Enzymatic hydrolysis; Gelation; Microstructure; Molecular characteristics; Quinoa protein; Rheological property; Formation mechanism; Physicochemical property; Property; Quinoa proteins; Safety problems; Self-assembled peptides; Self-assembly peptide; Synthesised; Food Science; Chemistry (all); Chemical Engineering (all); General Chemical Engineering; General Chemistry
Abstract :
[en] Currently, self-assembly peptides with hydrogel properties that are used in various applications are being chemically synthesized. These peptides not only have safety and environmental problems but are also expensive and cumbersome to prepare. The present study established a convenient and efficient method for producing plant-based peptides with decent gel-forming ability from quinoa proteins. After alkaline protease treatment, hydrogels made with quinoa protein hydrolysis exhibited potent self-assembly capacity, enhanced gel hardness, and improved rheological properties. Moreover, the microstructure results revealed that the quinoa peptide hydrogels had regular, uniform, and interconnected porous structures. These observations were primarily attributed to the hydrogen bonding force and hydrophobic aggregation caused by hydrophobic group exposure. Amino acid and proteomics analysis suggested that the amino acid composition and sequence of quinoa peptides significantly influenced the formation of self-assembled hydrogels. Overall, this study provided a cost-effective approach to improve the gelling ability of quinoa protein and could potentially replace the use of chemically synthesized peptides in various applications, laying the theoretical basis for the development of novel natural plant-based foods.
Disciplines :
Chemistry
Author, co-author :
Fan, Xin ; Université de Liège - ULiège > TERRA Research Centre ; Key Laboratory of Quality Evaluation and Nutrition Health of Agro-Products, Ministry of Agriculture and Rural Affairs, Institute of Crop Sciences, Chinese Academy of Agricultural Sciences, Beijing, China ; Key Laboratory of Coarse Cereal Processing, Ministry of Agriculture and Rural Affairs, School of Food and Biological Engineering, Chengdu University, Chengdu, China
Guo, Huimin; Key Laboratory of Quality Evaluation and Nutrition Health of Agro-Products, Ministry of Agriculture and Rural Affairs, Institute of Crop Sciences, Chinese Academy of Agricultural Sciences, Beijing, China ; Shanghai Key Laboratory of Agricultural Genetics and Breeding, Biotechnology Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, China ; Laboratory of Biomass and Green Technologies, Gembloux Agro-Bio Tech, University of Liège, Gembloux, Belgium
Richel, Aurore ; Université de Liège - ULiège > TERRA Research Centre > Technologie Alimentaire (TA)
Zhang, Lizhen; Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, School of Life Science, Shanxi University, Taiyuan, China
Liu, Chenghong ; Shanghai Key Laboratory of Agricultural Genetics and Breeding, Biotechnology Research Institute, Shanghai Academy of Agricultural Sciences, Shanghai, China
Qin, Peiyou ; Key Laboratory of Quality Evaluation and Nutrition Health of Agro-Products, Ministry of Agriculture and Rural Affairs, Institute of Crop Sciences, Chinese Academy of Agricultural Sciences, Beijing, China ; Key Laboratory of Coarse Cereal Processing, Ministry of Agriculture and Rural Affairs, School of Food and Biological Engineering, Chengdu University, Chengdu, China
Blecker, Christophe ; Université de Liège - ULiège > TERRA Research Centre > Technologie Alimentaire (TA)
Ren, Guixing; Key Laboratory of Quality Evaluation and Nutrition Health of Agro-Products, Ministry of Agriculture and Rural Affairs, Institute of Crop Sciences, Chinese Academy of Agricultural Sciences, Beijing, China ; Key Laboratory of Coarse Cereal Processing, Ministry of Agriculture and Rural Affairs, School of Food and Biological Engineering, Chengdu University, Chengdu, China ; Key Laboratory of Chemical Biology and Molecular Engineering of Ministry of Education, School of Life Science, Shanxi University, Taiyuan, China
Language :
English
Title :
Preparation, physicochemical properties, and formation mechanism of quinoa self-assembled peptide-based hydrogel
This work was supported by the Agricultural Science and Technology Innovation Program of the Chinese Academy of Agricultural Sciences (Grant No. CAAS-ASTIP-2022-ICS), Shanghai Pujiang Program (22PJD066), Shanghai “Science and Technology Innovation Action Plan” (22015810100), a postgraduate international exchange grant from the Chinese Academy of Agricultural Sciences and the China Scholarship Council ( CSC ). The authors would also like to thank Nicolas Jacquet, Lynn Doran and Marjorie Servais from the Teaching and Research Center, Gembloux, Belgium, for their guidance in this study.
Abugoch, L.E., Romero, N., Tapia, C.A., Silva, J., Rivera, M., Study of some physicochemical and functional properties of quinoa (Chenopodium quinoa willd) protein isolates. Journal of Agricultural and Food Chemistry 56:12 (2008), 4745–4750, 10.1021/jf703689u.
Beveridge, T., Toma, S.J., Nakai, S., Determination of SH- and SS-groups in some food proteins using Ellman's Reagent. Journal of Food Science 39:1 (1974), 49–51, 10.1111/j.1365-2621.1974.tb00984.x.
Bowerman, C.J., Nilsson, B.L., Review self-assembly of amphipathic β-sheet peptides: Insights and applications. Peptide Science 98:3 (2012), 169–184, 10.1002/bip.22058.
Brinegar, C., Goundan, S., Isolation and characterization of chenopodin, the 11S seed storage protein of quinoa (Chenopodium quinoa). Journal of Agricultural and Food Chemistry 41:2 (1993), 182–185, 10.1021/jf00026a006.
Brinegar, C., Sine, B., Nwokocha, L., High-cysteine 2S seed storage proteins from quinoa (Chenopodium quinoa). Journal of Agricultural and Food Chemistry 44:7 (1996), 1621–1623, 10.1021/jf950830+.
Chen, D., Campanella, O.H., Limited enzymatic hydrolysis induced pea protein gelation at low protein concentration with less heat requirement. Food Hydrocolloids, 128, 2022, 107547, 10.1016/j.foodhyd.2022.107547.
Daliri, H., Ahmadi, R., Pezeshki, A., Hamishehkar, H., Mohammadi, M., Beyrami, H., et al. Quinoa bioactive protein hydrolysate produced by pancreatin enzyme- functional and antioxidant properties. Lebensmittel-Wissenschaft & Technologie, 150, 2021, 111853, 10.1016/j.lwt.2021.111853.
De Leon Rodriguez, L.M., Hemar, Y., Prospecting the applications and discovery of peptide hydrogels in food. Trends in Food Science & Technology 104 (2020), 37–48, 10.1016/j.tifs.2020.07.025.
Elsohaimy, S.A., Refaay, T.M., Zaytoun, M.A.M., Physicochemical and functional properties of quinoa protein isolate. Annals of Agricultural Science 60:2 (2015), 297–305, 10.1016/j.aoas.2015.10.007.
Fu, K., Wu, H., Su, Z., Self-assembling peptide-based hydrogels: Fabrication, properties, and applications. Biotechnology Advances, 49, 2021, 107752, 10.1016/j.biotechadv.2021.107752.
Galante, M., De Flaviis, R., Boeris, V., Spelzini, D., Effects of the enzymatic hydrolysis treatment on functional and antioxidant properties of quinoa protein acid-induced gels. Lebensmittel-Wissenschaft & Technologie, 118, 2020, 108845, 10.1016/j.lwt.2019.108845.
Gosal, W.S., Ross-Murphy, S.B., Globular protein gelation. Current Opinion in Colloid & Interface Science 5:3 (2000), 188–194, 10.1016/S1359-0294(00)00057-1.
Liang, R., Zhang, H., Wang, Y., Ye, J., Guo, L., He, L., et al. Dual dynamic network system constructed by waterborne polyurethane for improved and recoverable performances. Chemical Engineering Journal, 442, 2022, 136204, 10.1016/j.cej.2022.136204.
Luo, L., Cheng, L., Zhang, R., Yang, Z., Impact of high-pressure homogenization on physico-chemical, structural, and rheological properties of quinoa protein isolates. Food Structure, 32, 2022, 100265, 10.1016/j.foostr.2022.100265.
Luo, L., Zhang, R., Palmer, J., Hemar, Y., Yang, Z., Impact of high hydrostatic pressure on the gelation behavior and microstructure of quinoa protein isolate dispersions. ACS Food Science & Technology 1:11 (2021), 2144–2151, 10.1021/acsfoodscitech.1c00332.
Mäkinen, O.E., Zannini, E., Koehler, P., Arendt, E.K., Heat-denaturation and aggregation of quinoa (Chenopodium quinoa) globulins as affected by the pH value. Food Chemistry 196 (2016), 17–24, 10.1016/j.foodchem.2015.08.069.
Ma, Z., Li, L., Wu, C., Huang, Y., Teng, F., Li, Y., Effects of combined enzymatic and ultrasonic treatments on the structure and gel properties of soybean protein isolate. Lebensmittel-Wissenschaft & Technologie, 158, 2022, 113123, 10.1016/j.lwt.2022.113123.
McClements, D.J., Newman, E., McClements, I.F., Plant-based milks: A review of the science underpinning their design, fabrication, and performance. Comprehensive Reviews in Food Science and Food Safety 18:6 (2019), 2047–2067, 10.1111/1541-4337.12505.
Nieto-Nieto, T.V., Wang, Y.X., Ozimek, L., Chen, L., Effects of partial hydrolysis on structure and gelling properties of oat globular proteins. Food Research International 55 (2014), 418–425, 10.1016/j.foodres.2013.11.038.
Ruiz, G.A., Xiao, W., van Boekel, M., Minor, M., Stieger, M., Effect of extraction pH on heat-induced aggregation, gelation and microstructure of protein isolate from quinoa (Chenopodium quinoa Willd). Food Chemistry 209 (2016), 203–210, 10.1016/j.foodchem.2016.04.052.
Saiani, A., Mohammed, A., Frielinghaus, H., Collins, R., Hodson, N., Kielty, C.M., et al. Self-assembly and gelation properties of α-helix versus β-sheet forming peptides. Soft Matter 5:1 (2009), 193–202, 10.1039/B811288F.
Shen, Y., Tang, X., Li, Y., Drying methods affect physicochemical and functional properties of quinoa protein isolate. Food Chemistry, 339, 2021, 127823, 10.1016/j.foodchem.2020.127823.
Wang, Y.-L., Yang, J.-J., Dai, S.-C., Tong, X.-H., Tian, T., Liang, C.-C., et al. Formation of soybean protein isolate-hawthorn flavonoids non-covalent complexes: Linking the physicochemical properties and emulsifying properties. Ultrasonics Sonochemistry, 84, 2022, 105961, 10.1016/j.ultsonch.2022.105961.
Xu, K., Wang, J., Discovering the effect of alum on UV photo-degradation of gelatin binder via FTIR, XPS and DFT calculation. Microchemical Journal, 149, 2019, 103934, 10.1016/j.microc.2019.05.034.
Yang, Z., de Campo, L., Gilbert, E.P., Knott, R., Cheng, L., Storer, B., et al. Effect of NaCl and CaCl2 concentration on the rheological and structural characteristics of thermally-induced quinoa protein gels. Food Hydrocolloids, 124, 2022, 107350, 10.1016/j.foodhyd.2021.107350.
Yin, S.-W., Tang, C.-H., Wen, Q.-B., Yang, X.-Q., Functional and conformational properties of phaseolin (phaseolus vulgris L.) and kidney bean protein isolate: A comparative study. Journal of the Science of Food and Agriculture 90:4 (2010), 599–607, 10.1002/jsfa.3856.
Yu, M., Lin, S., Ge, R., Xiong, C., Xu, L., Zhao, M., et al. Buckwheat self-assembling peptide-based hydrogel: Preparation, characteristics and forming mechanism. Food Hydrocolloids, 125, 2022, 107378, 10.1016/j.foodhyd.2021.107378.
Zhao, C., Chu, Z., Miao, Z., Liu, J., Liu, J., Xu, X., et al. Ultrasound heat treatment effects on structure and acid-induced cold set gel properties of soybean protein isolate. Food Bioscience, 39, 2021, 100827, 10.1016/j.fbio.2020.100827.
Zhao, G., Liu, Y., Zhao, M., Ren, J., Yang, B., Enzymatic hydrolysis and their effects on conformational and functional properties of peanut protein isolate. Food Chemistry 127:4 (2011), 1438–1443, 10.1016/j.foodchem.2011.01.046.
Zuo, Z., Zhang, X., Li, T., Zhou, J., Yang, Y., Bian, X., et al. High internal phase emulsions stabilized solely by sonicated quinoa protein isolate at various pH values and concentrations. Food Chemistry, 378, 2022, 132011, 10.1016/j.foodchem.2021.132011.
