The DOI matches its Crossref record; 14 of the 14 references it cites were found in a registry or an index.
Heat stability of milk
Abstract
The heat stability of milk has been the subject of a considerable amount of research for about a century. This research has been aimed mainly at understanding the effects of compositional and processing factors on heat stability and elucidating the mechanisms of protein coagulation. This paper provides an overview of the factors that influence the pH dependence of the heat stability of normal and concentrated milks. The principal heat‐induced changes in the milk system that contribute to coagulation are discussed. Current knowledge of the mechanisms of heat coagulation in normal and concentrated milks is also reviewed.
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Citations
Cites
Structure and Stability of Bovine Casein Micelles
Holt, C. (1992) · Advances in Protein Chemistry · doi:10.1016/s0065-3233(08)60554-9 · Cited by 470
Anema, S. G., & Li, Y. (2003) · Journal of Dairy Research · doi:10.1017/s0022029902005903 · Cited by 341
Harper, W. J. (1996) · International Dairy Journal · doi:10.1016/0958-6946(95)00053-4 · Cited by 310
Heat-induced association of β-lactoglobulin and casein micelles
Smits, P., & Brouwershaven, J. H. V. (1980) · Journal of Dairy Research · doi:10.1017/s0022029900021208 · Cited by 166
Heat-Induced Coagulation of Milk
O’Connell, J. E., & Fox, P. F. (2003) · Advanced Dairy Chemistry—1 Proteins · doi:10.1007/978-1-4419-8602-3_25 · Cited by 163
Disulfide Bond Formation Between Thermally Denatured β-Lactoglobulin and κ-Casein in Casein Micelles
Jang, H. D., & Swaisgood, H. E. (1990) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(90)78746-2 · Cited by 142
Singh, H., & Fox, P. F. (1985) · Journal of Dairy Research · doi:10.1017/s0022029900024481 · Cited by 124
Self-citationζ-Potentials of casein micelles from reconstituted skim milk heated at 120 °C
Anema, S. G., & Klostermeyer, H. (1996) · International Dairy Journal · doi:10.1016/0958-6946(95)00070-4 · Cited by 105
Heat-Induced Changes in Milk Preceding Coagulation
Fox, P. F. (1981) · Journal of Dairy Science · doi:10.3168/jds.s0022-0302(81)82819-6 · Cited by 104
Singh, H., & Fox, P. F. (1987) · Journal of Dairy Research · doi:10.1017/s0022029900025711 · Cited by 91
Self-citation
Cited by
The Chemistry of Protein Oxidation in Food
Hellwig, M. (2019) · Angewandte Chemie International Edition · doi:10.1002/anie.201814144 · Cited by 259
van Lieshout, G. A. A., Lambers, T. T., Bragt, M. C. E., & Hettinga, K. A. (2020) · Critical Reviews in Food Science and Nutrition · doi:10.1080/10408398.2019.1646703 · Cited by 254
“Phosphorylation has generally been considered to be sensitive to heat (Singh 2004) although limited studies determined the impact of milk protein dephosphorylation on digestion.”
Background
Metadata
- Authors
- Singh, H.
- Venue
- International Journal of Dairy Technology
- Publisher
- Wiley
- Published
- 2004-04-26
- Volume
- 57
- Issue
- 2-3
- Pages
- 111-119
- ISSN
- 1364-727X (ISSN-L)
- 1471-0307
- OpenAlex
- W1973921376
- Cited by
- 302
- References
- 14
- FWCI
- 8.20
- Type
- journal article
- Language
- en
- Open access
- closed
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Data sources
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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.
