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
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“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
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Items 401–500 of 643
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Tian, M., Cheng, J., Wang, H., Xie, Q., Wei, Q., & Guo, M. (2022) · Journal of Dairy Science · doi:10.3168/jds.2021-21581 · Cited by 18
Clímaco, G. N., Gonçalves, R. F. S., Fernandes, J., Pinheiro, A. C., Vicente, A. A., & Fasolin, L. H. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110460 · Cited by 18
Fu, Y., Wang, J., Liu, X., Ni, Y., Niu, Z., Qiu, L., Liu, Z., & Wei, C. (2024) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2024.110728 · Cited by 18
Strength of microbeads for the encapsulation of heat sensitive, hydrophobic components
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“For WPI this is around pH 5.1 (Bryant & McClements, 1998), for alginate 71 this is below 3.5 (Draget, Skjåk Bræk, & Smidsrød, 1994).”
BackgroundInfluentialTseng, Y., Xiong, Y. L., & Yang, F. (2009) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.3770 · Cited by 18
Ali, F., O’Mahony, J. A., O’Sullivan, M. G., & Kerry, J. P. (2025) · Foods · doi:10.3390/foods14152701 · Cited by 17
“After the peak, tan δ decreased slightly due to hydrophobic protein interactions [69].”
Improving vitamin D3 stability to environmental and processing stresses using mixed micelles
Mulrooney, S. L., O’Neill, G. J., Brougham, D. F., Lyng, J. G., & O’Riordan, D. (2021) · Food Chemistry · doi:10.1016/j.foodchem.2021.130114 · Cited by 17
Braitmaier, S. H., Wahl, A.-L., Hinrichs, J., & Atamer, Z. (2024) · International Dairy Journal · doi:10.1016/j.idairyj.2024.106056 · Cited by 17
Heat-induced interactions between microfluidized hemp protein particles and caseins or whey proteins
Ma, S., Ye, A., Singh, H., & Acevedo-Fani, A. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.141290 · Cited by 18
Hu, Q., Qiu, L., Zhu, Y., Huang, Y., Liu, L., Han, T., Song, Y., & Zhu, X. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.143329 · Cited by 17
Egan, T., Jacquier, J., Rosenberg, Y., & Rosenberg, M. (2013) · Journal of Microencapsulation · doi:10.3109/02652048.2013.824513 · Cited by 17
Liu, G., & Zhong, Q. (2014) · Journal of Dairy Science · doi:10.3168/jds.2014-8439 · Cited by 17
Chikhoune, A., Gagaoua, M., Nanema, K. D., Souleymane, A. S., Hafid, K., Aliane, K., Hadjal, S., Madani, K., Sentandreu, E., Sentandreu, M. Á., et al. (2017) · Arabian Journal for Science and Engineering · doi:10.1007/s13369-017-2428-z · Cited by 17
Interaction of ciprofloxacin with the activated sludge of the sewage treatment plant
Wang, K., Gao, D., Xu, J., Cai, L., Cheng, J., Yu, Z., Hu, Z., & Yu, J. (2018) · Environmental Science and Pollution Research · doi:10.1007/s11356-018-3413-0 · Cited by 17
“Furthermore, CIP+ (17% of the total CIP) containing –NH2 + and –COOH is prone to interact with the negatively charged residues of the protein, with a strong electrostatic interaction as the main driving force (Bryant and McClements 1998; Rybacka and Andersson 2016).”
BackgroundErtaş, N., Sert, D., DEMİR, M. K., & Elgün, A. (2009) · Food Science and Technology Research · doi:10.3136/fstr.15.51 · Cited by 17
Resch, J. J., Daubert, C. R., & Foegeding, E. A. (2004) · International Journal of Food Science & Technology · doi:10.1111/j.1365-2621.2004.00882.x · Cited by 17
Laiho, S., Ercili-Cura, D., Forssell, P., Myllärinen, P., & Partanen, R. (2015) · International Dairy Journal · doi:10.1016/j.idairyj.2015.05.002 · Cited by 17
Observation of salt-induced β-lactoglobulin aggregation using sedimentation field-flow fractionation
Saeseaw, S., Shiowatana, J., & Siripinyanond, A. (2006) · Analytical and Bioanalytical Chemistry · doi:10.1007/s00216-006-0783-9 · Cited by 17
Whey Protein Structure and Denaturation and Interactions with Other Food Components
Wang, C., & Guo, M. (2019) · doi:10.1002/9781119256052.ch4 · Cited by 17
Shu, M., Fan, L., Zhang, J., & Li, J. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2161994 · Cited by 16
“The good rheological properties of WPI are mainly determined by hydrogen bonding, electrostatic interaction, van der Waals force and hydrophobic interaction (Bryant and McClements 1998).”
BackgroundPeptide bonds cleaved by pepsin are affected by the morphology of heat-induced ovalbumin aggregates
Suwareh, O., Causeur, D., Feunteun, S. L., Jardin, J., Briard‐Bion, V., Pezennec, S., & Nau, F. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.140260 · Cited by 16
Study on the thermal behavior of casein in air
Moldoveanu, C. C., Odochian, L., Păiuş, C., Iancu, L., & Băiceanu, A. (2013) · Acta Chemica Iasi · doi:10.2478/achi-2013-0004 · Cited by 16
Influence of Sodium Chloride and Glucose on Acid‐Induced Gelation of Heat‐Denatured Ovalbumin
Choi, S. J., Lee, S. E., & Moon, T. W. (2008) · Journal of Food Science · doi:10.1111/j.1750-3841.2008.00770.x · Cited by 16
β‐Lactoglobulin Gelation and Modification: Effect of Selected Acidulants and Heating Conditions
Resch, J. J., Daubert, C. R., & Foegeding, E. A. (2005) · Journal of Food Science · doi:10.1111/j.1365-2621.2005.tb09025.x · Cited by 16
Farrag, A. F. (2007) · International Journal of Dairy Science · doi:10.3923/ijds.2008.20.28 · Cited by 16
“Whey proteins are applied as food ingredients in formulating products due to their nutritional & health benefits (Bryant and McClements 1998; Harper, 2000; Hudson, et al., 2000).”
BackgroundRako, A., Kalit, M. T., Kalit, S., Soldo, B., & Ljubenkov, I. (2018) · LWT · doi:10.1016/j.lwt.2018.06.024 · Cited by 16
Coupling between polysaccharide gelation and micro-phase separation of globular protein clusters
Baussay, K., Durand, D., & Nicolaï, T. (2006) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2006.09.059 · Cited by 16
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Koutina, G., Ioannidi, E., Nogueira, B. M., & Ipsen, R. (2017) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12458 · Cited by 15
Wu, J., Chen, H., Zhou, L., Liu, W., Zhong, J., & Liu, C. (2021) · European Food Research and Technology · doi:10.1007/s00217-021-03741-x · Cited by 15
Protein micro/nanoparticles for controlled nutraceutical delivery in functional foods
Chen, L. (2009) · Elsevier eBooks · doi:10.1533/9781845696603.3.572 · Cited by 15
Meza, B. E., Verdini, R. A., & Rubiolo, A. C. (2011) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2011.11.002 · Cited by 15
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Pedersen, J. B., Fojan, P., Sørensen, J., & Petersen, S. B. (2006) · Journal of Fluorescence · doi:10.1007/s10895-006-0088-6 · Cited by 15
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BackgroundChung, C., Degner, B., & McClements, D. J. (2013) · Food Research International · doi:10.1016/j.foodres.2013.08.018 · Cited by 14
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Okur, S., Ceylan, Ç., & Çulcular, E. (2011) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2011.09.078 · Cited by 14
George, P., Lundin, L., & Kasapis, S. (2013) · Food Chemistry · doi:10.1016/j.foodchem.2013.01.032 · Cited by 14
Bağcı, P. O., & Gunasekaran, S. (2016) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12317 · Cited by 14
Kharlamova, A., Nicolaï, T., & Chassenieux, C. (2018) · International Dairy Journal · doi:10.1016/j.idairyj.2018.07.002 · Cited by 14
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Nanometric‐Size Delivery Systems for Bioactive Compounds for the Nutraceutical and Food Industries
Donsı̀, F., Sessa, M., & Ferrari, G. (2013) · doi:10.1002/9781118451915.ch37 · Cited by 14
Whey Protein Functional Properties and Applications in Food Formulation
Wang, C., Killpatrick, A., Humphrey, A., & Guo, M. (2019) · Wiley eBooks · doi:10.1002/9781119256052.ch7 · Cited by 14
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Zhang, Z., Arrighi, V., Campbell, L., Lonchamp, J., & Euston, S. R. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108811 · Cited by 13
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Ibáñez, R. A., Waldron, D. S., & McSweeney, P. L. H. (2015) · International Dairy Journal · doi:10.1016/j.idairyj.2015.10.004 · Cited by 13
Suárez, A., Fernández, L., Balbarie, P., Iglesias, J. R., & Riera, F. A. (2016) · European Food Research and Technology · doi:10.1007/s00217-015-2625-5 · Cited by 13
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BackgroundLiu, D.-S., Zhou, P., & Nicolai, T. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.105590 · Cited by 12
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Al‐Jassar, S., Mikajiri, S., & Roos, Y. H. (2020) · LWT · doi:10.1016/j.lwt.2020.110099 · Cited by 13
Effect of GdL Addition on Physico-chemical Properties of Fermented Sausages during Ripening
Yim, D.-G., Jang, K.-H., & Chung, K.-Y. (2015) · Korean Journal for Food Science of Animal Resources · doi:10.5851/kosfa.2015.35.3.322 · Cited by 13
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BackgroundJanjarasskul, T., Tananuwong, K., Leuangsukrerk, M., Phupoksakul, T., & Borompichaichartkul, C. (2017) · Food Biophysics · doi:10.1007/s11483-017-9510-7 · Cited by 13
Zheng, N.-Y., Chen, Y., Chen, Y., Shiu, J.-S., & Wang, S. (2021) · Poultry Science · doi:10.1016/j.psj.2021.101373 · Cited by 12
“Then, these protein chains gradually form into aggregates and ultimately result in a stable egg white gel (Bryant and McClements, 1998; Zhao et al., 2016a).”
BackgroundZhang, L., Zhang, Z., Euston, S., Li, B., Li, E.-H., Fu, C., & Chen, G.-Y. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.109003 · Cited by 12
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de Amarante, M. C. A., Ong, L., Spyropoulos, F., Gras, S. L., & Wolf, B. (2024) · Food Chemistry · doi:10.1016/j.foodchem.2024.140399 · Cited by 12
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Vahedifar, A., Madadlou, A., & Salami, M. (2017) · International Dairy Journal · doi:10.1016/j.idairyj.2017.06.003 · Cited by 12
Kim, J., Watkinson, P. J., Lad, M., Matia‐Merino, L., Smith, J. R., & Golding, M. (2022) · Food Biophysics · doi:10.1007/s11483-022-09719-w · Cited by 12
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“3) and a granular aspect with presence of dense aggregates that scatter the light [33, 34].”
BackgroundNourbakhsh, H., Madadlou, A., Emam‐Djomeh, Z., Wang, Y., Gunasekaran, S., & Mousavi, M. (2016) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5b04867 · Cited by 12
Ribeiro, A., Gomes, A. C., & Cavaco-Paulo, A. M. (2012) · Journal of Biomedical Materials Research Part B Applied Biomaterials · doi:10.1002/jbm.b.32797 · Cited by 12
“Different molecular interactions lead to gel formation and structure stabilization including hydrophobic interactions, hydrogen bonding, electrostatic interactions, and covalent bonds.(10,14)”
BackgroundMethodBSA/HSA ratio modulates the properties of Ca2+-induced cold gelation scaffolds
Ribeiro, A., Volkov, V., Oliveira, M. B., Padrão, J., Mano, J. F., Gomes, A. C., & Cavaco-Paulo, A. M. (2016) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2016.05.012 · Cited by 12
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BackgroundFood Protein Nanoparticles: Formation, Properties and Applications
Loveday, S. M., Rao, M. A., & Singh, H. (2012) · doi:10.1002/9781118373903.ch10 · Cited by 12
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Hui, D., Liang, W., Wang, R., Feng, X., & Tang, X. (2025) · Sustainable Food Proteins · doi:10.1002/sfp2.70037 · Cited by 12
Kim, J., Watkinson, P. J., Matia‐Merino, L., Smith, J. R., & Golding, M. (2022) · International Journal of Food Science & Technology · doi:10.1111/ijfs.15950 · Cited by 11
Wang, W., & Zhong, Q. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2014.04.025 · Cited by 11
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BackgroundSetiowati, A. D., Vermeir, L., Neve, L. D., Doost, A. S., Sinnaeve, D., & der Meeren, P. V. (2018) · Magnetic Resonance in Chemistry · doi:10.1002/mrc.4812 · Cited by 11
Meza, B. E., Vicin, D. A. D. P., Marino, F., Sihufe, G. A., Peralta, J. M., & Zorrilla, S. E. (2019) · International Journal of Dairy Technology · doi:10.1111/1471-0307.12669 · Cited by 11
Calcium-induced skim milk gels: Impact of holding temperature and ionic strength
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Tan, M. C., Chin, N. L., Yusof, Y. A., Taip, F. S., & Abdullah, J. B. (2014) · Agriculture and Agricultural Science Procedia · doi:10.1016/j.aaspro.2014.11.021 · Cited by 11
Abhyankar, A. R., Mulvihill, D. M., Fenelon, M. A., & Auty, M. A. E. (2009) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2009.07.004 · Cited by 11
Gellan gum/cassava starch mixtures in water systems and in milk systems
Coronato, R., Biasutti, E. A. R., de Carvalho, C. W. P., & Grossmann, M. V. E. (2012) · Starch - Stärke · doi:10.1002/star.201100102 · Cited by 11
Li, H., Ma, B., Zhou, S.-M., Zhang, L., & Yi, J. (2010) · Colloid & Polymer Science · doi:10.1007/s00396-010-2278-7 · Cited by 11
Developments in Science, Technology, Quality and Constraints of Restructured Meat Products-A Review
Reddy, G. V. B., Mandal, P. K., Sen, A. R., & Reddy, K. S. (2014) · International Journal of Meat Science · doi:10.3923/ijmeat.2015.14.48 · Cited by 12
Nanostructures of whey proteins for encapsulation of food ingredients
Ramos, Ó. L., Pereira, R. N., Simões, L. S., Madalena, D. A., Rodrigues, R. M. M., Teixeira, J. A., & Vicente, A. A. (2019) · Elsevier eBooks · doi:10.1016/b978-0-12-815663-6.00003-3 · Cited by 11
Cheese | Cheese as a Food Ingredient
Guinee, T. P. (2011) · Encyclopedia of Dairy Sciences · doi:10.1016/b978-0-12-374407-4.00097-2 · Cited by 11
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Cooke, D. R., & McSweeney, P. L. H. (2017) · Wiley eBooks · doi:10.1002/9781119046165.ch0b · Cited by 11
Zhang, F., Ma, Z., Han, J., Yang, X., & Lin, D. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112673 · Cited by 10
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“These interactions lead to protein aggregation and the formation of a stable egg white gel (Bryant and McClements, 1998; Zhao et al., 2016a,b).”
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Zhong, Q., & Shah, B. S. (2012) · Elsevier eBooks · doi:10.1533/9780857095657.2.177 · Cited by 10
Iqbal, S., Ayyub, A., Iqbal, H., & Chen, X. D. (2020) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.10645 · Cited by 10
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Jiang, C., Fu, W., Ma, Z., Wang, J., Zhang, M., & Wang, C. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111716 · Cited by 9
de Jesus, G. I., Baldasso, C., Marcílio, N. R., & Tessaro, I. C. (2020) · Journal of Applied Polymer Science · doi:10.1002/app.49282 · Cited by 9
Alhazmi, H. A., Ahsan, W., Ibrahim, A. M. M., Khubrani, R. A. Y., Haddadi, Z. A. A., Safhi, A. Y. F., Shubayr, N., Bratty, M. A., & Najmi, A. (2021) · Open Chemistry · doi:10.1515/chem-2021-0089 · Cited by 9
“Importantly, the protein aggregation process is supposed to be lesser in case of monovalent ions than the divalent metal ions as they can form bridges and provide electrostatic attractions between the negatively charged species of surrounding protein molecules [36,37].”
BackgroundTailoring the rheological properties of high protein suspension by thermal-mechanical treatment
Siddiqui, U., Ilavský, J., & Chen, D. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108863 · Cited by 9
Giefer, P., Bäther, S., Kaufmes, N., Kieserling, H., Heyse, A., Wagemans, W., Barthel, L., Meyer, V., Schneck, E., Fritsching, U., et al. (2023) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2023.08.103 · Cited by 9
Property and storage stability of whey protein‐sucrose based safe paper glue
Wang, G., & Guo, M. (2013) · Journal of Applied Polymer Science · doi:10.1002/app.39710 · Cited by 9
Pal, S., Maity, S., Sardar, S., Parvej, H., Das, N. C., Chakraborty, J., & Halder, U. C. (2016) · RSC Advances · doi:10.1039/c6ra24570f · Cited by 9
Luna-Valdez, J. G., Balandrán‐Quintana, R. R., Azamar-Barrios, J. A., Montfort, G. R.-C., Wilson, A. M. M., Madera-Santana, T. J., Rascón‐Chu, A., & Chaquilla-Quilca, G. (2019) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2019.03.003 · Cited by 9
Ultrasound Viscosity Measurements Allow Determination of Gas Volume Fraction in Foamed Gels
Tomczyńska‐Mleko, M., & Ozimek, L. (2013) · Journal of Food Process Engineering · doi:10.1111/jfpe.12019 · Cited by 9
Marinea, M., Ellis, A., Golding, M., & Loveday, S. M. (2022) · Food Biophysics · doi:10.1007/s11483-022-09763-6 · Cited by 8
Dou, X., & Ren, J. (2024) · International Journal of Food Science & Technology · doi:10.1111/ijfs.17195 · Cited by 8
Liu, Y., Zhang, L., & Chi, Y. (2024) · Poultry Science · doi:10.1016/j.psj.2024.104279 · Cited by 8
“More Ca 2+ will bond to the exposed carboxyl group as a result of the addition of CaCl 2 to the salting solution, which helps maintain the integrity of the egg yolk granule structure (Bryant and Mcclements, 1998; Yang et al., 2019).”
BackgroundParticle size effects in colloidal gelatin particle suspensions
van Riemsdijk, L. E., Snoeren, J. P. M., van der Goot, A. J., Boom, R. M., & Hamer, R. J. (2010) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2010.07.025 · Cited by 8
Chun, J., Choi, M., Min, S., & Hong, G.-P. (2014) · Meat Science · doi:10.1016/j.meatsci.2014.05.032 · Cited by 8
Pirdashti, M., Mohammadi, M., Rahimpour, F., & Kennedy, D. T. (2008) · International Journal of Applied Decision Sciences · doi:10.1504/ijads.2008.020326 · Cited by 8
“On a dry basis, commercial WPCs may have protein concentration between 35% and 80% (Ha and Zemel, 2003; Lucena et al., 2006; Bryant and McClements, 1998; Lizarragaa et al., 2006).”
BackgroundNonthermal gelation of whey proteins induced by organic acids
Queirós, A. S., & Lopes‐da‐Silva, J. A. (2017) · Journal of Applied Polymer Science · doi:10.1002/app.45134 · Cited by 8
Wang, T., Wang, R., Chen, Z., & Zhong, Q. (2017) · RSC Advances · doi:10.1039/c7ra08167g · Cited by 8
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
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