Comprehensive review of emerging analytical methods for pea protein structure analysis: Advances and implications for food science over the last five years.

Othmeni, Ines; Blecker, Christophe; Karoui, Romdhane

doi:10.1016/j.foodchem.2025.143745

Article (Scientific journals)

Comprehensive review of emerging analytical methods for pea protein structure analysis: Advances and implications for food science over the last five years.

Othmeni, Ines; Blecker, Christophe; Karoui, Romdhane

2025 • In Food Chemistry, 478, p. 143745

Peer Reviewed verified by ORBi

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https://hdl.handle.net/2268/330856

DOI
10.1016/j.foodchem.2025.143745

PubMed
40073603

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Keywords :

Analytical methods; Environmental impact; Food processing; Pea protein; Protein interactions; Spectroscopy; Structural characterization; Pea Proteins; Protein Conformation; Magnetic Resonance Spectroscopy; Pisum sativum/chemistry; Pea Proteins/chemistry; Food Technology/methods; Analytical method; Environmental conditions; Food science; Property; Protein interaction; Protein sources; Protein structure analysis; Proteins structures; Analytical Chemistry

Abstract :

[en] This review explores recent advancements in analytical techniques for characterizing pea protein structure. With growing interest in sustainable protein sources, understanding the relationship between pea protein's structure and its functionality has become essential. This review covers a range of methods used to assess the structural properties of pea protein, focusing on the impact of environmental and processing conditions, as well as interactions with other materials, including mid-infrared spectroscopy, fluorescence spectroscopy, nuclear magnetic resonance spectroscopy, scanning electron microscopy, X-ray methods and calorimetric methods. By elucidating these methods, detailed insights into pea protein's structural and conformational properties as well as its dynamics are provided, contributing to enhance their potential applications. Thus, a comprehensive overview of commonly used analytical techniques for pea protein structure characterization in its different organization levels, aiming to offer readers an understanding of these techniques and highlight their relevance in selecting the most suitable method for analyzing complex matrices.

Disciplines :

Food science

Author, co-author :

Othmeni, Ines ; Université de Liège - ULiège > TERRA Research Centre

Blecker, Christophe ; Université de Liège - ULiège > TERRA Research Centre > Technologie Alimentaire (TA)

Karoui, Romdhane ; Université de Liège - ULiège > Agronomie, Bio-ingénierie et Chimie (AgroBioChem)

Language :

English

Title :

Comprehensive review of emerging analytical methods for pea protein structure analysis: Advances and implications for food science over the last five years.

Publication date :

30 June 2025

Journal title :

Food Chemistry

ISSN :

0308-8146

eISSN :

1873-7072

Publisher :

Elsevier, England

Volume :

478

Pages :

143745

Peer reviewed :

Peer Reviewed verified by ORBi

Additional URL :

https://api.elsevier.com/content/article/PII:S0308814625009963?httpAccept=text/xml

Funding text :

This work was supported by Cosucra Groupe Warcoing S.A. (Warcoing, Belgium) and the Walloon Region (Convention 8224).

Available on ORBi :

since 17 April 2025

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Bibliography

Acquah, C., Zhang, Y., Dubé, M.A., Udenigwe, C.C., Formation and characterization of protein-based films from yellow pea (Pisum sativum) protein isolate and concentrate for edible applications. Current Research in Food Science 2 (2020), 61–69, 10.1016/J.CRFS.2019.11.008.
Addo, P.W., Ossowski, P., Macpherson, S., Gravel, A.E., Kaur, R., Hoyos-Villegas, V., Lefsrud, M., Development of a nuclear magnetic resonance method and a near infrared calibration model for the rapid determination of lipid content in the field pea (Pisum sativum). Molecules, 27(5), 2022, 10.3390/molecules27051642.
Alrosan, M., Tan, T.C., Easa, A.M., Gammoh, S., Alu'datt, M. H., Molecular forces governing protein-protein interaction: Structure-function relationship of complexes protein in the food industry. Critical reviews in food science and nutrition, 2021, Bellwether Publishing, Ltd., 10.1080/10408398.2021.1871589.
Arbach, C.T., Alves, I.A., Serafini, M.R., Stephani, R., Perrone, Í.T., de Carvalho da Costa, J., Recent patent applications in beverages enriched with plant proteins. npj Science of Food, 5(1), 2021, 28, 10.1038/s41538-021-00112-4.
Asen, N.D., Aluko, R.E., Physicochemical and functional properties of membrane-fractionated heat-induced pea protein aggregates. Frontiers in Nutrition, 9, 2022, 10.3389/fnut.2022.852225.
Assad Bustillos, M., Jonchère, C., Garnier, C., Réguerre, A.L., Della Valle, G., Rheological and microstructural characterization of batters and sponge cakes fortified with pea proteins. Food Hydrocolloids, 101, 2020, 105553, 10.1016/j.foodhyd.2019.105553.
Azevedo, V.M., de Oliveira, A.C.S., Borges, S.V., Raguzzoni, J.C., Dias, M.V., Costa, A.L.R., Pea protein isolate nanocomposite films for packaging applications: Effect of starch nanocrystals on the structural. Emirates Journal of Food and Agriculture 32:7 (2020), 495–504, 10.9755/ejfa.2020.v32.i7.2124.
Beck, S.M., Knoerzer, K., Sellahewa, J., Emin, M.A., Arcot, J., Effect of different heat-treatment times and applied shear on secondary structure, molecular weight distribution, solubility and rheological properties of pea protein isolate as investigated by capillary rheometry. Journal of Food Engineering 208 (2017), 66–76, 10.1016/j.jfoodeng.2017.03.016.
Bertrand, D., Dufour, É., la spectroscopie infrarouge et ses applications analytiques (D. Bertrand & É. Dufour, Eds.; 2nd ed., Vol. 660). Editions Tec & doc. 2006.
Bloch, F., Nuclear Induction. Physical Review 70:7–8 (1946), 460–474, 10.1103/PhysRev.70.460.
Bogahawaththa, D., Bao Chau, N.H., Trivedi, J., Dissanayake, M., Vasiljevic, T., Impact of selected process parameters on solubility and heat stability of pea protein isolate. LWT 102 (2019), 246–253, 10.1016/J.LWT.2018.12.034.
Bogahawaththa, D., Chau, N.H.B., Trivedi, J., Dissanayake, M., Vasiljevic, T., Impact of controlled shearing on solubility and heat stability of pea protein isolate dispersed in solutions with adjusted ionic strength. Food Research International, 125, 2019, 108522, 10.1016/J.FOODRES.2019.108522.
Boukid, F., Rosell, C.M., Castellari, M., Pea protein ingredients: A mainstream ingredient to (re)formulate innovative foods and beverages. Trends in food science and technology, Vol. 110, 2021, Elsevier Ltd., 729–742, 10.1016/j.tifs.2021.02.040.
Cao, Y., Mezzenga, R., Food protein amyloid fibrils: Origin, structure, formation, characterization, applications and health implications. Advances in Colloid and Interface Science 269 (2019), 334–356, 10.1016/j.cis.2019.05.002.
Carbonaro, M., Maselli, P., Nucara, A., Relationship between digestibility and secondary structure of raw and thermally treated legume proteins: A Fourier transform infrared (FT-IR) spectroscopic study. Amino Acids 43:2 (2012), 911–921, 10.1007/s00726-011-1151-4.
Chang, L., Lan, Y., Chen, B., Rao, J., Interfacial, and emulsifying properties nexus of green pea protein fractions: Impact of pH and salt. Food Hydrocolloids, 140, 2023, 108652, 10.1016/j.foodhyd.2023.108652.
Chao, D., Aluko, R.E., Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment. CyTA - Journal of Food 16:1 (2018), 357–366, 10.1080/19476337.2017.1406536.
Chen, F.L., Wei, Y.M., Zhang, B., Chemical cross-linking and molecular aggregation of soybean protein during extrusion cooking at low and high moisture content. LWT - Food Science and Technology 44:4 (2011), 957–962, 10.1016/j.lwt.2010.12.008.
Chen, M., Lu, J., Liu, F., Nsor-Atindana, J., Xu, F., Goff, H.D., Zhong, F., Study on the emulsifying stability and interfacial adsorption of pea proteins. Food Hydrocolloids 88 (2019), 247–255, 10.1016/j.foodhyd.2018.09.003.
Chen, Q., Zhang, J., Zhang, Y., Liu, H., Li, T., Wang, Q., Kaplan, D.L., Microscopic insight into the interactions between pea protein and fatty acids during high-moisture extrusion processing. Food Chemistry, 404, 2023, 134176, 10.1016/J.FOODCHEM.2022.134176.
Chen, Q., Zhang, J., Zhang, Y., Wang, Q., Effect of fatty acid saturation degree on the rheological properties of pea protein and its high-moisture extruded product quality. Food Chemistry, 390, 2022, 133139, 10.1016/J.FOODCHEM.2022.133139.
Cheng, J., Cui, L., Effects of high-intensity ultrasound on the structural, optical, mechanical and physicochemical properties of pea protein isolate-based edible film. Ultrasonics Sonochemistry, 80, 2021, 105809, 10.1016/J.ULTSONCH.2021.105809.
Cheng, J., Li, Z., Wang, J., Zhu, Z., Yi, J., Chen, B., Cui, L., Structural characteristics of pea protein isolate (PPI) modified by high-pressure homogenization and its relation to the packaging properties of PPI edible film. Food Chemistry, 388, 2022, 132974, 10.1016/j.foodchem.2022.132974.
Cui, L., Bandillo, N., Wang, Y., Ohm, J.-B., Chen, B., Rao, J., Functionality and structure of yellow pea protein isolate as affected by cultivars and extraction pH. Food Hydrocolloids, 108, 2020, 106008, 10.1016/j.foodhyd.2020.106008.
Cui, L., Kimmel, J., Zhou, L., Chen, B., Rao, J., Improving the functionality of pea protein isolate through co-spray drying with emulsifying salt or disaccharide. Food Hydrocolloids, 113, 2021, 106534, 10.1016/J.FOODHYD.2020.106534.
Dahl, W.J., Foster, L.M., Tyler, R.T., Review of the health benefits of peas (Pisum sativum L.). In. British Journal of Nutrition, 108, Issue SUPPL. 1, 2012, 10.1017/S0007114512000852.
Divekar, M.T., Karunakaran, C., Lahlali, R., Kumar, S., Chelladurai, V., Liu, X., Jayas, D.S., Effect of microwave treatment on the cooking and macronutrient qualities of pulses. International Journal of Food Properties 20:2 (2017), 409–422, 10.1080/10942912.2016.1163578.
Falsafi, S.R., Rostamabadi, H., Jafari, S.M., X-ray diffraction (XRD) of nanoencapsulated food ingredients. Characterization of Nanoencapsulated Food Ingredients, 271–293, 2020, 10.1016/B978-0-12-815667-4.00009-2.
Fang, L., Xiang, H., Sun-Waterhouse, D., Cui, C., Lin, J., Enhancing the usability of pea protein isolate in food applications through modifying its structural and sensory properties via Deamidation by Glutaminase. Journal of Agricultural and Food Chemistry 68:6 (2020), 1691–1697, 10.1021/ACS.JAFC.9B06046/SUPPL_FILE/JF9B06046_SI_001.PDF.
FAOSTAT, FAOSTAT statistical database. 2022.
Freeman, R., Spin choreography: Basic steps in high resolution NMR. Vol. 35, 1997, Oxford University Press, 10.5860/CHOICE.35-1525 35-1525-35–1525.
Gao, K., Zha, F., Yang, Z., Rao, J., Chen, B., Structure characteristics and functionality of water-soluble fraction from high-intensity ultrasound treated pea protein isolate. Food Hydrocolloids, 125, 2022, 107409, 10.1016/j.foodhyd.2021.107409.
Ghobadi, M., Varidi, M.J., Koocheki, A., Varidi, M., Effect of heat treatment on the structure and stability of grass pea (Lathyrus sativus) protein isolate/Alyssum homolocarpum seed gum nanoparticles. International Journal of Biological Macromolecules 182 (2021), 26–36, 10.1016/J.IJBIOMAC.2021.03.170.
Gonzalez, M., Alvarez-Ramirez, J., Vernon-Carter, E.J., Reyes, I., Alvarez-Poblano, L., Effect of the drying temperature on color, antioxidant activity and in vitro digestibility of green pea ( Pisum sativum L.) flour. Starch - Stärke, 72(9–10), 1900228. 2020, 10.1002/star.201900228.
Gräwert, T.W., Svergun, D.I., Structural modeling using solution small-angle X-ray scattering (SAXS). Journal of Molecular Biology 432:9 (2020), 3078–3092, 10.1016/J.JMB.2020.01.030.
Guo, Q., Bayram, I., Zhang, W., Su, J., Shu, X., Yuan, F., Mao, L., Gao, Y., Fabrication and characterization of curcumin-loaded pea protein isolate-surfactant complexes at neutral pH. Food Hydrocolloids, 111, 2021, 106214, 10.1016/J.FOODHYD.2020.106214.
Hao, L., Sun, J., Pei, M., Zhang, G., Li, C., Li, C., Ma, X., He, S., Liu, L., Impact of non-covalent bound polyphenols on conformational, functional properties and in vitro digestibility of pea protein. Food Chemistry, 383, 2022, 132623, 10.1016/j.foodchem.2022.132623.
He, X., Chen, J., He, X., Feng, Z., Li, C., Liu, W., Dai, T., Liu, C., Industry-scale microfluidization as a potential technique to improve solubility and modify structure of pea protein. Innovative Food Science & Emerging Technologies, 67, 2021, 102582, 10.1016/j.ifset.2020.102582.
Helmick, H., Tonner, T., Hauersperger, D., Ettestad, S., Hartanto, C., Okos, M., Kokini, J.L., Physicochemical characterization of changes in pea protein as the result of cold extrusion. Food Chemistry, 423, 2023, 136240, 10.1016/j.foodchem.2023.136240.
Hood-Niefer, S.D., Warkentin, T.D., Chibbar, R.N., Vandenberg, A., Tyler, R.T., Effect of genotype and environment on the concentrations of starch and protein in, and the physicochemical properties of starch from, field pea and fababean. Journal of the Science of Food and Agriculture 92:1 (2012), 141–150, 10.1002/jsfa.4552.
Hoover, R., Hughes, T., Chung, H.J., Liu, Q., Composition, molecular structure, properties, and modification of pulse starches: A review. Food Research International 43:2 (2010), 399–413, 10.1016/J.FOODRES.2009.09.001.
Hu, T., Chen, J., He, X., Tang, Y., Sun, J., Liu, C., Dai, T., Complex plant protein prepared from rice protein and pea protein: Improve the thermal stability of betanin. Food Research International, 164, 2023, 112341, 10.1016/J.FOODRES.2022.112341.
Ilhan, E., Pocan, P., Ogawa, M., Oztop, M.H., Role of ‘D-allulose’ in a starch based composite gel matrix. Carbohydrate Polymers, 228, 2020, 115373, 10.1016/j.carbpol.2019.115373.
Jarpa-Parra, M., Bamdad, F., Wang, Y., Tian, Z., Temelli, F., Han, J., Chen, L., Optimization of lentil protein extraction and the influence of process pH on protein structure and functionality. LWT - Food Science and Technology 57:2 (2014), 461–469, 10.1016/j.lwt.2014.02.035.
Jia, X.W., Qin, Z.Y., Xu, J.X., Kong, B.H., Liu, Q., Wang, H., Preparation and characterization of pea protein isolate-pullulan blend electrospun nanofiber films. International Journal of Biological Macromolecules 157 (2020), 641–647, 10.1016/J.IJBIOMAC.2019.11.216.
Kalayci, A., Ozel, B., Oztop, M.H., Alpas, H., Investigation of the effects of high hydrostatic pressure on the functional properties of pea protein isolate. Journal of Food Process Engineering., 2022, 10.1111/jfpe.14243.
Karoui, R., Spectroscopic technique: Mid-infrared (MIR) and Fourier transform mid-infrared (FT-MIR) spectroscopies. Modern techniques for food authentication, 2018, Elsevier, 23–50, 10.1016/b978-0-12-814264-6.00002-5.
Karoui, R., Dufour, E., Pillonel, L., Picque, D., Cattenoz, T., Bosset, J.-O., Fluorescence and infrared spectroscopies: A tool for the determination of the geographic origin of Emmental cheeses manufactured during summer. Le Lait 84:4 (2004), 359–374, 10.1051/lait:2004010.
Karunakaran, C., Vijayan, P., Stobbs, J., Bamrah, R.K., Arganosa, G., Warkentin, T.D., High throughput nutritional profiling of pea seeds using Fourier transform mid-infrared spectroscopy. Food Chemistry, 309, 2020, 125585, 10.1016/J.FOODCHEM.2019.125585.
Keivaninahr, F., Gadkari, P., Zoroufchi Benis, K., Tulbek, M., Ghosh, S., Prediction of emulsification behaviour of pea and faba bean protein concentrates and isolates from structure-functionality analysis. RSC Advances 11:20 (2021), 12117–12135, 10.1039/d0ra09302e.
Kirtil, E., Oztop, M.H., 1H nuclear magnetic resonance Relaxometry and magnetic resonance imaging and applications in food science and processing. Food Engineering Reviews 8:1 (2016), 1–22, 10.1007/s12393-015-9118-y.
Kleinberg, R.L., Jackson, J.A., An introduction to the history of NMR well logging. Concepts in Magnetic Resonance 13:6 (2001), 335–413.
Kornet, R., Roozalipour, S.L., Venema, P., van der Goot, A.J., Meinders, M.B.J., van der Linden, E., Coacervation in pea protein solutions: The effect of pH, salt, and fractionation processing steps. Food Hydrocolloids, 125, 2022, 107379, 10.1016/J.FOODHYD.2021.107379.
Kowalczyk, D., Gustaw, W., Świeca, M., Baraniak, B., A study on the mechanical properties of pea protein isolate films. Journal of Food Processing and Preservation 38:4 (2014), 1726–1736, 10.1111/jfpp.12135.
Ladjal-Ettoumi, Y., Boudries, H., Chibane, M., Romero, A., Pea, chickpea and lentil protein isolates: Physicochemical characterization and emulsifying properties. Food Biophysics 11:1 (2016), 43–51, 10.1007/s11483-015-9411-6.
Lan, Y., Xu, M., Ohm, J.B., Chen, B., Rao, J., Solid dispersion-based spray-drying improves solubility and mitigates beany flavour of pea protein isolate. Food Chemistry 278 (2019), 665–673, 10.1016/J.FOODCHEM.2018.11.074.
Landis, E.N., Keane, D.T., X-ray microtomography. Materials Characterization 61:12 (2010), 1305–1316, 10.1016/J.MATCHAR.2010.09.012.
Li, R., Kirkensgaard, J.J.K., Corredig, M., Structural evolution of pea-derived albumins during pH and heat treatment studied with light and X-ray scattering. Food Research International, 186, 2024, 114380, 10.1016/j.foodres.2024.114380.
Li, X.L., Liu, W.J., Xu, B.C., Zhang, B., Wang, W., Su, D.L., OSA-linear dextrin enhances the compactness of pea protein isolate nanoparticles: Increase of high internal phase emulsions stability. Food Chemistry, 404, 2023, 134590, 10.1016/J.FOODCHEM.2022.134590.
Linares-García, L., Repo-Carrasco-Valencia, R., Paulet, P.G., Schoenlechner, R., Development of gluten-free and egg-free pasta based on quinoa (Chenopdium quinoa Willd) with addition of lupine flour, vegetable proteins and the oxidizing enzyme POx. European Food Research and Technology 245:10 (2019), 2147–2156, 10.1007/s00217-019-03320-1.
Liu, Y., Wang, D., Wang, J., Yang, Y., Zhang, L., Li, J., Wang, S., Functional properties and structural characteristics of phosphorylated pea protein isolate. International Journal of Food Science and Technology 55:5 (2020), 2002–2010, 10.1111/ijfs.14391.
Lohumi, S., Lee, S., Lee, H., Cho, B.K., A review of vibrational spectroscopic techniques for the detection of food authenticity and adulteration. Trends in Food Science & Technology 46:1 (2015), 85–98, 10.1016/J.TIFS.2015.08.003.
Lu, Z.X., He, J.F., Zhang, Y.C., Bing, D.J., Composition, physicochemical properties of pea protein and its application in functional foods. Critical Reviews in Food Science and Nutrition 60:15 (2020), 2593–2605, 10.1080/10408398.2019.1651248.
Luo, L., Wang, Z., Deng, Y., Wei, Z., Zhang, Y., Tang, X., Liu, G., Zhou, P., Zhao, Z., Zhang, M., Li, P., High-pressure homogenization: A potential technique for transforming insoluble pea protein isolates into soluble aggregates. Food Chemistry, 397, 2022, 133684, 10.1016/j.foodchem.2022.133684.
Luykx, D.M.A.M., van Ruth, S.M., An overview of analytical methods for determining the geographical origin of food products. Food Chemistry 107:2 (2008), 897–911, 10.1016/J.FOODCHEM.2007.09.038.
Melchior, S., Moretton, M., Calligaris, S., Manzocco, L., Nicoli, M.C., High pressure homogenization shapes the techno-functionalities and digestibility of pea proteins. Food and Bioproducts Processing 131 (2022), 77–85, 10.1016/j.fbp.2021.10.011.
Mession, J.L., Chihi, M.L., Sok, N., Saurel, R., Effect of globular pea proteins fractionation on their heat-induced aggregation and acid cold-set gelation. Food Hydrocolloids 46 (2015), 233–243, 10.1016/j.foodhyd.2014.11.025.
Mession, J.L., Sok, N., Assifaoui, A., Saurel, R., Thermal denaturation of pea globulins (Pisum sativum L.) - molecular interactions leading to heat-induced protein aggregation. Journal of Agricultural and Food Chemistry 61:6 (2013), 1196–1204, 10.1021/jf303739n.
Miriani, M., Keerati-u-rai, M., Corredig, M., Iametti, S., Bonomi, F., Denaturation of soy proteins in solution and at the oil-water interface: A fluorescence study. Food Hydrocolloids 25:4 (2011), 620–626, 10.1016/j.foodhyd.2010.07.020.
Möller, A.C., van der Padt, A., van der Goot, A.J., From raw material to mildly refined ingredient – Linking structure to composition to understand fractionation processes. Journal of Food Engineering, 291, 2021, 110321, 10.1016/J.JFOODENG.2020.110321.
Moreno, H.M., Domínguez-Timón, F., Díaz, M.T., Pedrosa, M.M., Borderías, A.J., Tovar, C.A., Evaluation of gels made with different commercial pea protein isolate: Rheological, structural and functional properties. Food Hydrocolloids, 99, 2020, 105375, 10.1016/J.FOODHYD.2019.105375.
Moreno, H.M., Tovar, C.A., Domínguez-Timón, F., Cano-Báez, J., Díaz, M.T., Pedrosa, M.M., Borderías, A.J., Gelation of commercial pea protein isolate: Effect of microbitransglutaminase and thermal processing. Food Science and Technology (Brazil) 40:4 (2020), 800–809, 10.1590/fst.19519.
Mozafarpour, R., Koocheki, A., Effect of ultrasonic pretreatment on the rheology and structure of grass pea (Lathyrus sativus L.) protein emulsion gels induced by transglutaminase. Ultrasonics Sonochemistry, 92, 2023, 106278, 10.1016/J.ULTSONCH.2022.106278.
Mozafarpour, R., Koocheki, A., Nicolai, T., Modification of grass pea protein isolate (Lathyrus sativus L.) using high intensity ultrasound treatment: Structure and functional properties. Food Research International, 158, 2022, 111520, 10.1016/j.foodres.2022.111520.
Muhialdin, B.J., Ubbink, J., Effects of pH and aging on the texture and physicochemical properties of extruded pea protein isolate. Food Hydrocolloids, 140, 2023, 108639, 10.1016/j.foodhyd.2023.108639.
Othmeni, I., Karoui, R., Blecker, C., Impact of pH on the structure, interfacial and foaming properties of pea protein isolate: Investigation of the structure – Function relationship. International Journal of Biological Macromolecules, 278, 2024, 134818, 10.1016/j.ijbiomac.2024.134818.
Pavani, M., Singha, P., Singh, S.K., Effect of pH and biopolymer ratio on phase behavior, rheology, and structural characteristics of pea protein isolate-locust bean gum coacervates. JSFA Reports 4:4 (2024), 197–207, 10.1002/jsf2.187.
Peng, H., Zhang, J., Wang, S., Qi, M., Yue, M., Zhang, S., Song, J., Wang, C., Zhang, D., Wang, X., Ma, C., High moisture extrusion of pea protein: Effect of l-cysteine on product properties and the process forming a fibrous structure. Food Hydrocolloids, 129, 2022, 107633, 10.1016/J.FOODHYD.2022.107633.
Petsko, G.A., Ringe, D., Charmot, D., Structure et fonction des protéines (De Boeck Supérieur). https://scholar.google.com/scholar?hl=fr&as_sdt=0%2C5&q=Biochimie+des+Prot%C3%A9ines+&btnG=#d=gs_cit&u=%2Fscholar%3Fq%3Dinfo%3ArYbCezWccicJ%3Ascholar.google.com%2F%26output%3Dcite%26scirp%3D1%26hl%3Dfr. 2008.
Purohit, S.R., Jayachandran, L.E., Raj, A.S., Nayak, D., Rao, P.S., X-ray diffraction for food quality evaluation. Evaluation Technologies for Food Quality, 579–594, 2019, 10.1016/B978-0-12-814217-2.00022-6.
Qi, M., Zhang, G., Ren, Z., He, Z., Peng, H., Zhang, D., Ma, C., Impact of extrusion temperature on in vitro digestibility and pasting properties of pea flour. Plant Foods for Human Nutrition 70 (2021), 26–30, 10.1007/s11130-020-00869-1/Published.
Qu, Z., Chen, G., Wang, J., Xie, X., Chen, Y., Preparation, structure evaluation, and improvement in foaming characteristics of fibrotic pea protein isolate by cold plasma synergistic organic acid treatment. Food Hydrocolloids, 134, 2023, 108057, 10.1016/J.FOODHYD.2022.108057.
Rodriguez-Saona, L.E., Allendorf, M.E., Use of FTIR for rapid authentication and detection of adulteration of food. Annual Review of Food Science and Technology 2 (2011), 467–483, 10.1146/annurev-food-022510-133750.
Schreuders, F.K.G., Bodnár, I., Erni, P., Boom, R.M., der Goot, A.J., van., Water redistribution determined by time domain NMR explains rheological properties of dense fibrous protein blends at high temperature. Food Hydrocolloids, 101, 2020, 105562, 10.1016/J.FOODHYD.2019.105562.
Sha, L., Koosis, A.O., Wang, Q., True, A.D., Xiong, Y.L., Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein. Food Chemistry, 350, 2021, 10.1016/j.foodchem.2021.129271.
Sharma, V., Bhardwaj, A., Scanning electron microscopy (SEM) in food quality evaluation. Evaluation Technologies for Food Quality, 743–761, 2019, 10.1016/B978-0-12-814217-2.00029-9.
Shevkani, K., Singh, N., Chen, Y., Kaur, A., Yu, L., Pulse proteins: Secondary structure, functionality and applications. Journal of Food Science and Technology., 2019, 10.1007/s13197-019-03723-8.
Shevkani, K., Singh, N., Kaur, A., Rana, J.C., Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study. Food Hydrocolloids 43 (2015), 679–689, 10.1016/j.foodhyd.2014.07.024.
Shrestha, S., Vant Hag, L., Haritos, V., Dhital, S., Comparative study on molecular and higher-order structures of legume seed protein isolates: Lentil, mungbean and yellow pea. Food Chemistry, 411, 2023, 135464, 10.1016/J.FOODCHEM.2023.135464.
Sim, S.Y.J., Karwe, M.V., Moraru, C.I., High pressure structuring of pea protein concentrates. Journal of Food Process Engineering, 42(7), 2019, 10.1111/jfpe.13261.
Sirtori, E., Isak, I., Resta, D., Boschin, G., Arnoldi, A., Mechanical and thermal processing effects on protein integrity and peptide fingerprint of pea protein isolate. Food Chemistry 134:1 (2012), 113–121, 10.1016/J.FOODCHEM.2012.02.073.
Sobolev, A.P., Testone, G., Santoro, F., Nicolodi, C., Iannelli, M.A., Amato, M.E., Mannina, L., Quality traits of conventional and transgenic lettuce (Lactuca sativa L.) at harvesting by NMR metabolic profiling. Journal of Agricultural and Food Chemistry 58:11 (2010), 6928–6936, 10.1021/jf904439y.
Sun, D., Wu, M., Zhou, C., Wang, B., Transformation of high moisture extrusion on pea protein isolate in melting zone during: From the aspects of the rheological property, physicochemical attributes and modification mechanism. Food Hydrocolloids, 133, 2022, 108016, 10.1016/j.foodhyd.2022.108016.
Sun, D., Zhang, B., Zhou, C., Wang, B., Wu, M., Study on high moisture extruded pea protein isolate based on acid-induced process: Physicochemical properties, conformational changes and fibrous structure mechanism. Food Hydrocolloids, 141, 2023, 108746, 10.1016/J.FOODHYD.2023.108746.
Tanger, C., Engel, J., Kulozik, U., Influence of extraction conditions on the conformational alteration of pea protein extracted from pea flour. Food Hydrocolloids, 107, 2020, 105949, 10.1016/J.FOODHYD.2020.105949.
Tanger, C., Müller, M., Andlinger, D., Kulozik, U., Influence of pH and ionic strength on the thermal gelation behaviour of pea protein. Food Hydrocolloids, 123, 2022, 106903, 10.1016/J.FOODHYD.2021.106903.
Tas, O., Ertugrul, U., Grunin, L., Oztop, M.H., An investigation of functional quality characteristics and water interactions of navy bean, chickpea, pea, and lentil flours. Legume. Science, 4(1), 2022, 10.1002/leg3.136.
Tosh, S.M., Yada, S., Dietary fibres in pulse seeds and fractions: Characterization, functional attributes, and applications. Food Research International 43:2 (2010), 450–460, 10.1016/J.FOODRES.2009.09.005.
Trikusuma, M., Paravisini, L., Peterson, D.G., Identification of aroma compounds in pea protein UHT beverages. Food Chemistry, 312, 2020, 126082, 10.1016/j.foodchem.2019.126082.
Türker-Kaya, S., Huck, C.W., A review of mid-infrared and near-infrared imaging: Principles, concepts and applications in plant tissue analysis. Molecules, Vol. 22, Issue 1, 2017, MDPI AG, 10.3390/molecules22010168.
Tzitzikas, E.N., Vincken, J.P., De Groot, J., Gruppen, H., Visser, R.G.F., Genetic variation in pea seed globulin composition. Journal of Agricultural and Food Chemistry 54:2 (2006), 425–433, 10.1021/jf0519008.
Vilotte, A., Bodiguel, H., Gunes, D.Z., Schmitt, C., Roux, D., Guilbert, E., de Loubens, C., Formation and stability of fibers obtained by cold gelation of pea protein isolate aggregates in a hydrodynamic spinning process. Food Hydrocolloids, 145, 2023, 108999, 10.1016/J.FOODHYD.2023.108999.
Wang, H., van den Berg, F.W.J., Zhang, W., Czaja, T.P., Zhang, L., Jespersen, B.M., Lametsch, R., Differences in physicochemical properties of high-moisture extrudates prepared from soy and pea protein isolates. Food Hydrocolloids, 128, 2022, 107540, 10.1016/J.FOODHYD.2022.107540.
Webb, D., Dogan, H., Li, Y., Alavi, S., Physico-chemical properties and Texturization of pea, wheat and soy proteins using extrusion and their application in plant-based meat. Foods, 12(8), 2023, 1586, 10.3390/foods12081586.
Withana-Gamage, T.S., Wanasundara, J.P., Pietrasik, Z., Shand, P.J., Physicochemical, thermal and functional characterisation of protein isolates from Kabuli and desi chickpea (Cicer arietinum L.): A comparative study with soy (Glycine max) and pea (Pisum sativum L.). Journal of the Science of Food and Agriculture 91:6 (2011), 1022–1031, 10.1002/jsfa.4277.
Xia, S., Xue, Y., Xue, C., Jiang, X., Li, J., Structural and rheological properties of meat analogues from Haematococcus pluvialis residue-pea protein by high moisture extrusion. LWT, 154, 2022, 112756, 10.1016/J.LWT.2021.112756.
Xia, Y., Zhu, L., Wu, G., Liu, T., Li, X., Wang, X., Zhang, H., Comparative study of various methods used for bitterness reduction from pea (Pisum sativum L.) protein hydrolysates. LWT, 159, 2022, 113228, 10.1016/J.LWT.2022.113228.
Xu, Q., Qi, B., Han, L., Wang, D., Zhang, S., Jiang, L., Xie, F., Li, Y., Study on the gel properties, interactions, and pH stability of pea protein isolate emulsion gels as influenced by inulin. LWT, 137, 2021, 110421, 10.1016/J.LWT.2020.110421.
Yang, J., Mocking-Bode, H.C.M., van den Hoek, I.A.F., Theunissen, M., Voudouris, P., Meinders, M.B.J., Sagis, L.M.C., The impact of heating and freeze or spray drying on the interface and foam stabilising properties of pea protein extracts: Explained by aggregation and protein composition. Food Hydrocolloids, 133, 2022, 107913, 10.1016/j.foodhyd.2022.107913.
Youshanlouei, Y.A., Kiani, H., Mousavi, M., Mousavi, Z.E., Grass pea (Lathyrus sativus L.) protein yield and functionality as affected by extraction method: Alkaline, ultrasound-assisted, and ultrasound pretreatment extraction. Cereal Chemistry 99:4 (2022), 931–946, 10.1002/cche.10549.
Yu, X., Wang, H., Yuan, Y., Shi, J., Duan, Y., Wang, L., Wang, P., Xiao, Z., Changes in physicochemical and structural properties of pea protein during the high moisture extrusion process: Effects of carboxymethylcellulose sodium and different extrusion zones. International Journal of Biological Macromolecules, 251, 2023, 126350, 10.1016/J.IJBIOMAC.2023.126350.
Zhang, B., Kang, X., Cheng, Y., Cui, B., Abd El-Aty, A.M., Impact of high moisture contents on the structure and functional properties of pea protein isolate during extrusion. Food Hydrocolloids, 127, 2022, 107508, 10.1016/J.FOODHYD.2022.107508.
Zhang, H., Wang, T., He, F., Chen, G., Fabrication of pea protein-curcumin nanocomplexes via microfluidization for improved solubility, nano-dispersibility and heat stability of curcumin: Insight on interaction mechanisms. International Journal of Biological Macromolecules 168 (2021), 686–694, 10.1016/J.IJBIOMAC.2020.11.125.
Zhang, J., Liu, Q., Chen, Q., Sun, F., Liu, H., Kong, B., Synergistic modification of pea protein structure using high-intensity ultrasound and pH-shifting technology to improve solubility and emulsification. Ultrasonics Sonochemistry, 88, 2022, 106099, 10.1016/J.ULTSONCH.2022.106099.
Zhang, M., Fan, L., Liu, Y., Li, J., Relationship between protein native conformation and ultrasound efficiency: For improving the physicochemical stability of water–in–oil emulsions. Colloids and Surfaces A: Physicochemical and Engineering Aspects, 651, 2022, 129737, 10.1016/J.COLSURFA.2022.129737.
Zhang, X., Wang, C., Qi, Z., Zhao, R., Wang, C., Zhang, T., Pea protein based nanocarriers for lipophilic polyphenols: Spectroscopic analysis, characterization, chemical stability, antioxidant and molecular docking. Food Research International, 160, 2022, 111713, 10.1016/j.foodres.2022.111713.
Zhi, Z., Yan, L., Li, H., Dewettinck, K., Van der Meeren, P., Liu, R., Van Bockstaele, F., A combined approach for modifying pea protein isolate to greatly improve its solubility and emulsifying stability. Food Chemistry, 380, 2022, 131832, 10.1016/J.FOODCHEM.2021.131832.
Zhu, H.G., Tang, H.Q., Cheng, Y.Q., Li, Z.G., Tong, L.T., Potential of preparing meat analogue by functional dry and wet pea (Pisum sativum) protein isolate. LWT, 148, 2021, 111702, 10.1016/J.LWT.2021.111702.
Zhu, P., Huang, W., Chen, L., Develop and characterize thermally reversible transparent gels from pea protein isolate and study the gel formation mechanisms. Food Hydrocolloids, 125, 2022, 107373, 10.1016/J.FOODHYD.2021.107373.
Zhu, P., Huang, W., Guo, X., Chen, L., Strong and elastic pea protein hydrogels formed through pH-shifting method. Food Hydrocolloids, 117, 2021, 10.1016/j.foodhyd.2021.106705.