Milk curd self-segmentation in cheesemaking tank
https://doi.org/10.21323/2618-9771-2022-5-2-94-99
Abstract
The purpose of this work is to describe and study the previously unknown phenomenon of self-segmentation of a milk curd in an open-type cheesemaking tank. Based on the analysis of the kinetics of gel formation, it has been determined that self-segmentation of the gel begins near the gel point, develops over several tens of seconds, and becomes stable as the gel condenses. The segments in the milk curd do not have a definite regular shape; their average size varies from 5 to 50 cm. The shape and size of the segments do not repeat and do not correlate with the type of cheese being produced. The displacement of the segments of the milk curd in the cheesemaking tank relative to each other in height is from 0.5 to 2 mm. The width of the boundary layer between the curd segments increases during the secondary phase of gelation from 3 to 10 mm. As a result of experimental studies, it has been shown that self-segmentation of milk gel is caused by thermogravitational convection, which forms Benard convection cells. A description of a possible mechanism of milk gel self-segmentation in open-type cheesemaking tanks is proposed. The effective role of fat globules in the mechanism of self-segmentation of the milk curd has been noted. It has been suggested that self-segmentation of the milk curd in the cheesemaking tank may cause some organoleptic defects in the finished cheese, in particular inhomogeneity of texture and color.
About the Author
I. T. Smykov
All-Russian Scientific Research Institute of Butter- and Cheesemaking
Russian Federation
Russian Federation
Igor T. Smykov, Doctor of Technical Sciences, Chief Researcher, Department of Physical Chemisry
19, Krasnoarmeysky Boulevard, Uglich, 152613, Yaroslavl Region
References
1. Lucey, J. A. (2020). Milk protein gels. Chapter in a book: Milk proteins: From expression to food. Oxford: Academic Press. https://doi.org/10.1016/B978–0–12–815251–5.00016–5
2. Fox, P. F., Guinee, T. P., Cogan, T. M., McSweeney P. L. H. (2017). Fundamentals of cheese science. Springer, New York, 2017.
3. Dalgleish, D. G. (1993). The enzymatic coagulation of milk. Chapter in a book: Fox, P. F., (Ed.), Cheese: Chemistry, Physics and Microbiology, Vol 1, (2nd edn. pp. 69–100) Chapman & Hall, London. https://doi.org/10.1007/978–1–4615–2650–6_3
4. Hyslop, D. B. (2003). Enzymatic coagulation of milk. Chapter in a book: Fox, P. F., McSweeney, P. L. H. (Eds.), Advanced Dairy Chemistry, Vol. 1, Part B, Proteins, (3rd edn., pp. 839–878). Kluwer Academic — Plenum Publishers, New York. https://doi.org/10.1007/978–1–4419–8602–3_24
5. Fox, P F, Guinee, T P. (2013). Cheese science and technology. Chapter in a book: Y. W. Park., G. F. W. Haenlein (Eds). Milk and dairy products in human nutrition: Production, Composition and Health. Wiley Blackwell, Oxford. https://doi.org/10.1002/9781118534168.ch17
6. Smykov, I. T. (2015). Kinetics of milk gelation. Part I. Coagulation mechanism. Chapter in a book: Rheology: Principles, Applications and Environmental Impacts. New York, NY: Nova Science Publications, 2015.
7. Arai, M., Kuwajima, K. (2000). Role of the molten globule state in protein folding. Advanced Protein Chemistry, 53, 209–282. https://doi.org/10.1016/s0065–3233(00)53005–8
8. Surkov, B. A., Klimovskii, I. I., Krayushkin, V. A. (1982). Turbidimetric study of kinetics and mechanism of milk clotting by rennet. Milchwissenschaft, 37, 393–395.
9. Farrel, Jr. H. M., Qi, P.X., Brown, E. M., Cooke, P. H., Tunick, M. H., Wickham, E. D. et al. (2002). Molten globule structures in milk proteins: Implications for potential new structure-function relationships. Journal of Dairy Science, 85(3), 459–471. https://doi.org/10.3168/jds.S0022–0302(02)74096–4
10. Green, M. L, Grandison, A. S. (1993). Secondary (non-enzymatic) phase of rennet coagulation and postcoagulation phenomena. Chapter in a book: Fox, P. F. (Ed.), Cheese: Chemistry, Physics and Microbiology, Vol. 1, General Aspects. (pp. 101–140) Elsevier Applied Science, New York. https://doi.org/10.1007/978–1–4615–2650–6_4
11. Tuszynski, W. B. (1971). A kinetic model of the clotting of casein by rennet. Journal of Dairy Research, 3, 115–125.
12. Witten, T. A. Meakin, P. (1983). Diffusion-limited aggregation at multiple growth sites. Physical Review A, 28(10), 5632–5642. https://doi.org/10.1103/PhysRevB.28.5632
13. De Kruif, C. G., Holt, C. (2003). Casein micelle structure, functions and interactions. Chapter in a book: Fox, P. F., McSweeney, P. L. H. (Eds.), Advanced Dairy Chemistry, Vol. 1, Part B, Proteins, (3rd edn., pp. 233–276). Kluwer Academic — Plenum Publishers, New York.
14. Drake, M. A., Delahunty, C. M. (2017). Sensory Character of Cheese and Its Evaluation. Chapter in a book: P. L. H. McSweeney, P. F. Fox, P. D. Cotter, D. W. Everett (Eds), Cheese. Chemistry, Physics and Microbiology, (2nd edn., pp. 517–545). Springer Nature Switzerland AG. https://doi.org/10.1016/b978–0–12–417012–4.00020-x
15. Biango-Daniels, M. N., Wolfe, B. E. (2021). American artisan cheese quality and spoilage: A survey of cheesemakers’ concerns and needs. Journal of Dairy Science, 104(5), 6283–6294. https://doi.org/10.3168/jds.2020– 19345
16. Tunick, M. (2016). Texture. Chapter in a book: The Oxford Companion to Cheese, C. W. Donnelly (Ed.), Oxford University Press pp. 708–709.
17. Muthukumarappan, K., Karunanithy, C. (2021). Texture. Chapter in a book: Handbook of Dairy Foods Analysis. F. Toldrá, L. M. L. Nollet (Eds.), (2nd ed.). CRC Press Boca Raton. https://doi.org/10.1201/9780429342967 1
18. Ong, L., Li, X., Ong, A., Gras, S. L. (2022). New Insights into Cheese Microstructure. Annual Review of Food Science, 13, 89–115. https://doi.org/10.1146/annurev-food 032519–051812
19. Danev, A., Bosakova-Ardenska, A., Boyanova, P., Panayotov, P., Kostadinova-Georgieva, L. (2019). Cheese quality evaluation by image segmentation. Proceedings of the 20th International Conference on Computer Systems and Technologies — CompSysTech’19. https://doi.org/10.1145/3345252.3345258
20. Hori, T. (1985). Objective measurements of the process of curd formation during rennet treatment of milks by the hot wire method. Journal of Food Science, 50(4), 911–917. https://doi.org/10.1111/j.1365–2621.1985.tb12978.x
21. Goncalves, B.J., Pereira, C. G, Lago, A. M. T., Goncalves, C. S., Giarola, T. M. O., Abreu, L. R. et al. (2017). Thermal conductivity as influenced by the temperature and apparent viscosity of dairy products. Journal of Dairy Science, 100(5), 3513–3525. https://doi.org/10.3168/jds.2016–12051
22. Miyawaki, O., Akalke, S., Yano, T., Ito, K., Saeki, Y. (1993). Shielded hotwire viscosity sensor on-line for a flowing system using a shield of high thermal conductivity. Bioscience, Biotechnology, and Biochemistry, 57, 1816–1819. https://doi.org/10.1271/bbb.57.1816
23. Smykov, I.T. (2018). Milk curd cutting time determination in cheesemaking. Food systems, 1(2), 12–20. https://doi.org/10.21323/2618–9771–2018–1–2–12–20 (In Russian)
24. Dennig, D., Bureick, J., Link, J., Diener, D., Hesse, C., Neumann, I. (2017). Comprehensive and highly accurate measurements of crane runways, profiles and fastenings. Sensors, 17(5), Article 1118. https://doi.org/10.3390/s17051118
25. Benard, H. (1901). Cell vortices in a liquid web. Optical methods of observation and recording. Journal of Physics: Theories and Applications, 10(1), 254–266. https://doi.org/10.1051/jphystap:0190100100025400 (In French)
Review
For citations:
Smykov I.T. Milk curd self-segmentation in cheesemaking tank. Food systems. 2022;5(2):94-99. https://doi.org/10.21323/2618-9771-2022-5-2-94-99
Views: 396
Email this article 