The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
A review of physical and chemical protein-gel induction
Abstract
Protein gelation is important to obtain desirable sensory and textural structures in foods. Gelation phenomenon requires a driving force to unfold the native protein structure, followed by an aggregation retaining a certain degree of order in the matrix formed by association between protein strands. Protein gelation has been traditionally achieved by heating, but some physical and chemical processes form protein gels in an analogous way to heat-induction. A physical means, besides heat, is high pressure. Chemical means are acidification, enzymatic cross-linking, and use of salts and urea, causing modifications in protein–protein and protein–medium interactions. The characteristics of each gel are different and dependent upon factors like protein concentration, degree of denaturation caused by pH, temperature, ionic strength and/or pressure.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
Nakai, S. (1983) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf00118a001 · Cited by 421
Tombs, M. P. (1974) · Faraday Discussions of the Chemical Society · doi:10.1039/dc9745700158 · Cited by 216
Research works printed but not linked: 95
- Aguilera, 1995, Gelation of whey proteins, Food Technology, 49, 83
- Ando, 1989, Purification and characteristics of novel transglutaminase derived from microorganisms, Agricultural and Biological Chemistry, 53, 2613
- Angsupanich, 1999, Effects of high pressure on the myofibrillar proteins of cod and turkey muscle, Journal of Agriculture and Food Chemistry, 47, 92, 10.1021/jf980587p · DOI
- Ashie, 1999, High pressure effects on gelation of surimi and turkey breast muscle enhanced by microbial transglutaminase, Journal of Food Science, 64, 704, 10.1111/j.1365-2621.1999.tb15115.x · DOI
- Balny, 1993, Effects of high pressure on proteins, Food Review International, 9, 611, 10.1080/87559129309540980 · DOI · Paper page
- Barbut, 1993, Ca+2-Induced gelation of pre-heated whey protein isolates, Journal of Food Science, 58, 867, 10.1111/j.1365-2621.1993.tb09379.x · DOI · Paper page
- Bigelow, 1967, On the average hydrophobicity of proteins and their relation between it and protein structure, Journal of Theoretical Biology, 16, 187, 10.1016/0022-5193(67)90004-5 · DOI · Paper page
- Borderías, 1988, Fundamentos de la funcionalidad de las proteínas en alimentos, Revista de Agroquímica Y Tecnología de Alimentos, 28, 159
- Chanyonguorakul, 1997, Polymerisation of β-lactoglobulin and bovine serum albumin at oil–water interfaces in emulsions by transglutaminase, Food Hydrocoloids, 11, 449, 10.1016/S0268-005X(97)80043-4 · DOI
- Chawla, 1996, Gelation of proteins from washed muscle of threadfin bream (Nemipterus japonicus) under mild acid conditions, Journal of Food Science, 61, 362, 10.1111/j.1365-2621.1996.tb14194.x · DOI
- Cheftel, 1985, Protéines Alimentaries, Pp
- Clark, 1986, Functional Properties of Food Macromolecules, Pp
- Creighton, 1993, Proteins, Pp
- Damodaran, 1988, Refolding of thermally unfolded soy protein during the cooling regime of the gelation process: effect on gelation, Journal of Agriculture and Food Chemistry, 36, 262, 10.1021/jf00080a007 · DOI
- Damodaran, 1989, Food Proteins, Pp
- Dumay, 1998, Characteristics of pressure-induced gels of β-lactoglobulin at various times after pressure release, Lebensmittell-Wissenschaft und-Technologie, 31, 10, 10.1006/fstl.1997.0290 · DOI
- Dumoulin, 1998, Textural properties of pressure-induced gels of food proteins obtained under different temperatures including subzero, Journal of Food Science, 63, 92, 10.1111/j.1365-2621.1998.tb15683.x · DOI
- Dybowska, 1996, Effect of temperature and glucono-δ-lactone (GDL) concentration on milk aggregation and gelation as revealed by optical method, Milchwissenchaft, 51, 557
- Færgemand, 1997, Enzymatic cross-linking of whey proteins by a Ca2+-independent microbial transglutaminase from Sterptomyces ludicus, Food Hydrocolloids, 11, 19, 10.1016/S0268-005X(97)80006-9 · DOI
- Fernández, 1998, High pressure-cooking of chicken meat batters with starch, egg white and iota carrageenan, Journal of Food Science, 63, 267, 10.1111/j.1365-2621.1998.tb15723.x · DOI
- Ferry, 1948, Protein gels, Advances in Protein Science, 4, 1, 10.1016/S0065-3233(08)60004-2 · DOI · Paper page
- Foegeding, 1995, Factors that determine the fracture properties of globular protein gels, Food Hydrocolloids, 9, 237, 10.1016/S0268-005X(09)80254-3 · DOI
- Foegeding, 1986, Interactions of myosin-albumin and myosin-fibrinogen to form protein gels, Journal of Food Science, 51, 109, 10.1111/j.1365-2621.1986.tb10847.x · DOI
- Fretheim, 1985, Slow lowering of pH induces gel formation of myosin, Food Chemistry, 18, 169, 10.1016/0308-8146(85)90044-5 · DOI
- Gilleland, 1997, Covalent bonding in pressure-induced fish protein gels, Journal of Food Science, 62, 713, 10.1111/j.1365-2621.1997.tb15442.x · DOI
- Harwalkar, 1977, Gels prepared by adding d-glucono-δ-lactone to milk at high temperature, Milchwissenschaft, 32, 400
- Heremans, 1997, Food Proteins and Their Applications, Pp
- Hermansson, 1979, Functionality and Protein Structure, Pp
- Hermansson, 1986, Formation of two types of bovine myosin gels, Journal of the Science of Food and Agriculture, 37, 69, 10.1002/jsfa.2740370111 · DOI
- Ho, 2000, Technical approach to simplify the purification method and characterization of microbial transglutaminase produced from Streptoverticillium ladakanum, Journal of Food Science, 65, 76, 10.1111/j.1365-2621.2000.tb15959.x · DOI
- Hongsprabhas, 1997, Protein and salt effect on Ca+2-induced cold gelation of whey protein isolate, Journal of Food Science, 62, 382, 10.1111/j.1365-2621.1997.tb04006.x · DOI
- Hongsprabhas, 1997, Effects of N-ethylmelaimide and CaCl2 on cold gelation of whey protein isolate, Food Research International, 30, 451, 10.1016/S0963-9969(97)00068-9 · DOI
- Hongsprabhas, 1997, Structure-forming processes in Ca2+-induced whey protein isolate cold gelation, International Dairy Journal, 7, 827, 10.1016/S0958-6946(98)00011-9 · DOI
- Hongsprabhas, 1998, Ca2+-induced cold gelation of whey protein isolate: effect of two stage gelation, Food Research International, 30, 523, 10.1016/S0963-9969(98)00010-6 · DOI
- Hoover, 1993, Pressure effects on biological systems, Food Technology, 47, 150
- Huggins, 1951, Sulphydryl-disulphide relationship in the induction of gels in proteins by urea, Nature, 167, 592, 10.1038/167592a0 · DOI
- Ikeuchi, 1992, Dynamic rheological measurement on heat-induced pressured actomyosin gels, Journal of Agriculture and Food Chemistry, 40, 1751, 10.1021/jf00022a005 · DOI
- Imm, 2000, Gelation and water binding properties of transglutaminase -treated skim milk powder, Journal of Food Science, 65, 200, 10.1111/j.1365-2621.2000.tb15979.x · DOI
- Ipsen, 1999, Proceedings of the 1999 International Conference on Food Functionality
- Ju, 1998, Textural properties of cold-set gels induced from heat-denatured whey protein isolates, Journal of Food Science, 63, 288, 10.1111/j.1365-2621.1998.tb15728.x · DOI
- Ju, 1998, Effects of preheating on properties of aggregates and cold-set gels of whey protein isolates, Journal of Agriculture and Food Chemistry, 46, 3604, 10.1021/jf980392h · DOI
- Kang, 1994, Gelation and gel properties of soybean glycinin in a transglutaminase-catalysed system, Journal of Agriculture and Food Chemistry, 42, 159, 10.1021/jf00037a028 · DOI
- Katsuta, 1997, Isothermal gelation of proteins. 1. Urea induced gelation of whey proteins and their gelling mechanism, Food Hydrocolloids, 11, 367, 10.1016/S0268-005X(97)80033-1 · DOI
- Keshavarz, 1979, The relationship between hydrophobicity and interfacial tension of proteins, Biochimica et Biophysica Acta, 576, 269, 10.1016/0005-2795(79)90402-1 · DOI
- Kim, 1989, Rheological changes during slow acid induced gelation of milk by d-glucono-δ-lactone, Journal of Food Science, 54, 894, 10.1111/j.1365-2621.1989.tb07907.x · DOI
- Kim, 1993, Polymerisation of beef actomyosin induced by transglutaminase, Journal of Food Science, 58, 473, 10.1111/j.1365-2621.1993.tb04302.x · DOI
- Kinsella, 1994, Protein Structure-Function Relationship in Foods, Pp
- Kolakowski, 2001, Effects of high pressure and low temperature on b-lactoglobulin unfolding and aggregation, Food Hydrocolloids, 15, 215, 10.1016/S0268-005X(01)00017-0 · DOI
- Kuraishi, 1997, Production of restructured meat using microbial transglutaminase without salt or cooking, Journal of Food Science, 62, 488, 10.1111/j.1365-2621.1997.tb04412.x · DOI
- Kurth, 1983, Crosslinking of myosin and casein by the enzyme transglutaminase, Food Technology Australia, 35, 420
- Kurth, 1984, Transglutaminase catalysed cross-linking of myosin to soy protein, casein and gluten, Journal of Food Science, 49, 573, 10.1111/j.1365-2621.1984.tb12471.x · DOI
- Lee, 1997, Transglutaminase effects on low temperature gelation of fish proteins sols, Journal of Food Science, 62, 20, 10.1111/j.1365-2621.1997.tb04359.x · DOI
- Lucey, 1998, Formation and physical properties of acid milk gels: a review, Food Research International, 30, 529, 10.1016/S0963-9969(98)00015-5 · DOI · Paper page
- Matheis, 1984, A review: enzymatic cross-linking of proteins applicable to foods, Journal of Food Biochemistry, 11, 309, 10.1111/j.1745-4514.1987.tb00129.x · DOI
- Matsumura, 1996, Methods to Testing Protein Functionality, Pp
- Matsumura, 1996, Enhanced susceptibility to transglutaminase reaction of α-lactoglobulin in the molten globule state, Biochimica et Biophysica Acta, 1249, 69, 10.1016/0167-4838(95)00197-2 · DOI
- Matsumura, 2000, Molecular weight distributions of α-lactoglobulin polymers formed by mammalian and microbial transglutaminase, Food Hydrocolloids, 14, 49, 10.1016/S0268-005X(99)00045-4 · DOI
- McClements, 1993, Physical properties of cold-setting gels formed from heat-denatured whey protein isolated, Journal of the Science of Food and Agriculture, 69, 7, 10.1002/jsfa.2740690103 · DOI
- Mierovich, 1980, Empirical studies of hydrophobicity. 2. Distribution of the hydrophobic, hydrophilic, neutral, and ambivalent amino acids in the interior and exterior layers of native proteins, Macomolecules, 13, 1406, 10.1021/ma60078a014 · DOI
- Montero, 1997, Comparison of different gelation methods using washed sardine (Sardina pilchardus) mince: effects of temperature and pressure, Journal of Agriculture and Food Chemistry, 45, 4612, 10.1021/jf970400e · DOI
- Motoki, 1984, Functional properties of food proteins polymerized by transglutaminase, Agriculture and Biological Chemistry, 48, 1257
- Mulvihill, 1988, Gelation of β-lactoglobulin: effects of sodium chloride and calcium chloride on the rheological and structural properties of gels, Journal of Food Science, 53, 231, 10.1111/j.1365-2621.1988.tb10216.x · DOI
- Nakayama, 1983, New type of myosin gel induced by salts, Agriculture and Biological Chemistry, 47, 227
- Ngapo, 1996, 1,5-Glucono-δ-lactone-induced gelation of myofibrillar protein at chilled temperatures, Meat Science, 42, 3, 10.1016/0309-1740(95)00028-3 · DOI
- Ngapo, 1992, Proceedings of the 38th International Congress on Meat Science and Technology., Pp
- Nio, 1986, Gelation mechanism of protein solution by transglutaminase, Agriculture and Biological Chemistry, 50, 851
- Niwa, 1982, New gelling properties of Alaska pollack frozen mince induced by urea, Bulletin of Japan Society Science Fisheries, 48, 629
- Nonaka, 1989, Polymerization of several proteins by a Ca2+-independent transglutaminase derived from microorganisms, Agriculture and Biological Chemistry, 53, 2619
- Nonaka, 1994, Changes caused by microbial transglutaminase on physical properties of thermal induced soy protein gels, Food Hydrocolloids, 8, 1, 10.1016/S0268-005X(09)80139-2 · DOI
- Oakenfull, 1997, Food Proteins and Their Applications, Pp
- Okamoto, 1990, Application of high pressure to food processing: textural comparison of pressure- and heat-induced gels of food proteins, Agriculture and Biological Chemistry, 54, 183
- Otte, 1996, Protease-induced aggregation and gelation of whey proteins, Journal of Food Science, 61, 911, 10.1111/j.1365-2621.1996.tb10900.x · DOI
- Pérez-Mateos, 1997, High-pressure-induced gel of sardine (Sardina pilchardus) washed mince as affected by pressure-time-temperature, Journal of Food Science, 62, 1183, 10.1111/j.1365-2621.1997.tb12240.x · DOI
- Pérez-Mateos, 1997, Rheological and biochemical characteristics of high-pressure and heat-induced gels of blue whiting (Micromesistious poutassou) muscle proteins, Journal of Agriculture and Food Chemistry, 45, 44, 10.1021/jf960185m · DOI
- Phillips, 1994, Structure-Function Properties of Food Proteins, Pp
- Pomeranz, 1991, Functional Properties of Food Components, Pp
- Roff, 1996, Dicationic gelation of pre-denatures whey protein isolate, Food Hydrocolloids, 10, 193, 10.1016/S0268-005X(96)80034-8 · DOI
- Sakamoto, 1994, Strength of protein gels prepared with microbial transglutaminase as related to reaction conditions, Journal of Food Science, 59, 866, 10.1111/j.1365-2621.1994.tb08146.x · DOI
- Sakamoto, 1995, Gel strength enhancement by addition of microbial transglutaminase during onshore surimi manufacture, Journal of Food Science, 60, 300, 10.1111/j.1365-2621.1995.tb05660.x · DOI
- Samejima, 1986, Effects of temperature, actin-myosin ratio, pH, and salt and protein concentration on heat-induced gelling of cardiac myosin and reconstituted actomyosin, Agriculture and Biological Chemistry, 50, 2101
- Schmidt, 1981, Protein Functionality in Foods, Pp
- Shimada, 1980, Relationship between thermocoagulation and amino acid composition, Journal of Agriculture and Food Chemistry, 28, 413, 10.1021/jf60228a019 · DOI
- Smith, 1994, Protein Functionality in Food Systems, Pp
- Smith, 2000, High pressure unfolding of ovalbumin, International Journal of Food Science and Technology, 35, 361, 10.1046/j.1365-2621.2000.00395.x · DOI
- Totosaus, 2000, Dynamic rheological behaviour of meat proteins during acid-induced gelation, International Journal of Food Properties, 3, 465, 10.1080/10942910009524650 · DOI
- Venugopal, 1994, Gelation of shark myofibrillar proteins by weak organic acids, Food Chemistry, 50, 185, 10.1016/0308-8146(94)90118-X · DOI
- Walkenströn, 1997, Mixed gels of gelatine and whey proteins formed by combining temperature and high pressure, Food Hydrocolloids, 11, 457, 10.1016/S0268-005X(97)80044-6 · DOI
- Wong, 1989, Mechanism and Theory in Food Chemistry, Pp
- Xiong, 1990, Mechanism of urea induced whey protein gelation, Journal of Agriculture and Food Chemistry, 38, 1887, 10.1021/jf00100a001 · DOI
- Xiong, 1990, The effect of pH, thiol reagent and time on properties of urea-induced whey protein gels, Food Hydrocolloids, 4, 245, 10.1016/S0268-005X(09)80158-6 · DOI
- Xiong, 1991, Emulsified milkfat effects on rheology of acid-induced gels, Journal of Food Science, 56, 920, 10.1111/j.1365-2621.1991.tb14606.x · DOI
- Zasypkin, 1996, Pressure- and heat-induced gelation of mixed β-lactoglobulin/xanthan solutions, Food Hydrocolloids, 10, 203, 10.1016/S0268-005X(96)80036-1 · DOI
- Zayas, 1997, Functionality of Proteins in Foods, Pp, 10.1007/978-3-642-59116-7 · DOI · Paper page
- Zhu, 1995, Microbial transglutaminase – A review of its production and application in food processing, Applied Microbiology and Biotechnology, 44, 277, 10.1007/s002530050554 · DOI
- Ziegler, 1990, The gelation of proteins, Advances in Food and Nutrition Research, 34, 203, 10.1016/S1043-4526(08)60008-X · DOI · Paper page
Cited by
Natural biopolymer‐based hydrogels for use in food and agriculture
Klein, M., & Poverenov, E. (2020) · Journal of the Science of Food and Agriculture · doi:10.1002/jsfa.10274 · Cited by 259
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
Zhou, H., Hu, X., Xiang, X., & McClements, D. J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2023.108909 · Cited by 105
Zhao, C., Wang, F., Yang, X., Mao, Y., Qi, Q., Zheng, M., Xu, X., Cao, Y., Wu, Y., & Liu, J. (2023) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.108374 · Cited by 84
Mixing plant-based proteins: Gel properties of hemp, pea, lentil proteins and their binary mixtures
Guidi, S., Formica, F. A., & Denkel, C. (2022) · Food Research International · doi:10.1016/j.foodres.2022.111752 · Cited by 83
Metadata
- Authors
- Totosaus, A., Montejano, J. G., Salazar, J. A., & Guerrero, I.
- Venue
- International Journal of Food Science and Technology
- Publisher
- Oxford University Press (OUP)
- Published
- 2002-07-25
- Volume
- 37
- Issue
- 6
- Pages
- 589-601
- ISSN
- 0950-5423 (ISSN-L)
- 1365-2621
- OpenAlex
- W2100674205
- Cited by
- 488
- References
- 2
- FWCI
- 5.98
- Type
- journal article
- Language
- en
- Open access
- closed
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
How to cite
Cite CoChat for the checks on this page, and the paper for its own findings.
- This page
- CoChat. (2026). Citation check: A review of physical and chemical protein-gel induction. https://app.cochat.ai/papers/10.1046/j.1365-2621.2002.00623.x
- The paper
- Totosaus, A., Montejano, J. G., Salazar, J. A., & Guerrero, I. (2002). A review of physical and chemical protein-gel induction. International Journal of Food Science and Technology. https://doi.org/10.1046/j.1365-2621.2002.00623.x
Data sources
Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.