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The Enzymatic Coagulation of Milk

Dalgleish, D. G.·1993·Cheese: Chemistry, Physics and Microbiology

DOI 10.1007/978-1-4615-2650-6_3

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Park, Y. W. (2001) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(01)70202-0 · Cited by 129
Enzymes in cheese technology
Fox, P. F., & Stepaniak, L. (1993) · International Dairy Journal · doi:10.1016/0958-6946(93)90029-y · Cited by 129
Rheology, Microstructure, and Functionality of Low-Fat Iranian White Cheese Made with Different Concentrations of Rennet
Madadlou, A., Khosroshahi, A., & Mousavi, M. (2005) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(05)72986-6 · Cited by 134
“show no tendency to aggregate (Dalgleish, 1997).”
Effect of Insoluble Calcium Concentration on Rennet Coagulation Properties of Milk
Choi, J.-W., Horne, D. S., & Lucey, J. A. (2007) · Journal of Dairy Science · doi:10.3168/jds.2006-814 · Cited by 129
Milk protein coagulation under gastric conditions: A review
Huppertz, T., & Chia, L. W. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104882 · Cited by 146
Biochemistry of Cheese Ripening: Proteolysis
Ardö, Y., McSweeney, P. L. H., Magboul, A. A. A., Upadhyay, V. K., & Fox, P. F. (2017) · Cheese · doi:10.1016/b978-0-12-417012-4.00018-1 · Cited by 121
Bioactive Peptides in Ovine and Caprine Cheeselike Systems Prepared with Proteases from Cynara cardunculus
Silva, S. V., Pihlanto, A., & Malcata, F. X. (2006) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(06)72370-0 · Cited by 135
Biotechnological Methods to Accelerate Cheddar Cheese Ripening
Azarnia, S., Robert, N., & Lee, B. H. (2006) · Critical Reviews in Biotechnology · doi:10.1080/07388550600840525 · Cited by 121
“However, both enzymes hydrolyze the same bond of κ-casein, which leads to milk coagulation (Dalgleish, 1993).”
Background
Impaired rennetability of heated milk; study of enzymatic hydrolysis and gelation kinetics.
Vasbinder, A. J., Rollema, H., & de Kruif, C. D. (2003) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(03)73740-0 · Cited by 116
“This confirms one of the hypotheses often proposed in the literature (Dalgleish, 1990b; Wauguna et al., 1996; Raynal and Remeuf, 1998; Steffl et al., 1999; Singh and Wauguna, 2001).”
BackgroundResultInfluential
Rennet-Induced Coagulation of Milk
Horne, D., & Lucey, J. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-417012-4.00005-3 · Cited by 112
Monitoring the identity and the structure of soft cheeses by fluorescence spectroscopy
Herbert, S., Riou, N. M., Devaux, M., Riaublanc, A., Bouchet, B., Gallant, D., & Dufour, E. (2000) · Le Lait · doi:10.1051/lait:2000149 · Cited by 110
“measurements [5, 18, 22, 37, 38] agreed”
Fluorescence Spectroscopy Investigation of Acid-or Rennet-Induced Coagulation of Milk
Herbert, S., Riaublanc, A., Bouchet, B., Gallant, D., & Dufour, E. (1999) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(99)75446-9 · Cited by 110
“The resulting para-CN micelles spontaneously aggregate in a second phase of the process before a re-arrangement step takes place (4, 10).”
Background
Improvement of vitamin C stability in vitamin gummies by encapsulation in casein gel
Yan, B.-F., Davachi, S. M., Ravanfar, R., Dadmohammadi, Y., Deisenroth, T., Pho, T. V., Odorisio, P., Darji, R. H., & Abbaspourrad, A. (2020) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2020.106414 · Cited by 107
Casein micelle structure and stability
Horne, D. S. (2008) · Milk Proteins · doi:10.1016/b978-0-12-374039-7.00005-2 · Cited by 99
Influence of glycosylation on micelle-stabilizing ability and biological properties of C-terminal fragments of cow's κ-casein
Dziuba, J., & Mińkiewicz, P. (1996) · International Dairy Journal · doi:10.1016/0958-6946(95)00074-7 · Cited by 98
Effect of soluble calcium on the renneting properties of casein micelles as measured by rheology and diffusing wave spectroscopy
Sandra, S., Ho, M., Alexander, M., & Corredig, M. (2011) · Journal of Dairy Science · doi:10.3168/jds.2011-4713 · Cited by 108
“No differences were observed among all milk samples and all samples reached 90% of CMP release, the point necessary to reach the coagulation (Dalgleish, 1982; Sandra and Dalgleish, 2007), about 40 min after rennet addition.”
Background
Cheddar cheese ripening and flavor characterization: A review
Murtaza, M. A., Ur-Rehman, S., Anjum, F. M., Huma, N., & Hafiz, I. (2014) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2011.634531 · Cited by 94
“The casein micelles become unstable following the removal of these hydrophilic peptides; then, at an appropriate temperature (e.g., 30◦C) the milk coagulates under the influence of Ca2+ in the medium (Dalgleish, 1993).”
Background
Pre-treatment of cheese milk: principles and developments
Kelly, A., Huppertz, T., & Sheehan, J. (2008) · doi:10.1051/dst:2008017 · Cited by 93
“In the cheese vat, high heat treatment of milk prolongs rennet coagulation times and reduces the strength of rennet gels [5, 26], leading to impaired syneresis [10, 92, 115].”
Background
Rennet coagulation of skim milk and curd drainage: effect of pH, casein concentration, ionic strength and heat treatment
Daviau, C., Famelart, M., Pierre, A., Goudédranche, H., & Maubois, J. (2000) · Le Lait · doi:10.1051/lait:2000134 · Cited by 91
“8 leads to faster rennet coagulation [7, 11] and faster syneresis [30].”
Background
Advances in the role of a plant coagulant ( Cynara cardunculus ) in vitro and during ripening of cheeses from several milk species
Sousa, M. J., & Malcata, F. X. (2002) · Le Lait · doi:10.1051/lait:2002001 · Cited by 84
“The hypothesised distinct primary site of proteolysis on κ-casein may lead to more extensive losses of soluble peptides [14].”
Background
Effect of pH at heat treatment on the hydrolysis of κ-casein and the gelation of skim milk by chymosin
Anema, S., Lee, S. K., & Klostermeyer, H. (2007) · LWT · doi:10.1016/j.lwt.2005.08.002 · Cited by 84
Rennets: their role in milk coagulation and cheese ripening
Fox, P. F., & McSweeney, P. L. H. (1997) · Springer eBooks · doi:10.1007/978-1-4613-1121-8_1 · Cited by 98
Effect of milk protein standardization, by ultrafiltration, on the manufacture, composition and maturation of Cheddar cheese
Guinee, T. P., Pudja, P. D., & Mulholland, E. O. (1994) · Journal of Dairy Research · doi:10.1017/s0022029900028119 · Cited by 83
Casein micelle dispersions into water, NaCl and CaCl2: physicochemical characteristics of micelles and rennet coagulation
Famelart, M., Graet, Y. L., & Raulot, K. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00077-1 · Cited by 75
“Addition of CaCl 2 in milk leads to either a decrease in clotting time (Dalgleish, 1992), or a minimum at 0.”
Background
Delineation of the structure of soft cheeses at the molecular level by fluorescence spectroscopy—relationship with texture
Dufour, E., Devaux, M., Fortier, P., & Herbert, S. (2001) · International Dairy Journal · doi:10.1016/s0958-6946(01)00086-3 · Cited by 71
Bovine milk protein properties and the manufacturing quality of milk
Dalgleish, D. (1993) · Livestock Production Science · doi:10.1016/0301-6226(93)90183-i · Cited by 71
Self-citation
Proteolysis of milk proteins lactosylated in model systems.
Dalsgaard, T., Nielsen, J. H., & Larsen, L. B. (2007) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200600112 · Cited by 68
Acid- and acid/rennet-curd cheeses part A: Quark, cream cheese and related varieties
Schulz-Collins, D., & Senge, B. (2004) · Cheese · doi:10.1016/s1874-558x(04)80049-6 · Cited by 67
Digestion of food proteins: the role of pepsin
Yang, M., Yang, Z., Everett, D. W., Gilbert, E. P., Singh, H., & Ye, A. (2025) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2025.2453096 · Cited by 65
“Consequently, milk coagulation time is inversely dependent on enzyme concentration (Figure 3B3) (Dalgleish 1993; Carlson, Hill, and Olson 1987a; López, Lomholt, and Qvist 1998; Foltmann 1959; Hyslop, Richardson, and Ryan 1979).”
Effect of Increasing Dietary Threonine Intakes on Amino Acid Metabolism of the Central Nervous System and Peripheral Tissues in Growing Rats
Boehm, G., Cervantes, H., Georgi, G., Jelinek, J., Sawatzki, G., Wermuth, B., & Colombo, J. (1998) · Pediatric Research · doi:10.1203/00006450-199812000-00013 · Cited by 65
Proteolysis of Ovine and Caprine Caseins in Solution by Enzymatic Extracts from Flowers of Cynara cardunculus
Sousa, M. J., & Malcata, F. X. (1998) · Enzyme and Microbial Technology · doi:10.1016/s0141-0229(97)00173-7 · Cited by 64
Effect of heat treatment of rennet skim milk induced coagulation on the rheological properties and molecular structure determined by synchronous fluorescence spectroscopy and turbiscan.
Blecker, C., Habib-Jiwan, J.-M., & Karoui, R. (2012) · Food Chemistry · doi:10.1016/j.foodchem.2012.06.035 · Cited by 60
Progress in the field of aspartic proteinases in cheese manufacturing: structures, functions, catalytic mechanism, inhibition, and engineering
Yeğin, S., & Dekker, P. (2013) · Dairy Science and Technology · doi:10.1007/s13594-013-0137-2 · Cited by 68
“This is due to the loss of enzymatic activity and also the slow coagulation rate of rennetedmicelles at or below this temperature (Dalgleish 1999).”
Background
Application of capillary electrophoresis to the study of proteolysis of caseins
Recio, I., Amigo, L., Ramos, M., & López-Fandiño, R. (1997) · Journal of Dairy Research · doi:10.1017/s0022029996002087 · Cited by 59
Use of artichoke (Cynara scolymus) flower extract as a substitute for bovine rennet in the manufacture of Gouda-type cheese: Characterization of aspartic proteases
Llorente, B. E., Obregón, W. D., Avilés, F. X., Caffini, N. O., & Cavalli, S. V. (2014) · Food Chemistry · doi:10.1016/j.foodchem.2014.03.007 · Cited by 61
“This includes the rapid and highly specific cleavage of the hydrophilic caseinomacropeptide part from j-casein molecules located at the periphery of the casein micelles (Dalgleish, 1987; Visser, 1993).”
Background
Microstructure and rheological properties of Iranian white cheese coagulated at various temperatures.
Madadlou, A., Khosroshahi, A., Mousavi, S. M., & Djome, Z. E. (2006) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(06)72308-6 · Cited by 58
“aggregation rate (Dalgleish, 1993), which in turn affects”
Effects of lactation stage, parity, β-lactoglobulin genotype and milk SCC on whey protein composition in Sarda dairy ewes
Nudda, A., Feligini, M., Battacone, G., Macciotta, N., & Pulina, G. (2003) · doi:10.4081/ijas.2003.29 · Cited by 58
“There is also a notable relationship between WP and the technical properties of milk; denaturation of BLG at high temperatures markedly reduces the rennetability of the milk (Dalgleish, 1993).”
Background
Mechanism for the ethanol-dependent heat-induced dissociation of casein micelles.
O'Connell, J., Kelly, A., Fox, P., & de Kruif, K. D. (2001) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf001479h · Cited by 58
Sources, purification, immobilization and industrial applications of microbial lipases: An overview
Enespa, Chandra, P., & Singh, D. P. (2022) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2022.2038076 · Cited by 67
Effect of commercial grape extracts on the cheese-making properties of milk.
da Silva, D. F., Matumoto‐Pintro, P., Bazinet, L., Couillard, C., & Britten, M. (2015) · Journal of Dairy Science · doi:10.3168/jds.2014-8796 · Cited by 56
Ultrasonic analysis of rennet-induced pre-gelation and gelation processes in milk
Dwyer, C., Donnelly, L., & Buckin, V. (2005) · Journal of Dairy Research · doi:10.1017/s0022029905001020 · Cited by 56
“Second stage of renneting, aggregation of micelles The increase in the attenuation in the time interval between 7 and 20 min could be attributed to the aggregation of the casein micelles (Green et al. 1978; Dalgleish, 1993; Lucey, 2001).”
BackgroundResult
Enzymatic Coagulation of Milk
Hyslop, D. B. (2003) · Springer eBooks · doi:10.1007/978-1-4419-8602-3_24 · Cited by 56
Coagulation of milk enriched with ultrafiltered or diafiltered microfiltered milk retentate powders
Caron, A., St-Gelais, D., & Pouliot, Y. (1997) · doi:10.1016/s0958-6946(97)00024-1 · Cited by 54
Sour orange Citrus aurantium L. flowers: A new vegetable source of milk-clotting proteases
Mazorra-Manzano, M., Moreno-Hernández, J. M., Ramírez-Suárez, J. C., Torres-Llanez, M. D. J., González-Córdova, A. F., & Vallejo-Córdoba, B. (2013) · LWT · doi:10.1016/j.lwt.2013.07.009 · Cited by 53
Interaction between casein micelles and whey protein/κ-casein complexes during renneting of heat-treated reconstituted skim milk powder and casein micelle/serum mixtures.
Kethireddipalli, P., Hill, A., & Dalgleish, D. (2011) · Journal of Agricultural and Food Chemistry · doi:10.1021/jf103943e · Cited by 51
Self-citation
Effect of β-casein concentration in cheese milk on rennet coagulation properties, cheese composition and cheese ripening
St‐Gelais, D., & Haché, S. (2004) · Food Research International · doi:10.1016/j.foodres.2004.11.006 · Cited by 50
Novel assay for the determination of residual coagulant activity in cheese
Hurley, M., O'driscoll, B., Kelly, A., & McSweeney, P. (1999) · International Dairy Journal · doi:10.1016/s0958-6946(99)00118-1 · Cited by 51
Ultrasonic study of milk clotting
Benguigui, L., Emery, J., Durand, D., & Busnel, J. (1994) · Le Lait · doi:10.1051/lait:1994317 · Cited by 50
Engineering artificial casein micelles for future food: Is casein phosphorylation necessary?
Antuma, L. J., Steiner, I., Garamus, V., Boom, R., & Keppler, J. (2023) · Food Research International · doi:10.1016/j.foodres.2023.113315 · Cited by 49
“The proteolysis of κ -casein by enzymes in rennet results in a loss in steric stabilisation and a reduction in the electrostatic repulsion between micelles (Dalgleish, 1993).”
Influence of denaturation and aggregation of β-lactoglobulin on rennet coagulation properties of skim milk and ultrafiltered milk
Waungana, A., Singh, H., & Bennett, R. (1996) · doi:10.1016/s0963-9969(97)00011-2 · Cited by 49
Milk protein gels
Lucey, J. (2020) · Milk Proteins · doi:10.1016/b978-0-12-374039-7.00016-7 · Cited by 49
On effects of subclinical mastitis and stage of lactation on milk quality in goats
Silanikove, N., Merin, U., & Leitner, G. (2014) · doi:10.1016/j.smallrumres.2014.07.018 · Cited by 48
“In milk from uninfected glands, curd yield depends mainly the content and subtypes of αS1-, β- and κ-caseins (Hyslop, 2003; Vazquez-Flores et al., 2012; Mestawet et al., 2014), fat level, and protein to fat ratio (Guinee et al.”
Background
Application and validation of the lattice Boltzmann method for modelling flow-related clotting.
Harrison, S. E., Smith, S., Bernsdorf, J., Hose, D., & Lawford, P. (2007) · Journal of Biomechanics · doi:10.1016/j.jbiomech.2007.01.026 · Cited by 46
“onset of clot formation is known as the clotting time (Dalgleish, 1982; Payens et al., 1977; Payens, 1977).”
Background
Composition, coagulation characteristics, and cheese making capacity of yak milk
Zhang, J., Yang, M. D., Cai, D., Hao, Y., Zhao, X. Y., Zhu, Y., Zhu, H. M., & Yang, Z. (2019) · Journal of Dairy Science · doi:10.3168/jds.2019-17231 · Cited by 49
Effect of coagulation conditions on the microstructure and the large deformation properties of fat-free Feta cheese made from ultrafiltered milk
Wium, H., Pedersen, P. S., & Qvist, K. B. (2003) · doi:10.1016/s0268-005x(02)00079-6 · Cited by 45
“Also, the aggregation rate increases with temperature (Dalgleish, 1993), and hydrophobic interactions are enhanced.”
Background
Comparison of total milk-clotting activity measurement precision using the Berridge clotting time method and a proposed optical method
Tabayehnejad, N., Castillo, M., & Payne, F. (2012) · Journal of Food Engineering · doi:10.1016/j.jfoodeng.2011.09.009 · Cited by 44
“Note that casein micelles cannot appreciably aggregate until the degree of hydrolysis reaches 60-80% (Carlson et al., 1987; Dalgleish, 1993).”
Background
Effects of Limited Proteolysis on the Microstructure of Heat-Induced Whey Protein Gels at Varying pH
Otte, J., Ju, Z., Skriver, A., & Qvist, K. B. (1996) · doi:10.3168/jds.s0022-0302(96)76426-3 · Cited by 44
Accumulation γ-Aminobutyric Acid and Biogenic Amines in a Traditional Raw Milk Ewe’s Cheese
Tofalo, R., Perpetuini, G., Battistelli, N., Pepe, A., Ianni, A., Martino, G., & Suzzi, G. (2019) · Foods · doi:10.3390/foods8090401 · Cited by 45
Influence of different oral rehydration solutions on abomasal conditions and the acid-base status of suckling calves.
Bachmann, L., Homeier, T., Arlt, S., Brueckner, M., Rawel, H. M., Deiner, C., & Hartmann, H. (2009) · Journal of Dairy Science · doi:10.3168/jds.2008-1487 · Cited by 43
“This pH value is the isoelectric point of the caseins so that the casein micelles lose stability due to charge equalization (Dalgleish, 1992).”
Background
Comparison of milk protein composition and rennet coagulation properties in native Swedish dairy cow breeds and high-yielding Swedish Red cows.
Poulsen, N., Glantz, M., Rosengaard, A. K., Paulsson, M., & Larsen, L. B. (2017) · Journal of Dairy Science · doi:10.3168/jds.2017-12920 · Cited by 42
“Higher levels of ionic calcium will lower the surface charge of para-casein and improve cross-linking during aggregation (Dalgleish, 1983; Hyslop, 2003).”
Background
Rennets: General and Molecular Aspects
Crabbe, M. (2004) · Cheese · doi:10.1016/s1874-558x(04)80061-7 · Cited by 42
Manufacture and Properties of Milk Powders
Kelly, A., O'Connell, J., & Fox, P. (2003) · doi:10.1007/978-1-4419-8602-3_29 · Cited by 42
Revisiting the temperature dependence of the coagulation of renneted bovine casein micelles
Horne, D., & Lucey, J. (2014) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2013.12.021 · Cited by 41
Effect of protein and temperature on cutting time prediction in goats' milk using an optical reflectance sensor
Castillo, M., Payne, F., Hicks, C. L., Laencina, J., & López, M.-B. (2003) · Journal of Dairy Research · doi:10.1017/s0022029903006113 · Cited by 41
“A casein micelle is able to aggregate only if a critical percentage of its k-casein has been hydrolysed (Dalgleish, 1993).”
BackgroundMethod
The effect of dietary crude protein and phosphorus on grass-fed dairy cow production, nutrient status, and milk heat stability.
Reid, M., O'Donovan, M., Elliott, C., Bailey, J., Watson, C., Lalor, S., Corrigan, B., Fenelon, M., & Lewis, E. (2015) · Journal of Dairy Science · doi:10.3168/jds.2014-8437 · Cited by 41
Differential Somatic Cell Count as a Novel Indicator of Milk Quality in Dairy Cows
Stocco, G., Summer, A., Cipolat-Gotet, C., Zanini, L., Vairani, D., Dadousis, C., & Zecconi, A. (2020) · Animals · doi:10.3390/ani10050753 · Cited by 40
“These results about the effect of different ranges of DSCC on milk composition are particularly important in the case of milk destined for cheese-making, as the concentration of each component in milk strongly influences coagulation properties and the cheese-making ability of milk [42].”
Background
Addition of sodium caseinate to skim milk inhibits rennet-induced aggregation of casein micelles
Gaygadzhiev, Z., Massel, V., Alexander, M., & Corredig, M. (2012) · doi:10.1016/j.foodhyd.2011.02.015 · Cited by 40
Effect of coagulant type and storage temperature on the functionality of reduced-fat Mozzarella cheese
Sheehan, J. J., O’Sullivan, K., & Guinee, T. P. (2004) · Le Lait · doi:10.1051/lait:2004031 · Cited by 34
Dairy maturation of milk used in the manufacture of Parmigiano-Reggiano cheese: effects on physico-chemical characteristics, rennet-coagulation aptitude and rheological properties
Malacarne, M., Summer, A., Formaggioni, P., Franceschi, P., Sandri, S., Pecorari, M., Vecchia, P., & Mariani, P. (2008) · Journal of Dairy Research · doi:10.1017/s0022029908003221 · Cited by 38
“This parameter has a certain technological interest : it represents an index of the availability of ionic calcium (Ca+ +) during the second phase of milk rennet-coagulation, e.g. the aggregation of paracasein micelles (Hyslop, 2003).”
Background
Applications of protein crosslinking in food products
Sulaiman, N. S., Sintang, M. D., Zaini, H. M., Munsu, E., Matajun, P., & Pindi, W. (2022) · International food research journal · doi:10.47836/ifrj.29.4.01 · Cited by 37
“In particular, protein modification in curd and cheese yields has become a matter of great interest as a considerable number of proteins are lost in whey during rennet clotting (Fox et al., 2017).”
Background
Production and characterization of recombinant cyprosin B in Saccharomyces cerevisiae (W303-1A) strain
Sampaio, P., Fortes, A. M., Cabral, J. M. S., Pais, M. S., & Fonseca, L. P. (2008) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.105.305 · Cited by 45
On the activity and specificity of cardosin B, a plant proteinase, on ovine caseins
Silva, S. V., & Malcata, F. X. (1999) · Food Chemistry · doi:10.1016/s0308-8146(99)00126-0 · Cited by 34
Properties and applications of phytepsins from thistle flowers
Cavalli, S. V., Lufrano, D., Colombo, M. L., & Priolo, N. S. (2013) · Phytochemistry · doi:10.1016/j.phytochem.2013.04.013 · Cited by 41
Dairy enzymology
Stepaniak, L. (2004) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2004.00144.x · Cited by 51
“The specificity of chymosin on caseins and the coagulation mechanism have been studied extensively (McSweeney et al. 1993; Chitpinityol and Crabbe 1998; Mooney et al. 1998; Soeryapranata et al. 2002; Hyslop 2003).”
Background
Nondestructive monitoring of renetted whole milk during cheese manufacturing
Koc, A. B., & Özer, B. (2008) · doi:10.1016/j.foodres.2008.05.008 · Cited by 34
Chymosin, Pepsins and Other Aspartyl Proteinases: Structures, Functions, Catalytic Mechanism and Milk-Clotting Properties
Uniacke‐Lowe, T., & Fox, P. F. (2017) · Elsevier eBooks · doi:10.1016/b978-0-12-417012-4.00004-1 · Cited by 36
What is the impact of amino acid mutations in the primary structure of caseins on the composition and functionality of milk and dairy products?
Daniloski, D., McCarthy, N., Huppertz, T., & Vasiljevic, T. (2022) · Current Research in Food Science · doi:10.1016/j.crfs.2022.09.026 · Cited by 33
“For casein micelles, it is generally agreed that the κ-casein content was negatively correlated with size of the casein micelles (Bijl, de Vries, van Valenberg, Huppertz and Van Hooijdonk, 2014a; Dalgleish, 1993; Day et al., 2015).”
Background
The inhibitory roles of native whey protein on the rennet gelation of bovine milk.
Gamlath, C. J., Leong, T. S. H., Ashokkumar, M., & Martin, G. J. O. (2018) · Food Chemistry · doi:10.1016/j.foodchem.2017.10.029 · Cited by 33
“…and Discussion 229 3.1 Overall kinetics of gelation 230 Rennet induced gelation of milk proceeds in three overlapping stages: i) hydrolysis of κ-casein, 231 ii) interaction between para-casein micelles, and iii) the formation of a cross-linked gel 232 (Carlson & Hill Jr, 1987; Hyslop, 2003).”
BackgroundInfluential
Microstructure and textural properties of Kareish cheese manufactured by various ways
Hussein, G., & Shalaby, S. M. (2014) · Annals of Agricultural Science Cairo · doi:10.1016/j.aoas.2014.06.004 · Cited by 33
“Before they are renneted, the casein micelles in milk show no tendency to aggregate (Dalgleish, 1997).”
Background
Comparison of the rheology of mozzarella-type curd made from buffalo and cows’ milk
Hussain, I., Bell, A. E., & Grandison, A. S. (2011) · Food Chemistry · doi:10.1016/j.foodchem.2011.03.069 · Cited by 28
Monitoring of milk gelation using a low-frequency ultrasonic technique
Nassar, G., Nongaillard, B., & Noël, Y. (2001) · Journal of Food Engineering · doi:10.1016/s0260-8774(00)00178-3 · Cited by 31
Properties of Gels Induced by Heat, Protease, Calcium Salt, and Acidulant from Calcium Ion-Aggregated Whey Protein Isolate
Ju, Z., & Kilara, A. (1998) · doi:10.3168/jds.s0022-0302(98)75684-x · Cited by 33
Significance of Indigenous Enzymes in Milk and Dairy Products
Fox, P. F. (2002) · CRC Press eBooks · doi:10.1201/9780203910450.ch19 · Cited by 32
“Reviews on the enzymatic coagulation of milk include Dalgleish (8, 9), Fox (10–12), Fox and Mulvihill (13), and Fox and McSweeney (14).”
BackgroundInfluential
Comparative proteomic analysis of casein and whey as prepared by chymosin-induced separation, isoelectric precipitation or ultracentrifugation
Jensen, H. B., Poulsen, N., Møller, H., Stensballe, A., & Larsen, L. B. (2012) · Journal of Dairy Research · doi:10.1017/s0022029912000404 · Cited by 32
“Chymosin, being a neonatal gastric aspartic endoprotease, cleaves κ-casein with high specificity for the Phe105–Met106 peptide bond, dividing κ-casein into a hydrophobic para-κ-casein associated with the casein fraction, and a hydrophilic, soluble caseinomacropeptide (Hyslop, 2003).”
Background
Can the use of Australian cardoon (Cynara cardunculus L.) coagulant overcome the quality problems associated with cheese made from ultrafiltered milk?
Agboola, S. O., Chan, H. H., Zhao, J., & Rehman, A. (2009) · LWT - Food Science and Technology · doi:10.1016/j.lwt.2009.03.015 · Cited by 31
“Although clotting properties of milk can be good indices for cheese-making performance (Dalgleish, 1999), it is still important to study the actual cheese making process, due to the influence of other ingredients and the processing conditions on the final product.”
Background

Authors: Dalgleish, D. G.
Affiliations: University of Guelph (CA)
Corresponding author: Dalgleish, D. G.
Venue: Cheese: Chemistry, Physics and Microbiology
Publisher: Springer US
Published: 1993
Volume: 1
Pages: 69-100
DOI: 10.1007/978-1-4615-2650-6_3
OpenAlex: W1881198270
Cited by: 216
References: 0
Citations by year: 2026: 1 · 2025: 6 · 2024: 2 · 2023: 4 · 2022: 8 · 2021: 4 · 2020: 5 · 2019: 2 · 2018: 1 · 2017: 9 · 2016: 5 · 2015: 6 · 2014: 12 · 2013: 9 · 2012: 3
FWCI: 23.60
Type: book chapter
Language: en
Open access: closed
Locations: Springer eBooks (publishedVersion)
Topics: Life Sciences › Agricultural and Biological Sciences › Food Science › Proteins in Food Systems
Life Sciences › Agricultural and Biological Sciences › Animal Science and Zoology › Milk Quality and Mastitis in Dairy Cows
Life Sciences › Biochemistry, Genetics and Molecular Biology › Biotechnology › Enzyme Production and Characterization
Keywords: milk coagulation, rennet, chymosin, kappa-casein, casein micelles, proteolytic enzymes, pepsin, cheese production, micelle aggregation

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The Enzymatic Coagulation of Milk

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