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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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Lin, L., Oh, H. E., Deeth, H., & Wong, M. (2021) · doi:10.1016/j.idairyj.2020.104893 · Cited by 24
The Impact of Microbial Transglutaminase on the Quality and Antioxidant Activity of Camel-Milk Soft Cheese
Abou‐Soliman, N. H. I., Awad, S., & El-Sayed, M. (2020) · Food and Nutrition Sciences · doi:10.4236/fns.2020.113012 · Cited by 24
“The first one is to give rennet an adequate time to cleave κ-casein because casein micelles are not able to aggregate until about 60% - 80% of their κ-casein is degraded [38].”
Background
Cynara cardunculus: Use in Cheesemaking and Pharmaceutical Applications
Conceição, C., Martins, P., de Alvarenga, N. B., Dias, J. M., Lamy, E., Garrido, L. H., Gomes, S., Freitas, S., Belo, A. T., Brás, T., et al. (2018) · InTech eBooks · doi:10.5772/intechopen.76530 · Cited by 38
“The effect of calcium in the enzymatic coagulation for cheesemaking is well known and it is considered an important technological factor; it is essential for micellar aggregation, especially its Ca2+ ionic form, whose proportion depends on milk pH [110, 114, 120].”
Background
Production of Bioactive Recombinant Bovine Chymosin in Tobacco Plants
Wei, Z.-Y., Zhang, Y.-Y., Wang, Y., Fan, M., Zhong, X.-F., Xu, N., Lin, F., & Xing, S.-C. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17050624 · Cited by 24
“Cheeses are distinguished by their flavors and/or textures which depend both on their composition and the chymosin used in cheese processing to coagulate the milk [1–4].”
Background
The effect of high and low levels of supplementation on milk production, nitrogen utilization efficiency, and milk protein fractions in late-lactation dairy cows.
Reid, M., O'Donovan, M., Murphy, J. P., Fleming, C., Kennedy, E., & Lewis, E. (2015) · Journal of Dairy Science · doi:10.3168/jds.2014-9016 · Cited by 24
Genetic parameters for rennet- and acid-induced coagulation properties in milk from Swedish Red dairy cows
Gustavsson, F., Glantz, M., Poulsen, N. A., Wadsö, L., Stålhammar, H., Andrén, A., Månsson, H. L., Larsen, L. B., Paulsson, M. A., & Fikse, W. F. (2014) · Journal of Dairy Science · doi:10.3168/jds.2014-7996 · Cited by 23
Isolation and Partial Characterisation of Milk-clotting Aspartic Protease from Streblus asper
Sivanesan, S., Ramasamy, D., & Subramanian, S. (2006) · Food Science and Technology International · doi:10.1177/1082013206063839 · Cited by 21
“In this respect it may be stated that other milk-clotting enzymes (e.g. calf chymosin, various pepsins and mucor proteases) cleaving the phe105-met106 bond of -casein are of aspartic acid type (Dalgleish, 1982).”
Background
Axial compression properties of calcium caseinate gels
Konstance, R. (1993) · doi:10.3168/jds.s0022-0302(93)77669-9 · Cited by 23
Rheological Properties of Goat Milk Coagulation as Affected by Rennet Concentration, pH and Temperature
Hovjecki, M., Miloradović, Z., Barukčić, I., Blažić, M., & Miočinović, J. (2022) · Fermentation · doi:10.3390/fermentation8060291 · Cited by 21
Effect of high-pressure processing on the characteristics of cheese made from ultrafiltered milk: Influence of the kind of rennet
Ribeiro, L. R., Júnior, B. R. D. C. L., & Cristianini, N. (2018) · Innovative Food Science & Emerging Technologies · doi:10.1016/j.ifset.2018.10.012 · Cited by 23
Rennet-induced gelation of concentrated milk in the presence of sodium caseinate: differences between milk concentration using ultrafiltration and osmotic stressing.
Nair, P., & Corredig, M. (2015) · Journal of Dairy Science · doi:10.3168/jds.2014-8356 · Cited by 21
“…the enzyme chymosin specifically cleaves the protective layer of κ-casein from the surface of the casein micelles; this reaction results in the loss of steric stabilization, leaving hydrophobic and calcium-sensitive patches on the surface of the particles (Dalgleish, 1992; de Kruif, 1992).”
Background
Controlled gastrointestinal digestion of micellar casein loaded anthocyanins: The chelating and complexing effect of dextran sulfate
Liao, M.-H., Chen, F., Hu, X.-S., Liao, X., Miao, S., Ma, L.-J., & Ji, J.-F. (2022) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2022.107863 · Cited by 20
Thermostable trypsin‐like protease by Penicillium roqueforti secreted in cocoa shell fermentation: Production optimization, characterization, and application in milk clotting
Nogueira, L. S., Tavares, I. M. D. C., Santana, N. B., Ferrão, S. P. B., Teixeira, J. M., Costa, F. S., Silva, T. P., Pereira, H. J. V., Irfan, M. I., Bilal, M., et al. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2268 · Cited by 25
Interactive effects of casein micelle size and calcium and citrate content on rennet‐induced coagulation in bovine milk
Priyashantha, H., Lundh, Å. S., Höjer, A., Hetta, M., Johansson, M., & Langton, M. (2019) · Journal of Texture Studies · doi:10.1111/jtxs.12454 · Cited by 27
Heat Stability of Milk
Huppertz, T. (2016) · Springer eBooks · doi:10.1007/978-1-4939-2800-2_7 · Cited by 20
The effect of calcium addition on the rheological properties of a soft cheese at various stages of manufacture
SOLORZA, F. J., & Bell, A. E. (1998) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.1998.tb02634.x · Cited by 19
Proteolysis of ovine caseins by cardosin A, an aspartic acid proteinase from Cynara cardunculus L.
Silva, S. V., & Malcata, F. X. (1998) · Le Lait · doi:10.1051/lait:1998548 · Cited by 16
Effect of thermal treatment on serum protein reduced micellar casein concentrate: An evaluation of rennet coagulability, cheese composition and yield
Xia, X., Tobin, J., Subhir, S., Fenelon, M., McSweeney, P., & Sheehan, J. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104902 · Cited by 18
Improving rennet coagulation and cheesemaking properties of reverse osmosis skim milk concentrates by pH adjustment
Dussault-Chouinard, I., Britten, M., & Pouliot, Y. (2019) · International Dairy Journal · doi:10.1016/j.idairyj.2019.03.008 · Cited by 18
Rennet coagulation properties of milk in the presence of MFGM fragments isolated from raw – and pasteurised-cream buttermilk
Gauvin, M., Pouliot, Y., & Britten, M. (2018) · International Dairy Journal · doi:10.1016/j.idairyj.2018.06.006 · Cited by 18
Influence of ethanol on the rennet-induced coagulation of milk.
O'Connell, J., Saracino, P., Huppertz, T., Uniake, T., de Kruif, C. D., Kelly, A., & Fox, P. (2006) · Journal of Dairy Research · doi:10.1017/s0022029906001737 · Cited by 18
Impacts of feeding system and season on milk composition and Cheddar cheese yield in a subtropical environment
Amenu, B., Cowan, T., Deeth, H., & Moss, R. (2006) · doi:10.1071/ea04068 · Cited by 18
“In particular, there was no significant difference in the percentages of κ-casein, the casein that has a major influence on micelle stability (Dalgleish 1993) and hence cheesemaking.”
Background
Cheese | Rennet-Induced Coagulation of Milk
Gregersen, V., & Lucey, J. (2011) · Elsevier eBooks · doi:10.1016/b978-0-08-100596-5.00684-3 · Cited by 18
Plant-derived rennet: research progress, novel strategies for their isolation, identification, mechanism, bioactive peptide generation, and application in cheese manufacturing
Zhang, X., Tao, L., Wei, G., Yang, M., Wang, Z., Shi, C., Shi, Y., & Huang, A. (2023) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2023.2275295 · Cited by 17
“Similarly, for most different types of cheese, bitterness is usually not acceptable to consumers, and it is worth noting that some types of cheeses, such as some aged cheese, are produced with a certain degree of bitterness as part of the characteristic flavor of the cheese (Fox et al. 2017).”
Designing Protein Gels for Nutrient Delivery: From Formulation to Digestion
Dong, X., Wang, Y., Chen, X. D., & Selomulya, C. (2026) · Comprehensive Reviews in Food Science and Food Safety · doi:10.1111/1541-4337.70424 · Cited by 17
“Enzyme-mediated gelation utilizes a range of enzymes such as transglutaminase (TG), rennet and protease, which can cleave peptide bonds in protein chains, driving the formation of cross-links to stabilize the gel network (Corredig and Salvatore 2016 ; G. Chen, Hu, et al. 2023 ).”
Enzymatic proteolysis during the conversion of milk into cheese
Lepilkina, О. V., & Grigorieva, A. (2023) · Food systems · doi:10.21323/2618-9771-2023-6-1-36-45 · Cited by 17
“Агрегиро - вание мицелл происходит, когда около 97% κ -казеина в ми - целле гидролизовалось [54].”
Chemical interactions among caseins during rennet coagulation of milk.
Amaro-Hernández, J. C., Olivas, G. I., Acosta-Muñiz, C., Gutiérrez-Méndez, N., Rios-Velasco, C., & Sepúlveda, D. R. (2021) · Journal of Dairy Science · doi:10.3168/jds.2021-21071 · Cited by 16
“External factors such as pH and temperature play an important role in determining the establishment of the various types of chemical bonds among caseins during this period (Corredig and Salvatore, 2016; Mehta, 2018).”
Background
Influence of Chymosin on Physicochemical and Hydrolysis Characteristics of Casein Micelles and Individual Caseins
Chen, C.-C., Chen, L.-Y., Li, W.-T., Chang, K.-L., Kuo, M.-I., Chen, C.-J., & Hsieh, J.-F. (2021) · Nanomaterials · doi:10.3390/nano11102594 · Cited by 16
Effect of storage time and temperature of milk protein concentrate (MPC85) on the renneting properties of skim milk fortified with MPC85
Hunter, R. J., Hemar, Y., Pinder, D., & Anema, S. (2011) · doi:10.1016/j.foodchem.2010.09.086 · Cited by 16
Enzymatic Coagulation of Milk
Fox, P., Guinee, T., Cogan, T., & McSweeney, P. (2017) · Springer eBooks · doi:10.1007/978-1-4899-7681-9_7 · Cited by 16
Production of phosphorylated and functional αs1-casein in Escherichia coli.
Balasubramanian, S., Mobasseri, G., Shi, L., Jers, C., Køhler, J. B., Boire, A., Berton-Carabin, C., Mijakovic, I., & Jensen, P. R. (2025) · Trends in Biotechnology · doi:10.1016/j.tibtech.2025.05.015 · Cited by 15
Effects of ultrafiltration followed by heat or high-pressure treatment on camel and bovine milk cheeses
Mbye, M., Ayyash, M. M., Mohamed, H., Abu-Jdayil, B., Kamleh, R., & Kamal-Eldin, A. (2023) · NFS Journal · doi:10.1016/j.nfs.2023.04.004 · Cited by 15
Improving quark-type cheese yield and quality by treating semi-skimmed cow milk with microbial transglutaminase
Cadavid, A. M., Bohigas, L., Toldrà, M., Carretero, C., Parés, D., & Saguer, E. (2020) · LWT · doi:10.1016/j.lwt.2020.109756 · Cited by 20
An Overview of the Cheesemaking Process
Bintsis, T., & Papademas, P. (2017) · doi:10.1002/9781119046165.ch0f · Cited by 15
Sodium caseinate-stabilized fat globules inhibition of the rennet-induced gelation of casein micelles studied by Diffusing Wave Spectroscopy
Gaygadzhiev, Z., Alexander, M., & Corredig, M. (2009) · doi:10.1016/j.foodhyd.2008.07.019 · Cited by 15
Quantification of κ-casein in milk by an optical immunosensor
Muller-Renaud, S., Dupont, D., & Dulieu, P. (2003) · doi:10.1080/09540100400013401 · Cited by 15
“The milk coagulation is conveniently considered as a three step process: an enzymatic phase with proteolysis of k-CN, followed by a secondary phase during which the destabilized micelles begin to aggregate and a third phase that involves changes in the coagulum structure (Hyslop, 2003).”
Background
Chapter 6 – Casein Micelle Structure and Stability
Horne, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405171-3.00006-4 · Cited by 15
Dairy Products
Hill, A. R., & Kethireddipalli, P. (2012) · Elsevier eBooks · doi:10.1016/b978-0-08-091809-9.00008-x · Cited by 18
Effects of β- and κ-casein, and β-lactoglobulin single and composite genotypes on milk composition and milk coagulation properties of Italian Holsteins assessed by FT-MIR
Cendron, F., Franzoi, M., Penasa, M., Marchi, M. D., & Cassandro, M. (2021) · Italian Journal of Animal Science · doi:10.1080/1828051x.2021.2011442 · Cited by 14
“To the authors’ knowledge, this is the first time j-CN protein variants are associated with changes in milk urea content. SCS in the analysed individuals was lower for j-CN BB genotype compared to AA. Previously, Vallas et al. (2012) did not find a significant association between SCS and b-j-CN composite genotype. A s…”
ResultInfluential
HHP Influence on Food Quality and Bioactive Compounds: A Review of the Last Decade
Salazar, F. A., Yildiz, S., Leyva, D., Soto-Caballero, M., Welti-Chanes, J., Anubhav, P., Lavilla, M., & Escobedo-Avellaneda, Z. (2021) · doi:10.1016/b978-0-08-100596-5.22984-3 · Cited by 14
Innovative approaches for enzyme immobilization in milk processing: advancements and industrial applications
Khan, M. U., Farid, A., Liu, S., Zhen, L.-M., Alahmad, K., Chen, Z.-W., & Kong, L. (2025) · Critical reviews in food science and nutrition · doi:10.1080/10408398.2025.2450528 · Cited by 13
“However, the dairy industry is increasingly adopting plant-based and microbial coagulants to reduce dependence on animal-derived rennet (Fox, Cogan, and Guinee 2017).”
Algerian cardoon flowers express a large spectrum of coagulant enzymes with potential applications in cheesemaking
Zikiou, A., Esteves, A. C., Esteves, E., Rosa, N. D. N., Gomes, S., Martins, A. P. L., Zidoune, M. N., & Barros, M. (2020) · International Dairy Journal · doi:10.1016/j.idairyj.2020.104689 · Cited by 15
Light Scattering Studies of Colloid Stability and Gelation
Horne, D. (1995) · doi:10.1007/978-1-4615-2145-7_11 · Cited by 13
Microstructure and texture of khoa and gulabjamun made from cows' milk: Heat-induced changes during processing and frying
Adhikari, A. (1993) · doi:10.1002/jsfa.2740610103 · Cited by 13
Genetic parameters for noncoagulating milk, milk coagulation properties, and detailed milk composition in Swedish Red Dairy Cattle.
Duchemin, S., Nilsson, K., Fikse, W., Stålhammar, H., Johansen, L. B., Hansen, M., Lindmark-Månsson, H., de Koning, D., Paulsson, M., & Glantz, M. (2020) · Journal of Dairy Science · doi:10.3168/jds.2020-18315 · Cited by 12
Ultrasonographic imaging of abomasal milk clotting and abomasal diameter in healthy and diarrheic calves.
Kirchner, D., Schwedhelm, L., Wenge, J., Steinhöfel, I., Heinrich, C., Coenen, M., & Bachmann, L. (2015) · Animal science journal = Nihon chikusan Gakkaiho · doi:10.1111/asj.12382 · Cited by 12
Impact of Dietary Fiber (Inulin and Resistant Starch) on the Quality Parameters of Low Fat Cheddar Cheese from Buffalo Milk
Murtaza, M. (2022) · Pakistan Journal of Zoology · doi:10.17582/journal.pjz/20200630120620 · Cited by 12
“Combination of sensory elements resulting from physical properties professed by sense of light and touch is defined as the texture (Fox et al., 2000).”
Background
Cloning of a marsupial k-casein cDNA from the brushtail possum (Trichosurus vulpecula)
Stasiuk, S., Summers, E., & Demmer, J. (2000) · doi:10.1071/rd99036 · Cited by 12
Comparative study among rheological, near-infrared light backscattering and confocal microscopy methodologies in enzymatic milk coagulation: Impact of different enzyme and protein concentrations
Leite, B. R. D. C., Tribst, A. A. L., & Cristianini, M. (2017) · Food Hydrocolloids · doi:10.1016/j.foodhyd.2016.07.035 · Cited by 11
Novel applications of enzymes in the dairy sector: optimizing functional properties of milk proteins by enzymatic cross-linking.
Huppertz, T. (2009) · Elsevier eBooks · doi:10.1533/9781845697198.3.394 · Cited by 11
Biochemical Properties of a Promising Milk-Clotting Enzyme, Moose (Alces alces) Recombinant Chymosin
Balabova, D., Belash, E. A., Belenkaya, S., Shcherbakov, D., Belov, A., Koval, A. D., Mironova, A., Bondar, A., Volosnikova, E., Arkhipov, S., et al. (2023) · Foods · doi:10.3390/foods12203772 · Cited by 10
“Genetically engineered cow and camel Chns are a high-quality alternative to rennet and currently are widely represented in the market of industrial milk coagulants [11].”
Background
Correlation between the chemical, microbiological and sensory characteristics of cream cheese using a mixed and single probiotic culture
Tologana, R. D., Wikandari, R., Rahayu, E., Suroto, D., & Utami, T. (2022) · Journal of food science and technology · doi:10.1007/s13197-022-05603-0 · Cited by 10
“The milk starts to coagulate at pH 5.3–5.5 (Corredig and Salvatore 2016).”
BackgroundInfluential
Chapter 17 – Milk Protein Gels
Lucey, J. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-405171-3.00017-9 · Cited by 10
Production, characterization, and application of a new chymotrypsin-like protease from Pycnoporus sanguineus
Ferreira, A. N., da Silva, A. T., Nascimento, J., de Souza, C. B., Silva, M. D. C., Grillo, L. A. M., da Luz, J. M. R., & Pereira, H. J. V. (2023) · Biocatalysis and Biotransformation · doi:10.1080/10242422.2023.2196362 · Cited by 9
“Therefore, the addition of Ca 2 þ accelerates the coagulation of milk (Lucey 2011; Corredig and Salvatore 2016; Britten and Giroux 2022).”
Background
Application of Recombined Milk to Produce Crescenza-Type Cheese in Laboratory-Scale Cheesemaking: Implications on Technology and Sensory Properties
Tidona, F., Francolino, S., Ghiglietti, R., Locci, F., Brusa, G., Alinovi, M., Mucchetti, G., & Giraffa, G. (2020) · Foods · doi:10.3390/foods9070928 · Cited by 9
“05 g/L, which is one of the known causes of cheese bitterness [27,28], were not necessary in our trials.”
Background
The Basis of Structure in Dairy-Based Foods: Casein Micelles and their Properties
Dalgleish, D. (2014) · Elsevier eBooks · doi:10.1016/b978-0-12-404610-8.00003-7 · Cited by 9
Self-citation
Overview: cheese chemistry and rheology.
Holsinger, V., Smith, P., & Tunick, M. (1995) · Advances in Experimental Medicine and Biology · doi:10.1007/978-1-4615-1913-3_1 · Cited by 9
Machine Learning in Cheese-Making: Methods, Applications, and the Future
Pardo, D., Castillo, M., Mülâyim, M. O., & Cerquides, J. (2025) · Food Engineering Reviews · doi:10.1007/s12393-025-09420-x · Cited by 11
“It is determined by the type of cheese, the properties and characteristics of the milk, and the acidiﬁcation process, although in general, it lasts between 40 and 60 minutes for most cheeses [44].”
Casein micelles partially hydrolyzed by chymosin to modify the texture of lowfat ice cream
Chang, J., Marshall, R. T., & Heymann, H. (1995) · doi:10.3168/jds.s0022-0302(95)76890-4 · Cited by 8
22 – Microstructural approaches to the study and improvement of cheese and yogurt products
Lucey, J. (2007) · Elsevier eBooks · doi:10.1533/9781845693671.4.600 · Cited by 8
Effects of animal rennet, fermentation-produced chymosin, and microbial coagulants on bovine milk coagulation properties
Stocco, G., Casali, D., Summer, A., Mariani, E., Concar, E., Lantz, S. E., Goodwins, J., & Cipolat‐Gotet, C. (2025) · Journal of Dairy Science · doi:10.3168/jds.2024-26167 · Cited by 8
“The literature shows that curd firming is largely influenced by the type of rennet used: Bovine TR increases gel strength more rapidly than R. miehei because of the differences in the extent or specificity, or both, of proteolysis during the enzymatic phase of rennet coagulation (Fox et al., 2017).”
Influential
Effect of konjac glucomannan and soy soluble polysaccharides on the rheological, microstructural and syneretic properties of rennet gels
Ouyang, H., Kilcawley, K., Miao, S., Fenelon, M., Kelly, A., & Sheehan, J. (2022) · LWT · doi:10.1016/j.lwt.2022.113905 · Cited by 7
Effect of buffalo milk on the yield and composition of buffalo feta cheese at various processing parameters
Shakerian, M., Kiani, H., & Ehsani, M. (2016) · doi:10.1016/j.fbio.2016.06.002 · Cited by 7
NIR and other Luminometric Methods to Monitor the Primary Clotting Phase of Milk
Giangiacomo, R., Lizzano, R., Barzaghi, S., Cattaneo, T., & Barros, A. S. (1998) · doi:10.1255/jnirs.138 · Cited by 7
Effect of Ferric Chloride on Chymosin Hydrolysis and Rennet Clotting Time of Milk
Reddy, I. M., & Mahoney, A. (1992) · doi:10.3168/jds.s0022-0302(92)78026-6 · Cited by 7
Effect of Different Rennet Type on Physico-Chemical Properties and Bitterness in White Cheese
Ozcan, T., & Eren-Vapur, U. (2013) · International Journal of Environmental Science and Development · doi:10.7763/ijesd.2013.v4.307 · Cited by 7
“It causes the coagulation of milk by cleaving the Phe105-Met106 bond of k-casein [7], [8].”
Background
Different protein sources in concentrate feed for dairy cows affect cheese-making properties and yield
Olsen, M. A., Ferneborg, S., Vhile, S. G., Kidane, A., & Skeie, S. B. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22662 · Cited by 7
Sodium caseinate hinders chymosin-induced aggregation of caseins in concentrated milk: The role of soluble caseins and calcium ions
Nair, P., & Corredig, M. (2021) · JDS Communications · doi:10.3168/jdsc.2021-0124 · Cited by 6
“In skim milk, when more than 90% of κ-casein is hydrolyzed (Dalgleish, 1992), the micelles aggregate if sufficient calcium ions are present (Lucey, 2009).”
Background
Inhibition of the proteolytic activity of indigenous plasmin or exogenous chymosin and pepsin in bovine milk by blood serum
Huppertz, T., Uniacke, T., Kelly, A., & Fox, P. (2006) · doi:10.1016/j.idairyj.2005.10.022 · Cited by 6
Chapter VI Caseins
de Kruif, C. G. (2003) · Progress in biotechnology · doi:10.1016/s0921-0423(03)80006-0 · Cited by 10
Milk and dairy products
ICMSF (1998) · Springer eBooks · doi:10.1007/978-1-4615-5307-6_16 · Cited by 14
Cold ultrafiltered or microfiltered milk retentates: A systematic comparison of the effects of compositional differences on their gelation functionality.
Coşkun, Ö., Wiking, L., & Corredig, M. (2023) · Journal of Dairy Science · doi:10.3168/jds.2022-22497 · Cited by 5
Biochemical and technological properties of moose (Alces alces) recombinant chymosin
Balabova, D., Rudometov, A. P., Belen'kaya, S. V., Belov, A., Koval, A. D., Bondar, A., Bakulina, A., Rukhlova, E. A., Elchaninov, V. V., & Shcherbakov, D. (2022) · Vavilovskii zhurnal genetiki i selektsii · doi:10.18699/vjgb-22-31 · Cited by 5
A novel approach for characterisation of stabilising bonds in milk protein deposit layers on microfiltration membranes
Weinberger, M., Andlinger, D. J., & Kulozik, U. (2021) · International Dairy Journal · doi:10.1016/j.idairyj.2021.105044 · Cited by 5
Comparison of Cheddar cheeses produced with recombinant chymosin and with calf rennet using two dimensional high-performance liquid chromatography
Lagerwerf, F. M., WASSENAAR, P. D. V., & Haverkamp, J. (1995) · Journal of Dairy Research · doi:10.1017/s0022029900031435 · Cited by 3
Characterization of two aspartyl proteinases from a commercial fungal (Mucor miehei) rennet
Smith, J. L., & Yada, R. (1991) · Canadian Institute of Food Science and Technology Journal · doi:10.1016/s0315-5463(91)70019-9 · Cited by 5
Role of Clay Substrate Molecular Interactions in Some Dairy Technology Applications
Azzouz, A., Aruș, V., & Platon, N. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25020808 · Cited by 4
“Milk coagulation can also be triggered by chemical processes such as acidification in the presence of acidic species and/or proteolysis using a milk-clotting enzyme (MCE) [32].”
Background
Industrial Biotechnology in the Food and Feed Sector
MONSAN, P. F., & O’Donohue, M. J. (2010) · Industrial Biotechnology · doi:10.1002/9783527630233.ch10 · Cited by 4
Cheese Manufacture as a Separation and Reaction Process
Morison, K. R. (1997) · Journal of Food Engineering · doi:10.1016/s0260-8774(97)00022-8 · Cited by 4
“The casein micelles start to aggregate when the reaction is about 85% complete (Dalgleish, 1982) and continue to aggregate over several minutes.”
BackgroundInfluential
Instrumental texture parameters and solvation characteristics of mixed casein gels
Konstance, R., Holsinger, V., & Thompson, M. P. (1995) · doi:10.3168/jds.s0022-0302(95)76690-5 · Cited by 4
Ultrasound in Dairy Processing
Silva, M., & Chandrapala, J. (2021) · doi:10.1016/b978-0-08-100596-5.22955-7 · Cited by 4
Characterization of a Milk-clotting Enzyme from Hericium erinaceum and Its Proteolytic Action on Bovine Caseins
Sato, K., Goto, K., Suzuki, A., Miura, T., Endo, M., Nakamura, K. T., & Tanimoto, M. (2018) · Food Science and Technology Research · doi:10.3136/fstr.24.669 · Cited by 7
Influence of different genetic polymorphisms of αS1- and κ-casein on Havarti-type cheese: Effects on cheese-making efficiency and cheese quality
Olsen, M. A., Ketto, I., Øyaas, J., Abdelghani, A., Myhrer, K. S., & Skeie, S. (2023) · International Dairy Journal · doi:10.1016/j.idairyj.2023.105736 · Cited by 3
A novel electrochemical assay for chymosin determination using a label-free peptide as a substrate.
Li, C.-P., Liu, F., Zheng, J., & Zhao, H. (2021) · Journal of Dairy Science · doi:10.3168/jds.2020-19282 · Cited by 3
“This enzyme specifically cleaves the Phe105-Met106 peptide bond of κ-casein and releases a hydrophilic glycomacropeptide from the C-terminus of the protein (Fox and McSweeney, 1998; Dalgleish, 1992).”
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“It is well known that heat treatment of milk results in the denaturation of the whey proteins and interaction between the denatured whey proteins and the k-casein at the micelle surface [12].”
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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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