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 501–600 of 643
A Lactoglobulin-Composite Self-Healing Coating for Mg Alloys
Feng, J., Pan, Y., Yang, M., Fernández, C., Chen, X., & Peng, Q. (2021) · ACS Applied Bio Materials · doi:10.1021/acsabm.1c00560 · Cited by 8
Effects of pH and chitosan on beef emulsion properties
Kurt, Ş. (2009) · International Journal of Food Science & Technology · doi:10.1111/j.1365-2621.2009.02113.x · Cited by 8
Blazek, V. (2008) · The Sydney eScholarship Repository (The University of Sydney) · Cited by 8
Transglutaminase mediated crosslinking of pea protein: from rheology to proteomics
Mukherjee, A., Pee, J. V., Duijsens, D., Grauwet, T., Voorde, I. V. D., Fraeye, I., & Weiland, F. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.112233 · Cited by 7
Charoensuk, D., Brannan, R. G., Chaiyasit, W., & Chanasattru, W. (2021) · International Journal of Food Properties · doi:10.1080/10942912.2021.1960371 · Cited by 7
Nelly Cruz Cansino Guadalupe, P. (2008) · TDX (Tesis Doctorals en Xarxa) · Cited by 7
The effect of protein aggregate morphology on phase separation in mixtures with polysaccharides
Nguyen, B. T., Nicolaï, T., Chassenieux, C., & Benyahia, L. (2014) · Journal of Physics Condensed Matter · doi:10.1088/0953-8984/26/46/464102 · Cited by 7
“…are widely used in the food industry and their aggregation and gelling properties have been investigated extensively in the past both individually (Bryant and McClements 1998, Clark 1999, De la Fuente et al 2002, Gosal and Ross-Murphy 2000, Morris 2007, Piculell 2006, Totosaus et al 2002) and in…”
BackgroundGelling Properties of Heat-Denatured β-Lactoglobulin Aggregates in a High-Salt Buffer
Vittayanont, M., Steffe, J. F., Flegler, S. L., & Smith, D. M. (2002) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf011410p · Cited by 7
Trivedi, M. K., & Nayak, G. (2015) · Clinical Pharmacology & Biopharmaceutics · doi:10.4172/2167-065x.1000138 · Cited by 7
“The interesting structure and physicochemical properties allows it to be used in DDS [11].”
InfluentialRole of Whey Proteins in Food Packaging
Janjarasskul, T., & Tananuwong, K. (2019) · Elsevier eBooks · doi:10.1016/b978-0-08-100596-5.22399-8 · Cited by 7
Transcutaneous male sterilization.
Goldsmith, A., Edelman, D. A., & Zatuchni, G. I. (1985) · PubMed · Cited by 7
Mestawet, A. T., France, T. C., Mulcahy, P. G. J., & O’Mahony, J. A. (2024) · International Dairy Journal · doi:10.1016/j.idairyj.2024.106006 · Cited by 6
Brito‐Oliveira, T. C., Cavini, A. C. M., Ferreira, L. S., Moraes, I. C. F., & Pinho, S. C. (2024) · Gels · doi:10.3390/gels10070467 · Cited by 6
Tacer-Caba, Z., & Özkök, G. K. (2019) · Harran Tarım ve Gıda Bilimleri Dergisi · doi:10.29050/harranziraat.408889 · Cited by 6
Chen, H. (2014) · Cited by 6
Anuradha, S. N., & Prakash, V. (2009) · International Journal of Food Sciences and Nutrition · doi:10.1080/09637480701877736 · Cited by 6
Kuhn, K. R., Picone, C. S. F., & Cunha, R. L. (2012) · Contemporary food engineering · doi:10.1201/b12048-5 · Cited by 6
Tomczyńska‐Mleko, M., Gustaw, W., Piersiak, T., Terpiłowski, K., Sołowiej, B. G., Wesołowska–Trojanowska, M., & Mleko, S. (2014) · Acta Alimentaria · doi:10.1556/aalim.43.2014.3.14 · Cited by 6
Choi, S. J., & Moon, T. W. (2008) · Journal of Food Science · doi:10.1111/j.1750-3841.2007.00615.x · Cited by 6
Hosseinpour, S., Izadi, Aminlari, Ramezani, & Tavana (2011) · ISABB Journal of Food and Agricultural Sciences · doi:10.5897/isabb-jfas.9000002 · Cited by 6
“Whey proteins are used as functional ingredients in a wide variety of food products because of their ability to modify the texture and stability of emulsions, foams and gels ((Bryant and McClements, 1998, 1999; Cavallieri et al., 2007; Solar and Gunasekaran, 2010; Herceg et al., 2007).”
BackgroundResultKrešić, G., Jambrak, A. ., Lelas, V., & Herceg, Z. (2011) · University of Zagreb University Computing Centre (SRCE) · Cited by 6
Wang, Q., Xue, Z., Tang, J., Chen, M., Wu, D. C., Qin, W., & Zhang, Q. (2026) · Advances in Colloid and Interface Science · doi:10.1016/j.cis.2026.103906 · Cited by 5
Bamboo shoot powder: Characterization and application in culinary processed cheese “Requeijão”
de Oliveira, J. E. G., Scopel, B. C., Bettanin, L., Schuster, M. B., Schmiele, M. M., Fernandes, I. A., Cavalheiro, D., Rigo, E., & Sehn, G. A. R. (2024) · International Journal of Gastronomy and Food Science · doi:10.1016/j.ijgfs.2024.101071 · Cited by 5
Cheese: Cheese as a Food Ingredient ☆
Guinee, T. P. (2016) · Elsevier eBooks · doi:10.1016/b978-0-08-100596-5.00661-2 · Cited by 5
Physicochemical and rheological properties of skim milk with different added zinc salts
Zhao, S., Oh, H. E., & Wong, M. (2023) · International Dairy Journal · doi:10.1016/j.idairyj.2023.105584 · Cited by 5
Proteins in food microstructure formation
de Jongh, H. H. J. (2007) · Elsevier eBooks · doi:10.1533/9781845693671.1.40 · Cited by 5
Tavares, T. G., Ramos, Ó. L., & Malcata, F. X. (2017) · Journal of Food Science and Technology · doi:10.1007/s13197-017-2912-1 · Cited by 5
Elviri, L., & Mattarozzi, M. (2012) · Elsevier eBooks · doi:10.1016/b978-0-12-384862-8.00016-9 · Cited by 5
Effect of Addition of Tryptophan on Aggregation of Apo-α-Lactalbumin Induced by UV-Light
Zhao, Z., Li, R., Poojary, M. M., Nielsen, S. B., & Lund, M. N. (2021) · Foods · doi:10.3390/foods10071577 · Cited by 5
Kannan, A., HETTIARACHCHY, N. S., Sato, K., & Marshall, M. R. (2012) · CRC Press eBooks · doi:10.1201/b11768-4 · Cited by 5
Saalfeld, D., Riegel, I., Kulozik, U., & Gebhardt, R. (2015) · Foods · doi:10.3390/foods4020229 · Cited by 5
“Gels formed by filaments have smaller and more homogeneous pore sizes, which cause a better water binding capacity [21].”
BackgroundUltrasound assisted ethanolic gelation of lentil protein to encapsulate β-carotene
Mekala, S., Liu, Z., Vieira, É. N. R., Chen, L., & Saldaña, M. D. A. (2024) · LWT · doi:10.1016/j.lwt.2024.117053 · Cited by 5
Intensification and enhancement of phenolic compounds extraction using cooperative formulation
Suliman, S. S., Othman, N., Zaini, M. A. A., Noah, N. F. M., & Kahar, I. N. S. (2025) · Chemical Engineering and Processing - Process Intensification · doi:10.1016/j.cep.2025.110220 · Cited by 4
Effect of macrocyclic compounds to protein aggregation
Lebedevа, N. S., Yurina, E. S., Gubarev, Y. A., & Койфман, О. И. (2019) · Journal of Inclusion Phenomena and Macrocyclic Chemistry · doi:10.1007/s10847-019-00947-1 · Cited by 4
Zeiler, R. N. W., & Bolhuis, P. G. (2012) · Faraday Discussions · doi:10.1039/c2fd20030a · Cited by 4
Chemical and Enzymatic Protein Modifications and Functionality Enhancement
Kumagaı, H. (2012) · CRC Press eBooks · doi:10.1201/b11768-8 · Cited by 5
van Leusden, P., den Hartog, G. J. M., Bast, A., Postema, M., van der Linden, E., & Sagis, L. M. C. (2016) · Food & Function · doi:10.1039/c6fo00405a · Cited by 4
Food Structures and Delivery of Nutrients
Sharma, R. (2012) · doi:10.1002/9781118373903.ch8 · Cited by 4
Water-binding of protein particles
Peters, J. P. C. M. (2016) · doi:10.18174/385963 · Cited by 4
Raghunath, S., Mallikarjunan, K., & Schoenfuss, T. C. (2025) · Journal of Food Process Engineering · doi:10.1111/jfpe.70183 · Cited by 3
Yan, T., Wang, M., Wang, D., Song, B., Liu, M., & Zhou, L. (2026) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.5c17162 · Cited by 3
So, H., Jun, S., Ibañez, D., Wang, Y., Du, Z.-Y., & Yang, Z. (2026) · International Dairy Journal · doi:10.1016/j.idairyj.2026.106613 · Cited by 3
Guan, Y. (2021) · Springer eBooks · doi:10.1007/978-981-16-0320-4_6 · Cited by 3
de Amarante, M. C. A., Ong, L., Spyropoulos, F., Gras, S. L., & Wolf, B. (2025) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2025.111043 · Cited by 3
Hydrogels formed with shellac and zein: pH-responsiveness, rheology, and gelation mechanism.
Aleman, J., & Zhong, Q. (2025) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2025.142729 · Cited by 3
Moutkane, M., Mudau, C., Balakrishnan, G., Chassenieux, C., & Nicolai, T. (2025) · Journal of Colloid and Interface Science · doi:10.1016/j.jcis.2025.138109 · Cited by 2
Thermomechanical effects of co-solute on the structure formation of bovine serum albumin
George, P., Lundin, L., & Kasapis, S. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.02.041 · Cited by 3
Stegen, J., Ioannou, J., Tromp, H., Donald, A. M., & van der Schoot, P. (2015) · Journal of Physics D Applied Physics · doi:10.1088/0022-3727/48/38/384001 · Cited by 3
Effect of Hydration Condition of Non-Muscle Protein on Gelling
Cho, M. S., Lee, N.-G., & Cho, Y. J. (2002) · Korean Journal of Fisheries and Aquatic Sciences · doi:10.5657/kfas.2002.35.6.627 · Cited by 3
High-Performance Structures of Biopolymer Gels Activated with Scleroprotein Crosslinkers
Prochoń, M., Dzeikala, O., & Szczepanik, S. (2025) · Molecules · doi:10.3390/molecules30030627 · Cited by 3
Hong, G.-P., Chun, J.-Y., Lee, S.-K., & Choi, M. (2012) · Korean Journal for Food Science of Animal Resources · doi:10.5851/kosfa.2012.32.3.301 · Cited by 3
Liu, W., & Delaplace, G. (2024) · doi:10.1002/9781394312405.ch6 · Cited by 3
Chutani, D., Rani, P., Huppertz, T., & Murphy, E. G. (2026) · International Dairy Journal · doi:10.1016/j.idairyj.2026.106662 · Cited by 2
Silk-Fibroin-Based Adhesive Hydrogels: Mechanistic Insights and Biomedical Applications─A Review
Jitpibull, J., Soomherun, N., & Ratanavaraporn, J. (2026) · ACS Omega · doi:10.1021/acsomega.6c02513 · Cited by 2
Lee, S.-H., & Lee, W.-J. (2021) · Food and Life · doi:10.5851/fl.2021.e8 · Cited by 2
Corrigan, B. M., O’Mahony, J. A., & Fenelon, M. A. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22088 · Cited by 2
“…to aggregate in the presence of Ca at room temperature even without heating (i.e., cold gelation) via noncovalent interactions such as Van der Waals and hydrophobic interactions, as well as electrostatic interactions (Barbut and Foegeding, 1993; Bryant and McClements, 1998; Veerman et al., 2003).”
BackgroundPolymerized whey protein-SDS interactions at their high concentrations
Eissa, A. S., Jani, P. K., & Khan, S. A. (2024) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2024.136607 · Cited by 2
Li, Y., Zhou, S., Qiang, J., Cao, Y., Qu, G., Gao, Y., Li, Q., & Yu, X. (2025) · Food Research International · doi:10.1016/j.foodres.2025.116366 · Cited by 2
Studies on shelf-life ofPaneerwhey based jelly confection
Wasnik, P. K., & Changade, S. P. (2015) · Asian Journal of Dairy and Food Research · doi:10.5958/0976-0563.2015.00037.8 · Cited by 2
Shimo, S. P., XiaoYun, W., Xuezhi, D., & Yan, P. (2016) · Asian Journal of Dairy and Food Research · doi:10.18805/ajdfr.v3i1.3570 · Cited by 2
“Hence, heat treatment might limit the application of whey proteins in some food products, particularly those with pH closer to the isoelectric point (pI) (Bryant and McClements, 1998).”
BackgroundAntioxidant and Biological Activities of Proteinaceous Extract from Algerian Glycine max Plant
Soussi, N., Moulay, S., Bacharı, K., & Benmiri, Y. (2017) · Pakistan Journal of Biological Sciences · doi:10.3923/pjbs.2017.124.131 · Cited by 2
The Role of Proteins in the Development of Food Structure
Gagnaire, V., Lechevalier-Datin, V., Famelart, M., Croguennec, T., & Bouhallab, S. (2019) · Royal Society of Chemistry eBooks · doi:10.1039/9781788016155-00029 · Cited by 2
Wennman, M., Svagan, A. J., Hellberg, M., & Hedenqvist, M. S. (2023) · Industrial Crops and Products · doi:10.1016/j.indcrop.2023.117244 · Cited by 2
Effect of thermal processing on the digestion of egg proteins
Lechevalier-Datin, V. (2023) · Elsevier eBooks · doi:10.1016/b978-0-323-95052-7.00014-5 · Cited by 2
Hydrothermal extraction and characterization of hemicellulose from biomass as a natural emulsifier
Li, Y., Jiang, S. Y., Xu, Z., Xu, Y., Yoon, S., Liu, X., Cheng, Y., O’Keefe, S. F., Ogejo, J. A., Lin, F., et al. (2025) · Food Chemistry · doi:10.1016/j.foodchem.2025.147107 · Cited by 1
Wang, F., Karoui, R., & Blecker, C. S. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.148910 · Cited by 1
Cold-set gelation of whey proteins: Principles, mechanisms, and food applications.
Cortez-Trejo, M. C., Román-Doval, R., Abadía-García, L., Cruz‐Aldaco, K., & Amaya-Llano, S. (2026) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2026.112695 · Cited by 1
Dai, N., Xia, J.-H., Dai, Z., Chen, J., Li, C.-H., Geng, Q., Deng, L.-Z., Li, T., & Dai, T.-T. (2026) · Journal of Future Foods · doi:10.1016/j.jfutfo.2026.04.003 · Cited by 1
Gelation behavior and formation mechanism of ovalbumin gel induced by heat–alkali synergy
Zheng, H., Yang, S., Yao, Y., Wu, N., Zhao, Y., & Tu, Y. (2026) · Food Chemistry · doi:10.1016/j.foodchem.2026.149528 · Cited by 1
Advance sensing of high energy explosive: A DFT-Based study of C5N framework performance
Tiwari, R., Gautam, M., Sharma, S., Srinivas, D., Yadav, S., Rita, Nandal, N., & Rehman, H. U. (2026) · Journal of Molecular Graphics and Modelling · doi:10.1016/j.jmgm.2026.109438 · Cited by 1
Duong, T. N. D. (2013) · RMIT Research Repository (RMIT University Library) · doi:10.25439/rmt.27586803 · Cited by 1
Hong, G.-P., & Chin, K. B. (2010) · Korean Journal for Food Science of Animal Resources · doi:10.5851/kosfa.2010.30.5.746 · Cited by 1
“Both salt and the CA system influenced the gel strength of cold-set MPs (p 0.001).”
BackgroundInfluentialda Silva, M. V., & Delgado, J. M. P. Q. (2011) · Defect and diffusion forum/Diffusion and defect data, solid state data. Part A, Defect and diffusion forum · doi:10.4028/www.scientific.net/ddf.312-315.1143 · Cited by 1
Influence of Environmental Conditions on Whey Protein Gels Properties and Gels Microstructure
Xu-hai, C., & Kong, B. (2008) · Zhongguo nongye Kexue · Cited by 1
Electrostatic interaction of lecithin-whey protein concentrate in aqueous solution.
Kongsawat, P., & Klinkesorn, U. (2011) · Cited by 1
Development of Food-Grade Nano-Delivery Systems and Their Application to Dairy Foods: A Review
Ha, H., & Lee, W.-J. (2018) · Journal of Dairy Science and Biotechnology · doi:10.22424/jmsb.2018.36.4.187 · Cited by 1
“며, 또한 사전 열처리 공정을 통한 젤화와 산화안정성 향상과 관련된 보호능(shielding capability) 제공과 같은 다양한 기능적 특성을 지니고 있어 나노전달체 원료로써 이용되고 있다 (Bryant and McClements, 1998; Livney, 2010; Elzoghby et al., 2011).”
Farrag, A.-R. H. (2007) · Journal of Food and Dairy Sciences · doi:10.21608/jfds.2007.204665 · Cited by 1
Mah, E. (2008) · OhioLink ETD Center (Ohio Library and Information Network) · Cited by 1
Using Temperature Sweeps To Investigate Rheology of Bioplastics
Tunick, M. H., Onwulata, C. I., & Cooke, P. H. (2013) · ACS symposium series · doi:10.1021/bk-2013-1138.ch007 · Cited by 1
Innovaciones para la elaboración de productos lácteos azucarados saludables tipo dulce de leche
Ranalli, N. (2015) · doi:10.35537/10915/45463 · Cited by 1
Enzymatic hydrolysis of heat-denatured whey proteins
O’Loughlin, I. B. (2014) · University of Limerick Institutional Repository (University of Limerick) · doi:10.34961/5698 · Cited by 1
Design of high solids emulsions for dehydration and carotenoids stabilisation
Lim, A. S. L. (2017) · Cork Open Research Archive (University College Cork, Ireland) · Cited by 1
Yang, C. (2017) · ERA: Education and Research Archive (University of Alberta) · doi:10.7939/r3d50g891 · Cited by 1
Brito‐Oliveira, T. C. (2021) · Digital Library of Theses and Dissertations (Universidade de São Paulo) · doi:10.11606/t.74.2021.tde-04112021-102447 · Cited by 1
Braitmaier, S. H., Wahl, A.-L., Atamer, Z., & Hinrichs, J. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4824049 · Cited by 1
Enzymatically modified whey protein and other protein-based fat replacers
Leman, J. (2007) · Elsevier eBooks · doi:10.1533/9781845693718.2.140 · Cited by 1
effet de l’extraction des protéines de tourteaux de chanvre sur leurs fonctionnalités
Potin, F. (2019) · theses.fr (ABES) · doi:10.70675/111da87azb71ez4d8dzbe43zc1909ca919ae · Cited by 1
Wang, J., Jia, F., & Yang, G. (2013) · Focusing on modern food industry
Geleificação a frio de isolados proteicos de soja
Diniz, A. C. P. (2007) · doi:10.47749/t/unicamp.2007.399591
Cavallieri, Â. L. F., & Cunha, R. L. (2007) · Americanae (AECID Library)
Tarhan, Ö. (2013) · IYTE GCRIS Database (Izmir Institute of Technology)
Mass Spectrometry in Protein, Peptide and Amino Acid Analysis
Corradini, C., Elviri, L., & Cavazza, A. (2010) · Royal Society of Chemistry eBooks · doi:10.1039/9781849730921-00078
Okolo, O. (2014) · The Atrium (University of Guelph)
Sutariya, S. G. (2015) · Open PRAIRIE (South Dakota State University)
Production and Evaluation of a Novel High-protein Product
Culler, M. D. (2015)
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
