Emulsifying properties; Pea protein isolate; Protein structure; Droplets sizes; Emulsifying activity; Emulsifying property; Emulsifying stabilities; Pea protein isolates; Performance; PH-dependent; Proteins structures; Structure-function relationship; Surface hydrophobicity; Structural Biology; Biochemistry; Molecular Biology
Abstract :
[en] This study investigated the relationship between pea protein isolates (PPI) emulsifying properties and their structural, interfacial, and physicochemical characteristics at various pH values (native pH, 7, 5, and 3). Emulsion characteristics including emulsifying activity and stability, droplet size, flocculation index (FI) and coalescence index (CI) were examined. Additionally, physicochemical properties such as solubility, zeta potential, surface hydrophobicity, interfacial protein adsorption and protein conformation were analyzed. Results revealed significant pH-dependent variations in emulsifying performance. The poorest emulsifying performance was observed at pH 5, with the largest droplet size (28.84 μm) and highest CI (38.94 %). Optimal emulsifying properties were noticed at native pH, with the smallest droplet size (7.73 μm) and lowest CI (4.69). At pH 3, good emulsifying ability with the highest physical stability (5.43) were observed, associated with increased surface hydrophobicity and the presence of some aggregates contributing to the formation of cohesive interfacial film. Structural elements, particularly β-sheets and random coils, were positively correlated with emulsifying activity and stability, while β-turns had a negative impact. These findings provide insights into the pH-dependent emulsifying behavior of PPI, highlighting the complex relationship between protein structure and functionality, enabling the optimization of the use of PPI as an emulsifier in food applications.
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)
This research was funded by Cosucra Groupe Warcoing S.A. (Warcoing, Belgium) and the Walloon Region (grant number 8224).The authors wish to express their gratitude to the Walloon Region for their support (grant 8224). They also extend their thanks to Jonathan Willocq and Lionel Dumoulin from Cosucra Groupe Warcoing for their guidance and assistance throughout the project. The authors gratefully acknowledge Marjorie Servais (Teaching and Research Center, Gembloux Agro-BioTech, Belgium) for the support regarding the rheological analysis.This research was funded by Cosucra Groupe Warcoing S.A. (Warcoing, Belgium) and the Walloon Region (grant number 8224 ).
Ge, J., Sun, C., Corke, H., Gul, K., Gan, R., Fang, Y., The health benefits, functional properties, modifications, and applications of pea ( Pisum sativum L.) protein: current status, challenges, and perspectives. Compr. Rev. Food Sci. Food Saf. 19 (2020), 1835–1876, 10.1111/1541-4337.12573.
Chang, L., Lan, Y., Chen, B., Rao, J., Interfacial, and emulsifying properties nexus of green pea protein fractions: impact of pH and salt. Food Hydrocoll., 140, 2023, 108652, 10.1016/j.foodhyd.2023.108652.
Liang, H.N., Tang, C.H., PH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins. Food Hydrocoll. 33 (2013), 309–319, 10.1016/j.foodhyd.2013.04.005.
Shanthakumar, P., Klepacka, J., Bains, A., Chawla, P., Dhull, S.B., Najda, A., The current situation of pea protein and its application in the food industry. Molecules, 27, 2022, 5354, 10.3390/molecules27165354.
Burger, T.G., Zhang, Y., Recent progress in the utilization of pea protein as an emulsifier for food applications. Trends Food Sci. Technol. 86 (2019), 25–33, 10.1016/j.tifs.2019.02.007.
Karaca, A.C., Low, N., Nickerson, M., Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Res. Int. 44 (2011), 2742–2750, 10.1016/J.FOODRES.2011.06.012.
Mcclements, D.J., Critical review of techniques and methodologies for characterization of emulsion stability. Crit. Rev. Food Sci. Nutr. 47 (2007), 611–649, 10.1080/10408390701289292.
Tang, C.-H., Globular proteins as soft particles for stabilizing emulsions: concepts and strategies. Food Hydrocoll., 103, 2020, 105664, 10.1016/j.foodhyd.2020.105664.
Amine, C., Dreher, J., Helgason, T., Tadros, T., Investigation of emulsifying properties and emulsion stability of plant and milk proteins using interfacial tension and interfacial elasticity. Food Hydrocoll. 39 (2014), 180–186, 10.1016/J.FOODHYD.2014.01.001.
Damodaran, S., Protein-stabilized foams and emulsions. Paraf, A., Damodaran, S., (eds.) Food Proteins and Their Applications, 1st edition, 1997, CRC Press, New York, 57–110, 10.1201/9780203755617.
L'hocine, L., Boye, J.I., Arcand, Y., Composition and functional properties of soy protein isolates prepared using alternative defatting and extraction procedures. J. Food Sci. 71 (2006), C137–C145, 10.1111/j.1365-2621.2006.tb15609.x.
Asen, N.D., Aluko, R.E., Martynenko, A., Utioh, A., Bhowmik, P., Yellow field pea protein (Pisum sativum L.): extraction technologies, functionalities, and applications. Foods, 12, 2023, 3978, 10.3390/foods12213978.
García Arteaga, V., Kraus, S., Schott, M., Muranyi, I., Schweiggert-Weisz, U., Eisner, P., Screening of twelve pea (Pisum sativum L.) cultivars and their isolates focusing on the protein characterization, functionality, and sensory profiles. Foods, 10, 2021, 758, 10.3390/foods10040758.
Pedrosa, M.M., Varela, A., Domínguez-Timón, F., Tovar, C.A., Moreno, H.M., Borderías, A.J., Díaz, M.T., Comparison of bioactive compounds content and techno-functional properties of pea and bean flours and their protein isolates. Plant Foods Hum. Nutr. 75 (2020), 642–650, 10.1007/s11130-020-00866-4.
Hoehnel, A., Axel, C., Bez, J., Arendt, E.K., Zannini, E., Comparative analysis of plant-based high-protein ingredients and their impact on quality of high-protein bread. J. Cereal Sci., 89, 2019, 102816, 10.1016/j.jcs.2019.102816.
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. Int. J. Biol. Macromol., 278, 2024, 134818, 10.1016/j.ijbiomac.2024.134818.
Sha, L., Koosis, A.O., Wang, Q., True, A.D., Xiong, Y.L., Interfacial dilatational and emulsifying properties of ultrasound-treated pea protein. Food Chem., 350, 2021, 10.1016/j.foodchem.2021.129271.
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. Ultrason. Sonochem., 88, 2022, 106099, 10.1016/J.ULTSONCH.2022.106099.
Chao, D., Jung, S., Aluko, R.E., Physicochemical and functional properties of high pressure-treated isolated pea protein. Innov. Food Sci. Emerg. Technol. 45 (2018), 179–185, 10.1016/j.ifset.2017.10.014.
D'Alessio, G., Flamminii, F., Faieta, M., Prete, R., Di Michele, A., Pittia, P., Di Mattia, C.D., High pressure homogenization to boost the technological functionality of native pea proteins. Curr. Res. Food Sci., 6, 2023, 100499, 10.1016/j.crfs.2023.100499.
Chao, D., Aluko, R.E., Modification of the structural, emulsifying, and foaming properties of an isolated pea protein by thermal pretreatment. CyTA J. Food 16 (2018), 357–366, 10.1080/19476337.2017.1406536.
Peng, W., Kong, X., Chen, Y., Zhang, C., Yang, Y., Hua, Y., Effects of heat treatment on the emulsifying properties of pea proteins. Food Hydrocoll. 52 (2016), 301–310, 10.1016/j.foodhyd.2015.06.025.
Shen, Q., Xiong, T., Dai, J., Chen, X., Wang, L., Li, Y., Li, J., Li, B., Chen, Y., Effects of pH-shifting treatments on oil-water interfacial properties of pea protein isolates: identification and quantification of proteins at interfacial protein layer. Food Hydrocoll., 133, 2022, 107937, 10.1016/j.foodhyd.2022.107937.
Bidlingmeyer, B.A., Cohen, S.A., Tarvin, T.L., Rapid analysis of amino acids using pre-column derivatization. J. Chromatogr. B Biomed. Sci. Appl. 336 (1984), 93–104, 10.1016/S0378-4347(00)85133-6.
Landry, J., Delhaye, S., Simplified procedure for the determination of tryptophan of foods and feedstuffs from barytic hydrolysis. J. Agric. Food Chem. 40 (1992), 776–779, 10.1021/jf00017a014.
Gehrke, C.W., Wall, L.L., Absheer, J.S., Kaiser, F.E., Zumwalt, R.W., Sample preparation for chromatography of amino acids: acid hydrolysis of proteins. J. AOAC Int. 68 (1985), 811–821, 10.1093/jaoac/68.5.811.
Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685, 10.1038/227680a0.
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. J. Food Eng. 208 (2017), 66–76, 10.1016/j.jfoodeng.2017.03.016.
Bondu, C., Gimeno, F., Evon, P., Vaca-Medina, G., Rouilly, A., Use of FTIR to study secondary structure of texturized plant proteins by high moisture extrusion cooking, a comprehensive review. Food Res. Int., 197, 2024, 115147, 10.1016/j.foodres.2024.115147.
Shen, Q., Li, J., Shen, X., Zhu, X., Dai, J., Tang, C., Song, R., Li, B., Chen, Y., Linear and nonlinear interface rheological behaviors and structural properties of pea protein (vicilin, legumin, albumin). Food Hydrocoll., 139, 2023, 108500, 10.1016/j.foodhyd.2023.108500.
Bradford, M., A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72 (1976), 248–254, 10.1006/abio.1976.9999.
Lam, R.S.H., Nickerson, M.T., The effect of pH and temperature pre-treatments on the physicochemical and emulsifying properties of whey protein isolate. LWT Food Sci. Technol. 60 (2015), 427–434, 10.1016/j.lwt.2014.07.031.
Pownall, T.L., Udenigwe, C.C., Aluko, R.E., Amino acid composition and antioxidant properties of pea seed (Pisum sativum L.) enzymatic protein hydrolysate fractions. J. Agric. Food Chem. 58 (2010), 4712–4718, 10.1021/jf904456r.
Auer, J., Alminger, M., Marinea, M., Johansson, M., Zamaratskaia, G., Högberg, A., Langton, M., Assessing the digestibility and estimated bioavailability/bioaccessibility of plant-based proteins and minerals from soy, pea, and faba bean ingredients. LWT, 197, 2024, 115893, 10.1016/j.lwt.2024.115893.
Gorissen, S.H.M., Crombag, J.J.R., Senden, J.M.G., Waterval, W.A.H., Bierau, J., Verdijk, L.B., van Loon, L.J.C., Protein content and amino acid composition of commercially available plant-based protein isolates. Amino Acids 50 (2018), 1685–1695, 10.1007/s00726-018-2640-5.
Wang, S., Yang, J., Shao, G., Qu, D., Zhao, H., Zhu, L., Yang, L., Li, R., Li, J., Liu, H., Zhu, D., Dilatational rheological and nuclear magnetic resonance characterization of oil-water interface: impact of pH on interaction of soy protein isolated and soy hull polysaccharides. Food Hydrocoll., 99, 2020, 105366, 10.1016/j.foodhyd.2019.105366.
Jiang, S., Ding, J., Andrade, J., Rababah, T.M., Almajwal, A., Abulmeaty, M.M., Feng, H., Modifying the physicochemical properties of pea protein by pH-shifting and ultrasound combined treatments. Ultrason. Sonochem. 38 (2017), 835–842, 10.1016/J.ULTSONCH.2017.03.046.
Gao, Z., Shen, P., Lan, Y., Cui, L., Ohm, J.B., Chen, B., Rao, J., Effect of alkaline extraction pH on structure properties, solubility, and beany flavor of yellow pea protein isolate. Food Res. Int., 131, 2020, 10.1016/j.foodres.2020.109045.
Chen, M., Lu, J., Liu, F., Nsor-Atindana, J., Xu, F., Goff, H.D., Ma, J., Zhong, F., Study on the emulsifying stability and interfacial adsorption of pea proteins. Food Hydrocoll. 88 (2019), 247–255, 10.1016/j.foodhyd.2018.09.003.
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. J. Agric. Food Chem. 68 (2020), 1691–1697, 10.1021/ACS.JAFC.9B06046/SUPPL_FILE/JF9B06046_SI_001.PDF.
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 (2012), 911–921, 10.1007/s00726-011-1151-4.
Husband, H., Ferreira, S., Bu, F., Feyzi, S., Ismail, B.P., Pea protein globulins: does their relative ratio matter?. Food Hydrocoll., 148, 2024, 10.1016/j.foodhyd.2023.109429.
Barac, M., Cabrilo, S., Pesic, M., Stanojevic, S., Zilic, S., Macej, O., Ristic, N., Profile and functional properties of seed proteins from six pea (Pisum sativum) genotypes. Int. J. Mol. Sci. 11 (2010), 4973–4990, 10.3390/ijms11124973.
Belton, P.S., Bogracheva, T., Cserhalmi, Z., Czukor, B., Grant, A., Lambert, N., Wellner, N., NMR and FTIR studies of hydrated pea proteins. Food Hydrocoll. 11 (1997), 485–491, 10.1016/S0268-005X(97)80047-1.
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.
Chang, L., Lan, Y., Bandillo, N., Ohm, J.-B., Chen, B., Rao, J., Plant proteins from green pea and chickpea: extraction, fractionation, structural characterization and functional properties. Food Hydrocoll., 123, 2022, 107165, 10.1016/j.foodhyd.2021.107165.
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 Hydrocoll. 46 (2015), 233–243, 10.1016/j.foodhyd.2014.11.025.
Zhang, T., Jiang, B., Mu, W., Wang, Z., Emulsifying properties of chickpea protein isolates: influence of pH and NaCl. Food Hydrocoll. 23 (2009), 146–152, 10.1016/j.foodhyd.2007.12.005.
Jiang, J., Xiong, Y.L., Chen, J., Role of β-conglycinin and glycinin subunits in the pH-shifting-induced structural and physicochemical changes of soy protein isolate. J. Food Sci., 76, 2011, 10.1111/j.1750-3841.2010.02035.x.
Cheng, J., Cui, L., Effects of high-intensity ultrasound on the structural, optical, mechanical and physicochemical properties of pea protein isolate-based edible film. Ultrason. Sonochem., 80, 2021, 105809, 10.1016/J.ULTSONCH.2021.105809.
Zhang, X., Lei, Y., Luo, X., Wang, Y., Li, Y., Li, B., Liu, S., Impact of pH on the interaction between soybean protein isolate and oxidized bacterial cellulose at oil-water interface: dilatational rheological and emulsifying properties. Food Hydrocoll., 115, 2021, 106609, 10.1016/j.foodhyd.2021.106609.
Hu, H., Wu, J., Li-Chan, E.C.Y., Zhu, L., Zhang, F., Xu, X., Fan, G., Wang, L., Huang, X., Pan, S., Effects of ultrasound on structural and physical properties of soy protein isolate (SPI) dispersions. Food Hydrocoll. 30 (2013), 647–655, 10.1016/J.FOODHYD.2012.08.001.
Gong, K., Chen, L., Xia, H., Dai, H., Li, X., Sun, L., Kong, W., Liu, K., Driving forces of disaggregation and reaggregation of peanut protein isolates in aqueous dispersion induced by high-pressure microfluidization. Int. J. Biol. Macromol. 130 (2019), 915–921, 10.1016/J.IJBIOMAC.2019.02.123.
Andlinger, D.J., Röscheisen, P., Hengst, C., Kulozik, U., Influence of pH, temperature and protease inhibitors on kinetics and mechanism of thermally induced aggregation of potato proteins. Foods, 10, 2021, 796, 10.3390/foods10040796.
Dombrowski, J., Gschwendtner, M., Kulozik, U., Evaluation of structural characteristics determining surface and foaming properties of β-lactoglobulin aggregates. Colloids Surf. A Physicochem. Eng. Asp. 516 (2017), 286–295, 10.1016/j.colsurfa.2016.12.045.
Delahaije, R.J.B.M., Wierenga, P.A., van Nieuwenhuijzen, N.H., Giuseppin, M.L.F., Gruppen, H., Protein concentration and protein-exposed hydrophobicity as dominant parameters determining the flocculation of protein-stabilized oil-in-water emulsions. Langmuir 29 (2013), 11567–11574, 10.1021/la401314a.
Lan, Y., Chen, B., Rao, J., Pea protein isolate–high methoxyl pectin soluble complexes for improving pea protein functionality: effect of pH, biopolymer ratio and concentrations. Food Hydrocoll. 80 (2018), 245–253, 10.1016/J.FOODHYD.2018.02.021.
Zhao, W., Chen, Y., Liu, Z., Wang, L., Li, X., Effects of surface-modified coal-bearing metakaolin and graphene oxide on the properties of cement mortar. Constr. Build. Mater., 372, 2023, 130796, 10.1016/j.conbuildmat.2023.130796.
Jagdale, S., Karekar, S., Bird's eye view on aquasome: formulation and application. J. Drug Deliv. Sci. Technol., 58, 2020, 101776, 10.1016/j.jddst.2020.101776.
Dhinesh Kumar, D., Valan Arasu, A., A comprehensive review of preparation, characterization, properties and stability of hybrid nanofluids. Renew. Sust. Energ. Rev. 81 (2018), 1669–1689, 10.1016/j.rser.2017.05.257.
Liu, J., Tu, L., Cheng, M., Feng, J., Jin, Y., Mechanisms for oral absorption enhancement of drugs by nanocrystals. J. Drug Deliv. Sci. Technol., 56, 2020, 101607, 10.1016/j.jddst.2020.101607.
Moll, P., Salminen, H., Seitz, O., Schmitt, C., Weiss, J., Characterization of soluble and insoluble fractions obtained from a commercial pea protein isolate. J. Dispers. Sci. Technol., 2022, 1–12, 10.1080/01932691.2022.2093214.
Grasberger, K.F., Lund, F.W., Simonsen, A.C., Hammershøj, M., Fischer, P., Corredig, M., Role of the pea protein aggregation state on their interfacial properties. J. Colloid Interface Sci. 658 (2024), 156–166, 10.1016/J.JCIS.2023.12.068.
Yang, J., Huang, F., Huang, Q., Ma, D., Chen, Y., Peng, D., Yu, X., Deng, Q., Geng, F., Physical and emulsifying properties of pea protein: influence of combined physical modification by flaxseed gum and ultrasonic treatment. Food Sci. Human Wellness 12 (2023), 431–441, 10.1016/J.FSHW.2022.07.045.
Chang, C., Tu, S., Ghosh, S., Nickerson, M.T., Effect of pH on the inter-relationships between the physicochemical, interfacial and emulsifying properties for pea, soy, lentil and canola protein isolates. Food Res. Int. 77 (2015), 360–367, 10.1016/J.FOODRES.2015.08.012.
Gharsallaoui, A., Cases, E., Chambin, O., Saurel, R., Interfacial and emulsifying characteristics of acid-treated pea protein. Food Biophys. 4 (2009), 273–280, 10.1007/s11483-009-9125-8.
Gueguen, J., Barbot, J., Quantitative and Qualitative Variability of Pea (Pisum sativum L.) Protein Composition. 1988.
Yildiz, G., Andrade, J., Engeseth, N.E., Feng, H., Functionalizing soy protein nano-aggregates with pH-shifting and mano-thermo-sonication. J. Colloid Interface Sci. 505 (2017), 836–846, 10.1016/j.jcis.2017.06.088.
Tang, Q., Roos, Y.H., Miao, S., Plant protein versus dairy proteins: a pH-dependency investigation on their structure and functional properties. Foods, 12, 2023, 368, 10.3390/foods12020368.
Jiang, J., Chen, J., Xiong, Y.L., Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes. J. Agric. Food Chem. 57 (2009), 7576–7583, 10.1021/jf901585n.
Figueroa-González, J.J., Lobato-Calleros, C., Vernon-Carter, E.J., Aguirre-Mandujano, E., Alvarez-Ramirez, J., Martínez-Velasco, A., Modifying the structure, physicochemical properties, and foaming ability of amaranth protein by dual pH-shifting and ultrasound treatments. LWT, 153, 2022, 112561, 10.1016/j.lwt.2021.112561.
Lao, Y., Ye, Q., Wang, Y., Vongsvivut, J., Selomulya, C., Quantifying the effects of pre-roasting on structural and functional properties of yellow pea proteins. Food Res. Int., 172, 2023, 113180, 10.1016/j.foodres.2023.113180.
Zhao, R., Fu, W., Li, D., Dong, C., Bao, Z., Wang, C., Structure and functionality of whey protein, pea protein, and mixed whey and pea proteins treated by pH shift or high-intensity ultrasound. J. Dairy Sci. 107 (2024), 726–741, 10.3168/jds.2023-23742.
Yang, F., Yang, J., Qiu, S., Xu, W., Wang, Y., Tannic acid enhanced the physical and oxidative stability of chitin particles stabilized oil in water emulsion. Food Chem., 346, 2021, 128762, 10.1016/j.foodchem.2020.128762.
Chen, Y., Li, L., Zhao, X., Zeng, X., Xu, X., How environmental stresses affect the physical stability of oil in water emulsion prepared using pH-shifted myofibrillar protein?. LWT, 186, 2023, 115200, 10.1016/j.lwt.2023.115200.
Stone, A.K., Karalash, A., Tyler, R.T., Warkentin, T.D., Nickerson, M.T., Functional attributes of pea protein isolates prepared using different extraction methods and cultivars. Food Res. Int. 76 (2015), 31–38, 10.1016/j.foodres.2014.11.017.
Manoi, K., Rizvi, S.S.H., Emulsification mechanisms and characterizations of cold, gel-like emulsions produced from texturized whey protein concentrate. Food Hydrocoll. 23 (2009), 1837–1847, 10.1016/j.foodhyd.2009.02.011.
Chang, L., Chen, B., Rao, J., Synergistic effect of pH-shift and controlled heating on improving foaming properties of pea vicilin and its adsorption behavior at the air-water interface. Food Hydrocoll., 145, 2023, 109022, 10.1016/j.foodhyd.2023.109022.
Burger, T.G., Singh, I., Mayfield, C., Baumert, J.L., Zhang, Y., Comparison of Physicochemical and Emulsifying Properties of Commercial Pea Protein Powders. 2021, 10.1002/jsfa.11592.
Sun, H., Sun, J., Dou, N., Li, J., Hussain, M.A., Ma, J., Hou, J., Characterization and comparison of structure, thermal and functional characteristics of various commercial pea proteins. Food Biosci., 53, 2023, 102740, 10.1016/j.fbio.2023.102740.
Zhang, S., Cheng, J., Xie, Q., Jiang, S., Sun, Y., Foaming and physicochemical properties of commercial protein ingredients used for infant formula formulation. Foods, 11, 2022, 3710, 10.3390/foods11223710.
Kitabatake, N., Doi, E., Surface tension and foaming of protein solutions. J. Food Sci. 47 (1982), 1218–1221, 10.1111/j.1365-2621.1982.tb07651.x.