. Food Hydrocolloids 63(10):727–734. https://doi.org/10.1016/j.foodhyd.2016.10.024
Sun LC, Yi-Chen L, Wei-Feng L, Xu-Jian Q, Kai-Yuan C, Guang-Ming L, Min-Jie C (2019) Effect of pH shifting on conformation and gelation properties of myosin from skeletal muscle of blue round scads (Decapterus maruadsi). Food Hydrocolloids 93(2):137–145. https://doi.org/10.1016/j.foodhyd.2019.02.026
Taoran W, Xiaoyu M, Yu L, Yangchao L (2016) Solid lipid nanoparticles coated with cross-linked polymeric double layer for oral delivery of curcumin. Colloid Surf B-Biointerfaces 148(8):1–11. https://doi.org/10.1016/j.colsurfb.2016.08.047
Teresa E, Angela L, Eleonora H, Marcella C, Pasquale T, Bruno V, Germano G, Antonio D, Angelica P (2019) Effects of curcumin and its adjuvant on TPC1 thyroid cell line. Chem-Biol Interact 305(3):112–118. https://doi.org/10.1016/j.cbi.2019.03.031
Typek R, Dawidowicz AL, Bernacik K, Stankevič M (2019) Feruloyloacetone can be the main curcumin transformation product. Food Chem 286:136–140. https://doi.org/10.1016/j.foodchem.2019.01.194
Wang ZJ, Jiang LZ (2012) Raman spectral analysis of soy protein isolate at various pH. Sci Technol Food Ind 33(6):63–66
Wang R, Jingyuan L, Shuntang G (2018) Binding of phytate to soybean protein during the heat treatment of soymilk and its effect on protein aggregation. Food Hydrocolloids 84(6):368–378. https://doi.org/10.1016/j.foodhyd.2018.06.031
Yonar ME, Yonar SM, İspir Ü, Ural MŞ (2019) Effects of curcumin on haematological values, immunity, antioxidant status and resistance of rainbow trout (Oncorhynchus mykiss) against Aeromonas salmonicida subsp. achromogenes. Fish Shellfish Immunol 89:83–90. https://doi.org/10.1016/J.FSI.2019.03.038
Zeng J, Yang Y, Liu-Lin L (2019) Research progress on the dissociation association behavior of 11S glycinin during heat treatment. Food Sci 1–14. http://kns.cnki.net/kcms/detail/11.2206.ts.20181009.1512.064.html
Zhang Q, Chen F (2019) The effects of reverse micelle on the structure and physicochemical properties of soybean protein Isolate. Food Sci 1–7. http://kns.cnki.net/kcms/detail/11.2206.ts.20180622.1106.134.html
Zhang Y, Wei Z, Ruijin Y, Mohammed AA, Xiao H, Wenbin Z, Yiqi Z (2013) Preparation and functional properties of protein from heat-denatured soybean meal assisted by steam flash-explosion with dilute acid soaking. J Food Eng 119(5):56–64. https://doi.org/10.1016/j.jfoodeng.2013.05.008
Zhang QT, Tu ZC, Xiao H, Wang H, Huang XQ, Liu GX, Liu CM, Shi Y, Fan LL, Lin DR (2014) Influence of ultrasonic treatment on the structure and emulsifying properties of peanut protein isolate. Food Bioprod Process 92(1):30–37. https://doi.org/10.1016/j.fbp.2013.07.006
Zhang Y, Si C, Baokun Q, Xiaonan S, Lianzhou J (2018) Complexation of thermally-denatured soybean protein isolate with anthocyanins and its effect on the protein structure and in vitro digestibility. Food Res Int 106(1):619–625. https://doi.org/10.1016/j.foodres.2018.01.040
Zhao X, Liu H, Zhang X, Zhu H, Ao Q (2019) Surface structure and volatile characteristic of peanut proteins obtained through AOT reverse micelles. Colloids Surf B 173:860–868. https://doi.org/10.1016/j.colsurfb.2018.10.070
Zheng B, Zipei Z, Fang C, Xiang L, McClements David J (2017) Impact of delivery system type on curcumin stability: comparison of curcumin degradation in aqueous solutions, emulsions, and hydrogel beads. Food Hydrocolloids 71(5):187–197. https://doi.org/10.1016/J.FOODHYD.2017.05.022
Acknowledgements
We gratefully acknowledge the financial support received from Natural Science Foundation of China (Grant Number 31901643).This work was also financially supported by The foundation for young scientists of Hubei province (Grant Number Q20171401), the foundation for Doctoral startup project of Hubei University of Technology (Grant Number 411500028).
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Li, W., Shi, Y., Hu, Y. et al. Study on condition of ultrasound-assisted thermo-alkali-modified peanut protein embedding curcumin for nanoparticles. J Food Sci Technol 57, 1049–1060 (2020). https://doi.org/10.1007/s13197-019-04139-0
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DOI: https://doi.org/10.1007/s13197-019-04139-0