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
Food protein-based materials as nutraceutical delivery systems
Chen, L., Remondetto, G. E., & Subirade, M. (2006) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2005.12.011 · Cited by 1,183
“egg white, soybean, and whey proteins) has attracted much attention over the years because of its physicochemical and industrial significance (Bryant and McClement, 1998; Clark, Kavanagh, & Ross-Murphy, 2001; Clark & Ross-Murphy, 1987; Ziegler & Foegeding 1990).”
BackgroundInvited review: perspectives on the basis of the rheology and texture properties of cheese.
Lucey, J. A., Johnson, M. E., & Horne, D. S. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73869-7 · Cited by 723
β-Lactoglobulin and WPI aggregates: Formation, structure and applications
Nicolaï, T., Britten, M., & Schmitt, C. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.02.006 · Cited by 575
Mezzenga, R., & Fischer, P. (2013) · Reports on Progress in Physics · doi:10.1088/0034-4885/76/4/046601 · Cited by 560
“Furthermore, in addition to these potentials, other interactions play an important role in the phase behavior of proteins: hydrophobic interactions, hydration, solvation and hydrogen bonds, hydrophilic interaction, charge residues complementarity, salt specificity effects and molecular recognition all contribute to in…”
BackgroundEffect of ultrasound treatment on solubility and foaming properties of whey protein suspensions
Jambrak, A. ., Mason, T. J., Lelas, V., Herceg, Z., & Herceg, I. L. (2007) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2007.10.004 · Cited by 550
“Whey are widely used as ingredients in foods due to their unique functional properties, i.e. emulsification, gelation, thickening, foaming, and fat and flavor binding capacity (Bryant and McClements, 1998; McClements, 1995; Mason, 1998).”
BackgroundMatalanis, A., Jones, O. G., & McClements, D. J. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.04.014 · Cited by 530
Self-citationPhysical properties of ultrasound treated soy proteins
Jambrak, A. ., Lelas, V., Mason, T. J., Krešić, G., & Badanjak, M. (2009) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2009.02.001 · Cited by 523
“The high increase in temperature is causing denaturation of soy proteins and leads to gelling (Bryant and McClements, 1998).”
BackgroundCasein-based formulations as promising controlled release drug delivery systems
Elzoghby, A. O., El-Fotoh, W. S. A., & Elgindy, N. A. (2011) · Journal of Controlled Release · doi:10.1016/j.jconrel.2011.02.010 · Cited by 526
Composition, physicochemical properties of pea protein and its application in functional foods
Lu, Z. X., He, J. F., Zhang, Y. C., & Bing, D. J. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2019.1651248 · Cited by 529
An overview on preparation of emulsion-filled gels and emulsion particulate gels
Farjami, T., & Madadlou, A. (2019) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2019.02.043 · Cited by 496
Advances in modifying and understanding whey protein functionality
Foegeding, E. A., Davis, J. P., Doucet, D., & McGuffey, M. K. (2002) · Trends in Food Science & Technology · doi:10.1016/s0924-2244(02)00111-5 · Cited by 433
Effect of ultrasound treatment on particle size and molecular weight of whey proteins
Jambrak, A. ., Mason, T. J., Lelas, V., Paniwnyk, L., & Herceg, Z. (2013) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2013.08.012 · Cited by 402
Food Gels: Gelling Process and New Applications
Banerjee, S., & Bhattacharya, S. (2011) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2010.500234 · Cited by 388
“Ionic-induced gelation has been reported for pre-denatured whey proteins and in contrast to heat-induced gelation, is named cold gelation (Bryant and McClements, 1998; Alting et al., 2002).”
BackgroundAgro-Food Byproducts as a New Source of Natural Food Additives
Faustino, M., Veiga, M., Sousa, P., Costa, E. M., Silva, S., & Pintado, M. (2019) · Molecules · doi:10.3390/molecules24061056 · Cited by 367
“Whey proteins, obtained as a byproduct of the dairy industry, have many functional properties including gelation, thickening, and water-holding capacity [205].”
BackgroundLiang, X., Ma, C., Yan, X., Zeng, H., McClements, D. J., Liu, X., & Liu, F. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105569 · Cited by 346
Self-citationLoveday, S. M. (2019) · Annual Review of Food Science and Technology · doi:10.1146/annurev-food-032818-121128 · Cited by 325
Functional Biopolymer Particles: Design, Fabrication, and Applications
Jones, O. G., & McClements, D. J. (2010) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/j.1541-4337.2010.00118.x · Cited by 300
Self-citationApplication of inulin in cheese as prebiotic, fat replacer and texturizer: A review
Karimi, R., Azizi, M. H., Ghasemlou, M., & Vaziri, M. (2014) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2014.11.029 · Cited by 284
Oleogels/emulsion gels as novel saturated fat replacers in meat products: A review
Guo, J., Cui, L., & Meng, Z. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108313 · Cited by 278
Soy protein isolates: A review of their composition, aggregation, and gelation.
Zheng, L., Regenstein, J. M., Zhou, L., & Wang, Z. (2022) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12925 · Cited by 266
Gelation of food protein-protein mixtures.
Nicolai, T. (2019) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2019.06.006 · Cited by 263
Formation of Disulfide Bonds in Acid-Induced Gels of Preheated Whey Protein Isolate
Alting, A. C., Hamer, R. J., de Kruif, C. G., & Visschers, R. W. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf000474h · Cited by 248
Pérez-Gago, M. B., Nadaud, P., & Krochta, J. M. (1999) · Journal of Food Science · doi:10.1111/j.1365-2621.1999.tb12276.x · Cited by 244
Mession, J.-L., Sok, N., Assifaoui, A., & Saurel, R. (2013) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf303739n · Cited by 233
Mession, J.-L., Chihi, M. L., Sok, N., & Saurel, R. (2015) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.11.025 · Cited by 240
Nooshkam, M., & Varidi, M. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105389 · Cited by 235
Kan, X., Chen, G., Zhou, W., & Zeng, X. (2021) · Food Research International · doi:10.1016/j.foodres.2021.110740 · Cited by 223
Pérez-Gago, M. B., & Krochta, J. M. (2001) · Journal of Food Science · doi:10.1111/j.1365-2621.2001.tb04625.x · Cited by 218
Wang, W.-Q., Bao, Y., & Chen, Y. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.01.072 · Cited by 215
“Functionality of whey proteins as food ingredients has been extensively studied (Bryant & McClements, 1998).”
BackgroundEmulsion microgel particles: Novel encapsulation strategy for lipophilic molecules
Torres, O., Murray, B. S., & Sarkar, A. (2016) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2016.07.006 · Cited by 218
Doherty, S. B., Gee, V. L., Ross, R. P., Stanton, C., Fitzgerald, G. F., & Brodkorb, A. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2010.12.012 · Cited by 203
Marangoni, A. G. (2000) · Food Hydrocolloids · doi:10.1016/s0268-005x(99)00046-6 · Cited by 192
Formation of Soy Protein Isolate Cold‐set Gels: Protein and Salt Effects
Maltais, A., Remondetto, G. E., González, R. J., & Subirade, M. (2005) · Journal of Food Science · doi:10.1111/j.1365-2621.2005.tb09023.x · Cited by 192
Zhang, S., Huang, W., Feizollahi, E., Roopesh, M. S., & Chen, L. (2021) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2020.102567 · Cited by 188
Kao, F.-J., Su, N., & Lee, M.-H. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0342021 · Cited by 187
Flaxseed oil – Whey protein isolate emulsions: Effect of high pressure homogenization
Kuhn, K. R., & Cunha, R. L. (2012) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2012.01.016 · Cited by 186
Zhang, Z., Zhang, R., Chen, L., Tong, Q., & McClements, D. J. (2015) · European Polymer Journal · doi:10.1016/j.eurpolymj.2015.01.013 · Cited by 187
Self-citationJansens, K. J. A., Rombouts, I., Grootaert, C., Brijs, K., Camp, J. V., der Meeren, P. V., Rousseau, F., Schymkowitz, J. W. H., & Delcour, J. A. (2018) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.12404 · Cited by 188
Ezhilarasi, P., Indrani, D., Jena, B., & Anandharamakrishnan, C. (2013) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2013.01.009 · Cited by 174
Stability and mechanism of whey protein soluble aggregates thermally treated with salts
Ryan, K. N., Vardhanabhuti, B., Jaramillo, D., van Zanten, J. H., Coupland, J. N., & Foegeding, E. A. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.11.006 · Cited by 180
de Castro, R. J. S., Domingues, M. A. F., Ohara, A., Okuro, P. K., dos Santos, J. G., Brexó, R. P., & Sato, H. H. (2017) · Food Structure · doi:10.1016/j.foostr.2017.05.004 · Cited by 180
Kulmyrzaev, A., Bryant, C. M., & McClements, D. J. (2000) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf9911949 · Cited by 177
Self-citationHydrocolloid gels of polysaccharides and proteins
Nishinari, K., Zhang, H., & Ikeda, S. (2000) · Current Opinion in Colloid & Interface Science · doi:10.1016/s1359-0294(00)00053-4 · Cited by 175
Physical and Chemical Interactions in Cold Gelation of Food Proteins
Alting, A. C., de Jongh, H. H. J., Visschers, R. W., & Simons, J. F. A. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf011657m · Cited by 167
Alting, A. C., Hamer, R. J., de Kruif, C. G., Pâques, M., & Visschers, R. W. (2003) · Food Hydrocolloids · doi:10.1016/s0268-005x(03)00023-7 · Cited by 165
Xi, Z., Liu, W., McClements, D. J., & Zou, L. (2019) · Food Chemistry · doi:10.1016/j.foodchem.2019.04.011 · Cited by 165
Self-citationThermal aggregation properties of whey protein glycated with various saccharides
Liu, G., & Zhong, Q. (2013) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2012.12.008 · Cited by 151
Setiowati, A. D., Wijaya, W., & van der Meeren, P. (2020) · Trends in Food Science & Technology · doi:10.1016/j.tifs.2020.02.011 · Cited by 141
Alting, A. C., Hamer, R. J., de Kruif, C. G., & Visschers, R. W. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0209342 · Cited by 159
The Kinetics of Heat-Induced Structural Changes of β-Lactoglobulin
Sava, N., der Plancken, I. V., Claeys, W. L., & Hendrickx, M. (2005) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(05)72836-8 · Cited by 158
“In native β -LG, the free thiol group is masked in the hydrophobic interior of the protein and does not normally participate in a disulfide linkage (Bryant and McClements, 1998).”
BackgroundInfluence of NaCl and CaCl 2 on Cold‐Set Gelation of Heat‐denatured Whey Protein
Bryant, C. M., & McClements, D. J. (2000) · Journal of Food Science · doi:10.1111/j.1365-2621.2000.tb13590.x · Cited by 140
Self-citationGlycation of Whey Protein To Provide Steric Hindrance against Thermal Aggregation
Liu, G., & Zhong, Q. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf302883b · Cited by 153
Rheology of Emulsion-Filled Gels Applied to the Development of Food Materials
Geremias-Andrade, I. M., Souki, N. P. D. B. G., Moraes, I. C. F., & Pinho, S. C. (2016) · Gels · doi:10.3390/gels2030022 · Cited by 159
“Therefore, the denaturation and aggregation steps occur separately [27,33].”
BackgroundHall, A. E., & Moraru, C. I. (2021) · LWT · doi:10.1016/j.lwt.2021.112349 · Cited by 151
Khatkar, A. B., Kaur, A., Khatkar, S. K., & Mehta, N. (2018) · Ultrasonics Sonochemistry · doi:10.1016/j.ultsonch.2018.08.026 · Cited by 147
Nath, P. C., Debnath, S., Sridhar, K., Inbaraj, B. S., Nayak, P. K., & Sharma, M. (2022) · Gels · doi:10.3390/gels9010001 · Cited by 145
“It has been reported that pre-denatured whey proteins can undergo ionically induced gelation, which, in contrast to heat-induced gelation, is referred to as cold gelation [43,44].”
BackgroundMaltais, A., Remondetto, G. E., & Subirade, M. (2007) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2007.01.026 · Cited by 143
Veerman, C., Ruis, H. G. M., Sagis, L. M. C., & van der Linden, E. (2002) · Biomacromolecules · doi:10.1021/bm025533+ · Cited by 142
Kinetics of the breakdown of cross-linked soy protein films for drug delivery
Chen, L., Remondetto, G. E., Rouabhia, M., & Subirade, M. (2008) · Biomaterials · doi:10.1016/j.biomaterials.2008.05.025 · Cited by 141
Jiang, S., Hussain, M., Cheng, J., Jiang, Z., Geng, H., Sun, Y., Sun, C., & Hou, J. (2018) · LWT · doi:10.1016/j.lwt.2018.08.028 · Cited by 140
Cold gelation of β-lactoglobulin oil-in-water emulsions
Line, V. L. S., Remondetto, G. E., & Subirade, M. (2004) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2004.06.004 · Cited by 142
Brighenti, M., Govindasamy-Lucey, S., Lim, K., Nelson, K. L., & Lucey, J. A. (2008) · Journal of Dairy Science · doi:10.3168/jds.2008-1322 · Cited by 139
“Some of the weakening of gels with increasing temperature could also be due to the decrease in strength of hydrogen bonds (Bryant and McClements, 1998).”
Bryant, C. (2000) · Food Hydrocolloids · doi:10.1016/s0268-005x(00)00018-7 · Cited by 139
Self-citationHeat-Induced Soluble Protein Aggregates from Mixed Pea Globulins and β-Lactoglobulin
Chihi, M. L., Mession, J.-L., Sok, N., & Saurel, R. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.6b00087 · Cited by 140
Moschakis, T., Murray, B. S., & Βiliaderis, C. G. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.07.001 · Cited by 137
Functional food microstructures for macronutrient release and delivery
Norton, J. E., González-Espinosa, Y., Watson, R., Spyropoulos, F., & Norton, I. T. (2015) · Food & Function · doi:10.1039/c4fo00965g · Cited by 140
Vilela, J. A. P., Cavallieri, Â. L. F., & Cunha, R. L. (2011) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2011.03.012 · Cited by 131
Grasso, N., Roos, Y. H., Crowley, S. V., Arendt, E. K., & O’Mahony, J. A. (2021) · Future Foods · doi:10.1016/j.fufo.2021.100048 · Cited by 134
Alting, A. C., Weijers, M., de Hoog, E. H. A., van de Pijpekamp, A. M., Stuart, M. A. C., Hamer, R. J., de Kruif, C. G., & Visschers, R. W. (2004) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf034753r · Cited by 126
Yi, J., Fan, Y., Zhang, Y., Wen, Z., Zhao, L., & Lü, Y. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.05.036 · Cited by 125
Effect of processing on aggregation mechanism of egg white proteins
Gharbi, N., & Labbafi, M. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.01.088 · Cited by 124
Britten, M., & Giroux, H. J. (2001) · Food Hydrocolloids · doi:10.1016/s0268-005x(01)00049-2 · Cited by 124
Cortez-Trejo, M. C., Figueroa-Cárdenas, J. D., Quintanar-Guerrero, D., Baigts-Allende, D. K., Manríquez, J., & Mendoza, S. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107648 · Cited by 122
Nyemb, K., Guérin‐Dubiard, C., Pezennec, S., Jardin, J., Briard‐Bion, V., Cauty, C., Rutherfurd, S. M., Dupont, D., & Nau, F. (2015) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2015.10.011 · Cited by 126
Factors Affecting the Functional Properties of Whey Protein Products: A Review
EL‐SALAM, M. H. A., El‐Shibiny, S., & Salem, A. S. (2009) · Food Reviews International · doi:10.1080/87559120902956224 · Cited by 122
Ramos, Ó. L., Pereira, R. N., Martins, A. J., Rodrigues, R. M. M., Fuciños, C., Teixeira, J. A., Pastrana, L. M., Malcata, F. X., & Vicente, A. A. (2015) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2014.993749 · Cited by 128
“Consequently, high temperature (above protein denaturation level) is a common parameter selected for accelerating whey protein aggregation (Bryant and McClements, 1998).”
BackgroundInfluentialEffects of different oils on the properties of soy protein isolate emulsions and gels
Gu, X., Campbell, L. J., & Euston, S. R. (2009) · Food Research International · doi:10.1016/j.foodres.2009.04.015 · Cited by 121
Gelation properties of dispersions containing polymerized and native whey protein isolate
Vardhanabhuti, B., Foegeding, E. A., McGuffey, M. K., Daubert, C. R., & Swaisgood, H. E. (2001) · Food Hydrocolloids · doi:10.1016/s0268-005x(00)00062-x · Cited by 121
“It has been suggested that heating whey proteins under salt free conditions leads to the formation of molecules that aggregate in an ordered ‘string-of-beads’ or filament structure to form soluble linear aggregates ( Bryant & McClements, 1998; Kinekawa & Kitabatake, 1995; Kitabatake, Doi, & Kinekawa, 1994).”
BackgroundInfluentialXia, W., Zhu, L., Delahaije, R., Cheng, Z., Zhou, X.-L., & Sagis, L. (2021) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2021.107376 · Cited by 111
Ultrasonic effect on physicochemical and functional properties of α-lactalbumin
Jambrak, A. ., Mason, T. J., Lelas, V., & Krešić, G. (2009) · LWT · doi:10.1016/j.lwt.2009.09.001 · Cited by 118
Design of Bio-nanosystems for Oral Delivery of Functional Compounds
Cerqueira, M. Â., Pinheiro, A. C., Silva, H. D., Ramos, P. E., Azevedo, M. A., Flores-López, M. L., Rivera, M. C., Bourbon, A. I., Ramos, Ó. L., & Vicente, A. A. (2013) · Food Engineering Reviews · doi:10.1007/s12393-013-9074-3 · Cited by 116
“Besides it is relatively inexpensive (by-product from the cheese industry), classified as GRAS (generally regarded as safe), it presents a high nutritional value as well as an extraordinary binding capacity to various active compounds [12, 23, 54].”
BackgroundA New Multistep Ca2+-Induced Cold Gelation Process for β-Lactoglobulin
Veerman, C., Baptist, H. G. M., Sagis, L. M. C., & van der Linden, E. (2003) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf0261396 · Cited by 117
Baier, S. K., & McClements, D. J. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf001096j · Cited by 114
Self-citationShah, B. S., Davidson, P. M., & Zhong, Q. (2012) · Applied and Environmental Microbiology · doi:10.1128/aem.02225-12 · Cited by 113
“0, where unconjugated whey proteins would aggregate easily because of the close-to-zero net charge at this acidity near the isoelectric points of major whey proteins -lactoglobulin, -lactalbumin, and bovine serum albumin (6).”
BackgroundSoybean protein isolate gel particles as foaming and emulsifying agents
Matsumiya, K., & Murray, B. S. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.03.028 · Cited by 113
Binding of β-carotene to whey proteins: Multi-spectroscopic techniques and docking studies
Allahdad, Z., Varidi, M., Zadmard, R., Saboury, A. A., & Haertlé, T. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2018.10.057 · Cited by 113
Use of Whey Protein Soluble Aggregates for Thermal Stability—A Hypothesis Paper
Ryan, K. N., Zhong, Q., & Foegeding, E. A. (2013) · Journal of Food Science · doi:10.1111/1750-3841.12207 · Cited by 113
Improved Functional Characteristics of Whey Protein Hydrolysates in Food Industry
Jeewanthi, R. K. C., Lee, N., & Paik, H. (2015) · Korean Journal for Food Science of Animal Resources · doi:10.5851/kosfa.2015.35.3.350 · Cited by 111
“Cold-set gelation of WPs has also been noted by Bryant and McClements (1998).”
BackgroundCharacterization of casein hydrolysates derived from enzymatic hydrolysis
Wang, J., Su, Y., Jia, F., & Jin, H. (2013) · Chemistry Central Journal · doi:10.1186/1752-153x-7-62 · Cited by 111
“Casein has made us interest due to its numerous using in the food, drug, and cosmetic industries as well as to its importance as an investigation material for elucidating essential questions regarding the protein chemistry [1-4].”
BackgroundStructure and rheological properties of acid-induced egg white protein gels
Weijers, M., van de Velde, F., Stijnman, A. C., van de Pijpekamp, A. M., & Visschers, R. W. (2005) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2005.02.013 · Cited by 111
“This reduces the electrostatic repulsion between the aggregates and therefore promotes the formation of a percolation network (Alting et al., 2004; Bryant & McClements, 1998).”
BackgroundCold‐set whey protein gels induced by calcium or sodium salt addition
Kuhn, K. R., Cavallieri, Â. L. F., & Cunha, R. L. (2010) · International Journal of Food Science & Technology · doi:10.1111/j.1365-2621.2009.02145.x · Cited by 110
Geremias-Andrade, I. M., Souki, N. P. D. B. G., Moraes, I. C. F., & Pinho, S. C. (2017) · LWT · doi:10.1016/j.lwt.2017.07.063 · Cited by 112
Influence of Maillard reaction extent on acid induced gels of whey proteins and dextrans
Spotti, M. J., Loyeau, P. A., Marangón, A., Noir, H., Rubiolo, A. C., & Carrara, C. R. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.01.020 · Cited by 109
Chantrapornchai, W., & McClements, D. J. (2002) · Food Hydrocolloids · doi:10.1016/s0268-005x(01)00124-2 · Cited by 109
Self-citationMolecular mechanisms of Fe2+‐induced β‐lactoglobulin cold gelation
Remondetto, G. E., & Subirade, M. (2003) · Biopolymers · doi:10.1002/bip.10423 · Cited by 107
Ren, Z.-Y., Chen, Z.-Z., Zhang, Y.-Y., Lin, X.-R., & Li, B. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.05.015 · Cited by 100
Spotti, M. J., Tarhan, Ö., Schaffter, S., Corvalán, C. M., & Campanella, O. H. (2016) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.10.014 · Cited by 106
Enzymatic Hydrolysis of Heat-Induced Aggregates of Whey Protein Isolate
O’Loughlin, I. B., Murray, B. A., Kelly, P. M., Fitzgerald, R. J., & Brodkorb, A. (2012) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf205213n · Cited by 105
Rheological behaviour of whey protein concentrate and λ-carrageenan aqueous mixtures
Lizárraga, M. S., PIANTEVICIN, D., GONZALEZ, R., Rubiolo, A. C., & Santiago, L. G. (2005) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2005.07.007 · Cited by 105
Encapsulation of α-tocopherol in protein-based delivery particles
Somchue, W., Sermsri, W., Shiowatana, J., & Siripinyanond, A. (2009) · Food Research International · doi:10.1016/j.foodres.2009.04.021 · Cited by 105
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
