The DOI matches its Crossref record; 40 of the 41 references it cites were found in a registry or an index.
Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“Gels can be classified into transparent and opaque gels depending on the types of protein aggregates.Transparent gels are formed by fibrillar aggregates, while opaque gels are formed by particulate aggregates (Bryant and McClements 1998).”
From A Review of Gelation of Plant Proteins and Their Influencing Factors (2025) · cites this paper as Bryant and McClements 1998
In the citing paper
“Hydrophobic interactions play a major role in determining the conformation and interaction of protein molecules (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“It should be noted that hydrophobic interactions increase up to a maximum at about 60 to 70°C, at which point they begin to slowly lose strength as the temperature is further increased (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“Electrostatic repulsion increases with increasing temperature (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“Hydrophobic interactions tend to increase in strength with temperature (Bryant and McClements, 1998”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
In the citing paper
“They manifest themselves as strong attractive forces between nonpolar groups separated by water.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Bryant and McClements, 1998
Citations
Cites
Intermolecular and Surface Forces
(2011) · Elsevier eBooks · doi:10.1016/b978-0-12-391927-4.10024-6 · Cited by 17,242
Dominant forces in protein folding
Dill, K. A. (1990) · Biochemistry · doi:10.1021/bi00483a001 · Cited by 3,829
Hydrogen bonding in globular proteins
Baker, E. N., & Hubbard, R. E. (1984) · Progress in Biophysics and Molecular Biology · doi:10.1016/0079-6107(84)90007-5 · Cited by 1,860
Lumry, R. W., & Rajender, S. (1970) · Biopolymers · doi:10.1002/bip.1970.360091002 · Cited by 1,224
The colloidal domain: where physics, chemistry, biology, and technology meet
(1995) · Choice Reviews Online · doi:10.5860/choice.32-3315 · Cited by 1,130
An introduction to food colloids
(1992) · Choice Reviews Online · doi:10.5860/choice.30-2095 · Cited by 1,036
Némethy, G., & Scheraga, H. A. (1962) · The Journal of Physical Chemistry · doi:10.1021/j100816a004 · Cited by 974
Temperature dependence of the hydrophobic interaction in protein folding.
Baldwin, R. L. (1986) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.83.21.8069 · Cited by 900
Ben-Naim, A. Y. (1980) · Springer eBooks · doi:10.1007/978-1-4684-3545-0 · Cited by 651
Proteins in Whey: Chemical, Physical, and Functional Properties
Kinsella, J. E., & Whitehead, D. M. (1989) · Advances in food and nutrition research · doi:10.1016/s1043-4526(08)60130-8 · Cited by 619
Research works printed but not linked: 6
- Kinsella, J.E. (1982) ‘Relationships Between Structure and Functional Properties of Food Proteins’ in Food Proteins (P.F. Fox and J.J. Condon, eds), pp. 51–103, Applied Science
- Kilara, A. and Harwalker, V.R. (1996) ‘Denaturation’ in Food Proteins: Properties and Characterization (S. Nakai and H.W. Modler, eds), pp. 71–135, VCH Publishers, Inc
- Koning, M.M.G. and Visser, H. (1992) in Protein Interactions (H. Visser, ed.) pp. 1–24, VCH Publishers
- Fennema, O.R. (1996) ‘Water and Ice’ in Food Chemistry (3rd edn.) (O.R. Fennema, ed.), pp. 17–94, Marcel Dekker, Inc
- Freidman, M. (1973) The Chemistry and Biochemistry of the Sulfhydril Group in Amino Acids, Peptides and Proteins, Pergamon Press
- Hvidt, A. and Westh, P. (1992) ‘Stabilization and Destabilization of Protein Conformations’ in Protein Interactions (H. Visser, ed.), pp. 327–343, VCH Publishers
Cited by
Sorted by citations
Items 101–200 of 643
Xue, S., Xu, X., Shan, H., Wang, H., Yang, J., & Zhou, G. (2017) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2017.12.007 · Cited by 104
Cavallieri, Â. L. F., & Cunha, R. L. (2007) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2007.01.001 · Cited by 104
Influence of sugars on the characteristics of glucono-δ-lactone-induced soy protein isolate gels
Gu, X., Campbell, L. J., & Euston, S. R. (2008) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2008.01.005 · Cited by 104
Whey proteins: Musings on denaturation, aggregate formation and gelation
Wagner, J., Βiliaderis, C. G., & Moschakis, T. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2019.1708263 · Cited by 103
Khalesi, H., Sun, C., He, J., Lu, W. J., & Fang, Y. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109856 · Cited by 103
Qin, X., Yuan, D., Wang, Q., Hu, Z., Wu, Y., Cai, J., Huang, Q., Li, S., & Liu, G. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b03125 · Cited by 102
Xu, Y., Sun, L., Zhuang, Y., Gu, Y., Cheng, G., Fan, X., Ding, Y., & Liu, H. (2023) · Foods · doi:10.3390/foods12142703 · Cited by 103
Jones, O. G., & McClements, D. J. (2010) · Journal of Food Science · doi:10.1111/j.1750-3841.2009.01512.x · Cited by 101
Self-citationRheological and Physical Properties of Derivitized Whey Protein Isolate Powders
Hudson, H. M., Daubert, C. R., & Foegeding, E. A. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf990906s · Cited by 101
Mao, L., Miao, S., Yuan, F., & Gao, Y. (2017) · Food Research International · doi:10.1016/j.foodres.2017.10.024 · Cited by 100
Nieto-Nieto, T. V., Wang, Y., Ozimek, L., & Chen, L. (2016) · Food Research International · doi:10.1016/j.foodres.2016.01.027 · Cited by 99
Li, Z., Xi, J., Chen, H., Chen, W., Chen, W., Zhong, Q., & Zhang, M. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111363 · Cited by 99
Gonzalez-Jordan, A., Nicolai, T., & Benyahia, L. (2016) · Langmuir · doi:10.1021/acs.langmuir.6b01993 · Cited by 85
Formation of soluble whey protein aggregates and their stability in beverages
Ryan, K. N., & Foegeding, E. A. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.05.025 · Cited by 97
Calcium-induced gelation of whey protein aggregates: Kinetics, structure and rheological properties
Kharlamova, A., Nicolaï, T., & Chassenieux, C. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.11.049 · Cited by 97
Zhou, P., Liu, X., & Labuza, T. P. (2008) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf073216u · Cited by 95
Heat induced formation of beta-lactoglobulin microgels driven by addition of calcium ions
Phan-Xuan, T., Durand, D., Nicolaï, T., Donato, L., Schmitt, C., & Bovetto, L. (2012) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2012.09.008 · Cited by 93
Nyemb, K., Guérin‐Dubiard, C., Dupont, D., Jardin, J., Rutherfurd, S. M., & Nau, F. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.02.048 · Cited by 93
Control of Heat-Induced Aggregation of Whey Proteins Using Casein
O’Kennedy, B. T., & Mounsey, J. S. (2006) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0607866 · Cited by 93
Zhu, P., Huang, W., & Chen, L. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107373 · Cited by 89
Microencapsulation of Garcinia fruit extract by spray drying and its effect on bread quality.
Ezhilarasi, P., Indrani, D., Jena, B., & Anandharamakrishnan, C. (2014) · The Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.6378 · Cited by 70
Rheology and characteristics of sulfated polysaccharides from chlorophytan seaweeds Ulva fasciata
Shao, P., Qin, M., Han, L., & Sun, P. (2014) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2014.07.008 · Cited by 90
Paglarini, C. D. S., Vidal, V. A. S., Martini, S., Cunha, R. L., & Pollonio, M. A. R. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2020.1825322 · Cited by 90
“…be kept away (higher or lower) from the isoelectric point of the proteins to avoid immediate aggregation upon heating (and formation of disordered and weak structures), and the salt concentration must be low enough to prevent excessive aggregation of protein molecules (Bryant and McClements 1998).”
BackgroundKristinsson, H. G., & Ingadóttir, B. (2006) · Journal of Food Science · doi:10.1111/j.1365-2621.2006.tb15626.x · Cited by 90
Effect of preheating temperature and calcium ions on the properties of cold-set soybean protein gel
Lu, X., Lu, Z., Yin, L., Cheng, Y., & Li-te, L. (2010) · Food Research International · doi:10.1016/j.foodres.2010.05.011 · Cited by 91
Production of Whey Protein-Based Aggregates Under Ohmic Heating
Pereira, R. N., Rodrigues, R. M. M., Ramos, Ó. L., Malcata, F. X., Teixeira, J. A., & Vicente, A. A. (2015) · Food and Bioprocess Technology · doi:10.1007/s11947-015-1651-4 · Cited by 90
“Production and development of β-lg and WPI hydrogels have been studied extensively during the latest decades (Bryant and McClements 1998; Kavanagh et al. 2000; Lefevre and Subirade 2000; Phan-Xuan et al. 2013; Stading and Hermansson 1990, 1991; Stading et al. 1992).”
BackgroundEffect of protein–surfactant interactions on aggregation of β-lactoglobulin
Hansted, J. G., Wejse, P. L., Bertelsen, H., & Otzen, D. E. (2011) · Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics · doi:10.1016/j.bbapap.2011.03.011 · Cited by 89
Nafchi, A. M., طباطبایی, ر. ه., Pashania, B., رجبی, ح. ز., & Karim, A. A. (2013) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2013.09.050 · Cited by 88
Linoleic acid binding properties of ovalbumin nanoparticles
Sponton, O. E., Pérez, A. A., Carrara, C. R., & Santiago, L. G. (2015) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2015.01.037 · Cited by 87
Salt-Induced Gelation of Globular Protein Aggregates: Structure and Kinetics
Ako, K., Nicolaï, T., & Durand, D. (2010) · Biomacromolecules · doi:10.1021/bm9011437 · Cited by 86
Shao, P., Ma, H., Zhu, J., & Qiu, Q. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.01.039 · Cited by 85
On the reversibility of ethanol-induced whey protein denaturation
Nikolaidis, A., & Moschakis, T. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.05.051 · Cited by 85
Effects of Thermal Denaturation on Binding between Bixin and Whey Protein
Zhang, Y., & Zhong, Q. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf3021656 · Cited by 85
Effect of salt ions on mixed gels of wheat gluten protein and potato isolate protein
Zhang, Z., Chen, X., Liu, X., Liu, W., Liu, Q., Huang, J., Zhang, L., & Hu, H. (2021) · LWT · doi:10.1016/j.lwt.2021.112564 · Cited by 84
Chen, L., & Subirade, M. (2006) · European Journal of Pharmaceutics and Biopharmaceutics · doi:10.1016/j.ejpb.2006.10.012 · Cited by 83
Eugenol improves physical and chemical stabilities of nanoemulsions loaded with β-carotene
Guan, Y., Wu, J., & Zhong, Q. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.08.097 · Cited by 83
Effect of modified whey protein concentrate on physical properties and stability of whipped cream
Sajedi, M., Nasirpour, A., Keramat, J., & Desobry, S. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.09.007 · Cited by 82
Mocanu, A. M., Moldoveanu, C. C., Odochian, L., Păiuş, C., Apostolescu, N., & Neculau, R. (2012) · Thermochimica Acta · doi:10.1016/j.tca.2012.07.031 · Cited by 81
Cold Gelation of β‐lactoglobulin in the Presence of Iron
Remondetto, G. E., Paquin, P., & Subirade, M. (2002) · Journal of Food Science · doi:10.1111/j.1365-2621.2002.tb10643.x · Cited by 81
Physical effects upon whey protein aggregation for nano-coating production
Ramos, Ó. L., Pereira, R. N., Rodrigues, R. M. M., Teixeira, J. A., Vicente, A. A., & Malcata, F. X. (2014) · Food Research International · doi:10.1016/j.foodres.2014.09.036 · Cited by 80
“Distinct molecular interactions between protein molecules have been reviewed elsewhere (Bryant & McClements, 1998; Pérez-Gago et al., 1999), and are summarized in Table 2.”
InfluentialBrannan, R. G., Mah, E., Schott, M., Yuan, S., Casher, K. L., Myers, A. S., & Herrick, C. S. (2013) · European Journal of Lipid Science and Technology · doi:10.1002/ejlt.201200308 · Cited by 80
Rennet coagulation of heated milk: A review
Britten, M., & Giroux, H. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105179 · Cited by 66
Zhang, W., & Zhong, Q. (2009) · Food Chemistry · doi:10.1016/j.foodchem.2009.08.043 · Cited by 79
Herceg, Z., Jambrak, A. ., Lelas, V., Krešić, G., & Franetović, M. (2006) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2006.01.055 · Cited by 78
Wang, W., Bao, Y., Hendricks, G. M., & Guo, M. (2011) · International Dairy Journal · doi:10.1016/j.idairyj.2011.09.007 · Cited by 77
Composite hydrogels assembled from food-grade biopolymers: Fabrication, properties, and applications
McClements, D. J. (2024) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2024.103278 · Cited by 76
Self-citationHong, G. P., & Chin, K. B. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.11.011 · Cited by 75
Gelation of Native β-Lactoglobulin Induced by Electrostatic Attractive Interaction with Xanthan Gum
Laneuville, S. I., Turgeon, S. L., Sanchez, C., & Paquin, P. (2006) · Langmuir · doi:10.1021/la060149+ · Cited by 75
Improving the structure and rheology of high protein, low fat yoghurt with undenatured whey proteins
Jørgensen, C. E., Abrahamsen, R. K., Rukke, E., Johansen, A., Schüller, R. B., & Skeie, S. B. (2015) · International Dairy Journal · doi:10.1016/j.idairyj.2015.02.002 · Cited by 75
Kumar, P., Sharma, N., Ahmed, M. A., Verma, A. K., Umaraw, P., Mehta, N. R., Abubakar, A. A., Hayat, M. N., Kaka, U., Lee, S., et al. (2022) · Frontiers in Nutrition · doi:10.3389/fnut.2022.1044024 · Cited by 75
“Hydrophobic interactions induce network formation in solutions of filamentous aggregates and on their gel formation, other forces also consolidate the network, resulting in further improving gel strength (139), homogenous cold-set gels are transparent (140).”
BackgroundLi, B., Jiang, Y., Liu, F., Chai, Z., Li, Y., Li, Y., & Leng, X. (2011) · International Journal of Food Science & Technology · doi:10.1111/j.1365-2621.2011.02832.x · Cited by 74
Rheology and microstructure of cross-linked waxy maize starch/whey protein suspensions
Dang, H. V., Loisel, C., Desrumaux, A., & Doublier, J. L. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.01.004 · Cited by 74
Protein in Cheese and Cheese Products: Structure-Function Relationships
Guinee, T. P. (2015) · Springer eBooks · doi:10.1007/978-1-4939-2800-2_14 · Cited by 76
Cheese: Structure, Rheology and Texture
Fox, P. F., Guinee, T. P., Cogan, T. M., & McSweeney, P. L. H. (2016) · Springer eBooks · doi:10.1007/978-1-4899-7681-9_14 · Cited by 72
Burgos‐Díaz, C., Wandersleben, T., Olivos, M., Lichtin, N., Bustamante, M., & Solans, C. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.09.018 · Cited by 77
Mulcahy, E. M., Fargier-Lagrange, M., Mulvihill, D. M., & O'Mahony, J. A. (2017) · Food Chemistry · doi:10.1016/j.foodchem.2017.01.155 · Cited by 63
“Bryant and McClements (1998) reported that protein-protein interactions in whey protein solutions were promoted in a high ionic strength environment as bonds can form at several points on the surface of the protein molecules (due to a reduction in the electrostatic repulsion), leading to the formation of large, roughl…”
InfluentialBuchmann, L., Bertsch, P., Böcker, L., Krähenmann, U., Fischer, P., & Mathys, A. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105182 · Cited by 72
“According to literature, immunoglobulins present in WPI have a pI between pH 5.5 to 6.8 (Bryant & McClements, 1998).”
InfluentialDevelopment and Characterization of Whey Protein-Based Nano-Delivery Systems: A Review
Ha, H., Rankin, S. A., Lee, M.-R., & Lee, W.-J. (2019) · Molecules · doi:10.3390/molecules24183254 · Cited by 72
“Moreover, the use of whey protein, such as β-lg, is beneficial for the oral delivery of BCs since the pepsin resistance of native β-lg in the stomach can be utilized for the effective protection of entrapped BCs against the harsh gastric environment [10,14].”
BackgroundMolecular Description of the Formation and Structure of Plasticized Globular Protein Films
Lefèvre, T., Subirade, M., & Pézolet, M. (2005) · Biomacromolecules · doi:10.1021/bm050540u · Cited by 71
Microfluidization initiated cross-linking of gliadin particles for structured algal oil emulsions
Liu, X., Liu, Y., Guo, J., Yin, S., & Yang, X. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.07.001 · Cited by 71
Combined effect of heat treatment and ionic strength on the functionality of whey proteins
Hussain, R., Gaïani, C., Jeandel, C., Ghanbaja, J., & Scher, J. (2012) · Journal of Dairy Science · doi:10.3168/jds.2012-5416 · Cited by 70
“The lack of gelation in the absence of salt occurs because protein molecules have substantial negative charges; hence, a relatively strong electrostatic repulsion occurs between unfolded protein molecules, which prevents them from coming into close proximity (Bryant and McClements, 1998).”
BackgroundRodrigues, R. M. M., Fasolin, L. H., Avelar, Z., Petersen, S. B., Vicente, A. A., & Pereira, R. N. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105505 · Cited by 69
O’Mahony, J. A., McSweeney, P. L. H., & Lucey, J. A. (2006) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(06)72154-3 · Cited by 68
“Hydrophobic interactions, another principal structural agent in casein micelles, increase in strength with increasing temperature and reach a maximum at approximately 70°C (Bryant and McClements, 1998; Lucey et al., 2003).”
BackgroundZhang, Y., Yang, R., Zhang, W., Hu, Z., & Zhao, W. (2016) · Food Chemistry · doi:10.1016/j.foodchem.2016.09.079 · Cited by 69
RHEOLOGICAL AND PHYSICOCHEMICAL PROPERTIES OF DERIVATIZED WHEY PROTEIN CONCENTRATE POWDERS
Resch, J. J., & Daubert, C. R. (2002) · International Journal of Food Properties · doi:10.1081/jfp-120005795 · Cited by 69
“As the salt concentration is increased, the electrostatic repulsions are completely shielded and attractive forces dominate, resulting in protein aggregation and the formation of a particulate gel.([22]) Hudson et al.”
BackgroundCurrent ways to modify the structure of whey proteins for specific functionalities—a review
Guyomarc’H, F., Famelart, M., Henry, G., Gulzar, M., Léonil, J., Hamon, P., Bouhallab, S., & Croguennec, T. (2014) · Dairy Science and Technology · doi:10.1007/s13594-014-0190-5 · Cited by 68
“At sufficient protein concentration, soluble aggregates formed on heating can associate together at room temperature and form a gel when their charges are shielded by adding salt or reducing pH close to pI of aggregate (Bryant and Mcclements 1998).”
BackgroundElectrospinning of food-grade nanofibres from whey protein
Zhong, J., Mohan, S. D., Bell, A., Terry, A. E., Mitchell, G. R., & Davis, F. J. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.02.113 · Cited by 67
Sun, H., Zhang, M., Liu, Y., Wang, Y., Chen, Y., Guan, W., Li, X., & Wang, Y. (2021) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2021.117843 · Cited by 67
Brito‐Oliveira, T. C., Bispo, M., Moraes, I. C. F., Campanella, O. H., & Pinho, S. C. (2017) · Food Research International · doi:10.1016/j.foodres.2017.09.071 · Cited by 67
Stability, microstructure and rheological behavior of konjac glucomannan-zein mixed systems
Ni, X., Wang, K., Wu, K., Corke, H., Nishinari, K., & Jiang, F. (2018) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.02.001 · Cited by 67
Acid-induced gelation of whey protein aggregates: Kinetics, gel structure and rheological properties
Kharlamova, A., Chassenieux, C., & Nicolai, T. (2018) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2018.02.043 · Cited by 83
Wang, W., & Zhong, Q. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.11.018 · Cited by 66
Emulsifying and Foaming Properties of a Derivatized Whey Protein Ingredient
Firebaugh, J. D., & Daubert, C. R. (2005) · International Journal of Food Properties · doi:10.1081/jfp-200060245 · Cited by 66
Kutzli, I., Gibis, M., Baier, S. K., & Weiß, J. (2018) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b02104 · Cited by 66
Khaldi, M., Blanpain-Avet, P., Guérin, R., Ronse, G., Bouvier, L., André, C., Bornaz, S., Croguennec, T., Jeantet, R., & Delaplace, G. (2014) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2014.09.020 · Cited by 65
“The first phenomenon is related to intermolecular cross-linking of adjacent negatively-charged or carboxylic groups by the formation of protein–Ca–protein complexes (Bryant and McClements, 1998; Hongsprabhas et al., 1999).”
BackgroundEffect of whey protein agglomeration on spray dried microcapsules containing Saccharomyces boulardii
Duongthingoc, D., George, P., Katopo, L., Gorczyca, E., & Kasapis, S. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.04.093 · Cited by 65
Nanoscale Understanding of Thermal Aggregation of Whey Protein Pretreated by Transglutaminase
Wang, W., Zhong, Q., & Hu, Z. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf304506n · Cited by 65
Hsein, H., Garrait, G., Beyssac, E., & Hoffart, V. (2015) · Colloids and Surfaces B Biointerfaces · doi:10.1016/j.colsurfb.2015.10.016 · Cited by 65
Joyce, A., Kelly, A., & O'Mahony, J. A. (2018) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12507 · Cited by 62
Technological strategies to improve gelation properties of legume proteins with the focus on lupin
Al‐Ali, H., Shah, U., Hackett, M. J., Gulzar, M., Karakyriakos, E., & Johnson, S. K. (2021) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2021.102634 · Cited by 65
Baier, S. K., & McClements, D. J. (2005) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2005.tb00072.x · Cited by 64
Self-citationThermal aggregation and ion-induced cold-gelation of bovine serum albumin
Navarra, G., Giacomazza, D., Leone, M., Librizzi, F., Militello, V., & Biagio, P. L. S. (2009) · European Biophysics Journal · doi:10.1007/s00249-008-0389-6 · Cited by 68
“temperature of the heat treatment has a significant influence on the rate of gelation and on the morphological aspect of the final gel, while the protein concentration mainly affects the mechanical properties of gels formed ( Bryant and McClements 1998 ).”
BackgroundInfluentialEnzymatic Hydrolysis as a Means of Expanding the Cold Gelation Conditions of Soy Proteins
Kuipers, B. J. H., van Koningsveld, G. A., Alting, A. C., Driehuis, F., Gruppen, H., & Voragen, A. G. J. (2005) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf048622h · Cited by 64
Mäkinen, O. E., Zannini, E., & Arendt, E. K. (2015) · Plant Foods for Human Nutrition · doi:10.1007/s11130-015-0487-4 · Cited by 64
“, pH, temperature, ionic strength influence the properties of the formed aggregates [11, 12].”
BackgroundMethodInfluence of moderate electric fields in β-lactoglobulin thermal unfolding and interactions
Rodrigues, R. M. M., Avelar, Z., Vicente, A. A., Petersen, S. B., & Pereira, R. N. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.125442 · Cited by 64
Lipid and water crystallization in protein-stabilised oil-in-water emulsions
Cornacchia, L., & Roos, Y. H. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.03.014 · Cited by 63
Qi, P. X., Xiao, Y., & Wickham, E. D. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.12.032 · Cited by 63
Electric field effects on proteins – Novel perspectives on food and potential health implications
Rodrigues, R. M. M., Avelar, Z., Machado, L. F., Pereira, R. N., & Vicente, A. A. (2020) · Food Research International · doi:10.1016/j.foodres.2020.109709 · Cited by 63
Zhang, T., McCarthy, J., Wang, G., Liu, Y., & Guo, M. (2015) · Journal of Food Science · doi:10.1111/1750-3841.12834 · Cited by 63
Microemulsification–cold gelation of whey proteins for nanoencapsulation of date palm pit extract
Sadeghi, S., Madadlou, A., & Yarmand, M. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.07.021 · Cited by 62
Protein aggregation and gel formation studied with scattering methods and computer simulations
Nicolaï, T., & Durand, D. (2007) · Current Opinion in Colloid & Interface Science · doi:10.1016/j.cocis.2007.03.002 · Cited by 62
“This process happens even at room temperature and is often called coldgelation to distinguish it from the heat-induced aggregation of proteins [35].”
BackgroundPicot, A., & Lacroix, C. (2003) · Journal of Food Science · doi:10.1111/j.1365-2621.2003.tb05790.x · Cited by 62
Chen, N., Chassenieux, C., & Nicolaï, T. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2017.09.021 · Cited by 61
Heat-induced and acid-induced gelation of dairy/plant protein dispersions and emulsions
Schmitt, C., Silva, J. V. C., Amagliani, L., Chassenieux, C., & Nicolaï, T. (2019) · Current Opinion in Food Science · doi:10.1016/j.cofs.2019.05.002 · Cited by 60
Mehalebi, S., Nicolaï, T., & Durand, D. (2008) · Soft Matter · doi:10.1039/b718640a · Cited by 60
Lei, L., Zhao, Q., Selomulya, C., & Xiong, H. (2015) · Food Chemistry · doi:10.1016/j.foodchem.2015.01.081 · Cited by 59
Yılmaz, M. T., Karaman, S., Cankurt, H., Kayacıer, A., & Sağdıç, O. (2010) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2010.10.016 · Cited by 59
Protein-Based Nanostructures for Food Applications
Bourbon, A. I., Pereira, R. N., Pastrana, L. M., Vicente, A. A., & Cerqueira, M. Â. (2019) · Gels · doi:10.3390/gels5010009 · Cited by 59
“Consequently, high temperature, above the protein denaturation level is a key parameter for accelerating whey protein aggregation [26].”
BackgroundInfluence of sucrose on NaCl-induced gelation of heat denatured whey protein solutions
Bryant, C. M., & McClements, D. J. (2000) · Food Research International · doi:10.1016/s0963-9969(00)00109-5 · Cited by 58
Self-citationA comparative study of the gelation properties of whey protein concentrate and whey protein isolate
Lorenzen, P. C., & Schrader, K. (2006) · Le Lait · doi:10.1051/lait:2006008 · Cited by 58
“The gelation itself is induced by adding salt (transparent gels) or acid (turbid gels) to the heat-treated protein solutions after cooling [1, 4, 33, 38].”
Background
Metadata
- Authors
- Bryant, C. M., & McClements, D. J.
- Affiliations
- University of Massachusetts Amherst (US)
- Corresponding author
- Bryant, Cory M
- ORCID
- McClements, D.Julian
- Venue
- Trends in Food Science & Technology
- Publisher
- Elsevier BV
- Published
- 1998-04
- Volume
- 9
- Issue
- 4
- Pages
- 143-151
- ISSN
- 0924-2244 (ISSN-L)
- OpenAlex
- W2034747455
- Cited by
- 643
- References
- 41
- Citations by year
- 2026: 16 · 2025: 19 · 2024: 25 · 2023: 21 · 2022: 20 · 2021: 34 · 2020: 29 · 2019: 41 · 2018: 40 · 2017: 36 · 2016: 34 · 2015: 38 · 2014: 37 · 2013: 36 · 2012: 37
- FWCI
- 13.95
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Trends in Food Science & Technology (publishedVersion)
- Topics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Structure and Dynamics
- Life Sciences › Agricultural and Biological Sciences › Food Science › Polysaccharides Composition and Applications
- Keywords
- whey protein, cold-set gels, protein functional properties, emulsification, gelation, thickening, foaming, water holding capacity, functional food ingredients
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review
