The Enzymatic Coagulation of Milk

Dalgleish, D. G.

doi:10.1007/978-1-4615-2650-6_3

Cited by 232Proteins in Food SystemsMilk Quality and Mastitis in Dairy CowsEnzyme Production and Characterization

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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Rennet-altered CN micelles are susceptible to aggregation due to the reduction in steric and charge repulsion caused by the loss of the macropeptide from κ-CN.
“Rennet-altered CN micelles are susceptible to aggregation due to the reduction in steric and charge repulsion (between particles) caused by the loss of the macropeptide from κ-CN.”
From Invited review: perspectives on the basis of the rheology and texture properties of cheese. (2003) · cites this paper as Dalgleish, 1993

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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 · see citing works
“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 · see citing works
“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 43 · see citing works
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 · see citing works
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 · see citing works
Dairy enzymology
Stepaniak, L. (2004) · International Journal of Dairy Technology · doi:10.1111/j.1471-0307.2004.00144.x · Cited by 50 · see citing works
“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 34 · see citing works
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 · see citing works
“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 · see citing works
“…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 · see citing works
“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 · see citing works
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 · see citing works
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 · see citing works
“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 · see citing works
“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 › Agronomy and Crop Science › 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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