The effect of heat treatment on the nutritional and antioxidant content of different milk types

Abstract

Heat treatments may cause some chemical and physicochemical changes in milk, although milk is a heat-stable system. Heat treatments can cause different changes in different types of milk. This study aimed to compare the effects of pasteurization and boiling on goat and cow milk's macromolecular contents, glutathione levels, and superoxide dismutase activities. The protein level of both types of milk decreased with the pasteurization process, and boiling also reduced the protein level of goat milk. Both heat treatments reduced superoxide dismutase activity and glutathione levels in both types of milk. While the boiling process did not change the cow's milk lactose level, it increased the goat milk lactose level. It was determined that pasteurization reduced the lactose level in both types of milk. Pasteurization did not change the fat level in cow milk but decreased the fat level in goat milk. In conclusion, cow milk was less affected by these heat treatments, which can be attributed to having large fat globules, high lactose concentration, and high heat resistance protein content compared to goat milk.

Keywords

• Milk
• Boiling
• Pasteurization
• Antioxidants
• The Nutritional Content of Milk

References

1. Altun, D., Sarici, S. Ü. (2017). Keçi sütü: Bebek beslenmesinde ilk tercih mi olmali? Çocuk Sağlığı ve Hastalıkları Dergisi, 60(1), 22–33.
2. Barlowska, J., Szwajkowska, M., Litwińczuk, Z., Król, J. (2011). Nutritional value and technological suitability of milk from various animal species used for dairy production. Comprehensive Reviews in Food Science and Food Safety, 10(6), 291–302. https://doi.org/10.1111/j.1541-4337.2011.00163.x
3. Beutler, E. (1975). Glutathione in Red Cell Metabolism : A manual of Biochemical methods. In J. Lab. Clin. Med.
4. Bradford, M. M. (1976). A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Analytical Biochemistry, 72, 248–254. https://doi.org/10.1016/0003-2697(76)90527-3
5. Coghill, D. M., Mutzelburg, I. D., Birch, S. J. (1982). Effect of thermalization on the bacteriological and chemical quality of milk. Australian Journal of Dairy Technology, 37(2), 48–50.
6. Condas, L.A.Z., Ribeiro, M.G., Gonoi, T., Matsuzawa, T., Yazawa, K., Motta, R.G., Franco, M.M.J., Listoni, F.J.P. (2012). Molecular identification and thermoresistance to boiling of Nocardia farcinica and Nocardia cyriacigeorgica from bovine bulk tank milk. Brazilian Journal of Microbiology, 1038–1041. https://doi.org/10.1590/S1517-83822012000300029
7. Deeth, H. C., Lewis, M.J. (2017). Heat treatments of milk - thermisation and pasteurisation. High Temperature Processing of Milk and Milk Products, 15–39. https://doi.org/10.1002/9781118460467.ch2
8. Farrell, H.M., Jimenez-Flores, R., Bleck, G.T., Brown, E.M., Butler, J.E., Creamer, L.K., Hicks, C.L., Hollar, C.M., Ng-Kwai-Hang, K.F., Swaisgood, H.E. (2004). Nomenclature of the proteins of cows’ milk - Sixth revision. Journal of Dairy Science, 87(6), 1641–1674. https://doi.org/10.3168/jds.S0022-0302(04)73319-6

9. Folz, R., Crapo, J. (1994). Extracellular superoxide dismutase (SOD3): tissue-specific expression, genomic characterization, and computer-assisted sequence analysis of the human EC SOD gene. Genomics, 22, 162–171. https://doi.org/10.1006/geno.1994.1357
10. García-Lara, N.R., Escuder-Vieco, D., García-Algar, O., De La Cruz, J., Lora, D., Pallás-Alonso, C. (2012). Effect of freezing time on macronutrients and energy content of breastmilk. Breastfeeding Medicine, 7(4), 295–301. https://doi.org/10.1089/bfm.2011.0079
11. Granelli, K., Björck, L., Appelqvist, L. (1995). The variation of superoxide dismutase (SOD) and xanthine oxidase (XO) activities in milk using an improved method to quantitate SOD activity. Journal of the Science of Food and Agriculture, 67(1), 85–91. https://doi.org/10.1002/jsfa.2740670114
12. Hicks, C.L., Bucy, J., Stofer, W. (1979). Heat Inactivation of Superoxide Dismutase in Bovine Milk. Journal of Dairy Science, 62(4), 529–532. https://doi.org/10.3168/jds.S0022-0302(79)83285-3
13. Humbert, E. S., Campbell, J. N., Blankenagel, G., Gebre-Egziabher, A. (1985). Extended storage of raw milk. II. The role of thermization. Canadian Institute of Food Science and Technology Journal, 18(4), 302–305. https://doi.org/10.1016/S0315-5463(85)71962-1
14. Jenness, R. (1980). Composition and characteristics of goat milk: review 1968−1979. Journal of Dairy Science, 63(10), 1605–1630. https://doi.org/10.3168/jds.S0022-0302(80)83125-0
15. Joishy, T.K., Dehingia, M., Khan, M.R. (2019). Bacterial diversity and metabolite profiles of curd prepared by natural fermentation of raw milk and back sloping of boiled milk. World Journal of Microbiology and Biotechnology, 35(7). https://doi.org/10.1007/s11274-019-2677-y
16. Kamal, A.M., Salama, O.A., El-Saied, K.M. (2007). Changes in amino acids profile of camel milk protein during the early lactation. In International Journal of Dairy Science, 2(3), 226–234. https://doi.org/10.3923/ijds.2007.226.234
17. Khan, I.T., Nadeem, M., Imran, M., Ayaz, M., Ajmal, M., Ellahi, M.Y., Khalique, A. (2017). Antioxidant capacity and fatty acids characterization of heat treated cow and buffalo milk. Lipids in Health and Disease, 16(1), 1–10.
18. Khan, I.T., Nadeem, M., Imran, M., Ullah, R., Ajmal, M., Jaspal, M.H. (2019). Antioxidant properties of milk and dairy products: A comprehensive review of the current knowledge. Lipids in Health and Disease, 18(41), 1–13. https://doi.org/10.1186/s12944-019-0969-8
19. Khramov, V.A., Kolomeǐtseva, A.S., Papichev, N.V. (2008). Jaffe color test-based microtechnique for determination of milk lactose. Gigiena i Sanitariia, 3, 86–87.
20. Kilango, K., Makita, K., Kurwijila, L., Grace, D. (2012). Boiled milk, food safety and the risk of exposure to milk borne pathogens in informal dairy markets in Tanzania.
21. Kliem, K.E., Shingfield, K.J., Livingstone, K.M., Givens, D.I. (2013). Seasonal variation in the fatty acid composition of milk available at retail in the United Kingdom and implications for dietary intake. Food Chemistry, 141(1), 274–281. https://doi.org/10.1016/j.foodchem.2013.02.116
22. Korycka-Dahl, M., Richardson, T., Hicks, C.L. (1979). Superoxide dismutase activity in bovine milk serum. Journal of Food Protection, 42(11), 867–871.
23. Lamberti, C., Baro, C., Giribaldi, M., Napolitano, L., Cavallarin, L., Giuffrida, M.G. (2017). Effects of two different domestic boiling practices on the allergenicity of cow milk proteins. Journal of the Science of Food and Agriculture, 98(6), 2370–2377. https://doi.org/10.1002/jsfa.8728
24. László, N., Lányi, K., Laczay, P. (2017). LC-MS study of the heat degradation of veterinary antibiotics in raw milk after boiling. Food Chemistry, 267, 178–186. https://doi.org/10.1016/j.foodchem.2017.11.041
25. Li, Y., Chen, D., Li, J., Zhang, X.X., Wang, C.F., Wang, J.M. (2018). Changes in superoxide dismutase activity postpartum from Laoshan goat milk and factors influencing its stability during processing. Italian Journal of Animal Science, 17(4), 835–844. https://doi.org/10.1080/1828051X.2018.1448306
26. Lucas, A., Gibbs, J., Lyster, R., Baum, J. (1978). Creamatocrit: simple clinical technique for estimating fat concentration and energy value of human milk. British Medical Journal, 1018–1020. https://doi.org/10.1136/bmj.1.6119.1018
27. Martysiak-Żurowska, D., Puta, M., Kiełbratowska, B. (2019). The effect of convective heating and microwave heating on antioxidant enzymes in pooled mature human milk. International Dairy Journal, 91, 41–47. https://doi.org/10.1016/j.idairyj.2018.12.008
28. Medhammar, E., Wijesinha-Bettoni, R., Stadlmayr, B., Nilsson, E., Charrondiere, U.R., Burlingame, B. (2012). Composition of milk from minor dairy animals and buffalo breeds: A biodiversity perspective. Journal of the Science of Food and Agriculture, 92(3), 445–474. https://doi.org/10.1002/jsfa.4690
29. Montilla, A., Calvo, M.M. (1997). Goat ’ s milk stability during heat treatment: Effect of pH and Phosphates. 1978. https://doi.org/10.1021/jf960667y
30. Mylroie, A.A., Collins, H., Umbles, C., Kyle, J. (1986). Erythrocyte superoxide dismutase activity and other parameters of copper status in rats ingesting lead acetate. Toxicology and Applied Pharmacology, 82, 512–520. https://doi.org/10.1016/0041-008X(86)90286-3
31. Öner, Z., Sanlıdere-Aloglu, H., Dedebaş, T. (2011). Determination of antioxidant capacity in milk from various animals and humans. Milchwissenschaft-Milk Science International, 66(2), 133–135.
32. Park, Y.W., Haenlein, G.F.W. (2016). Goat milk, its products and nutrition. Handbook of Food Products Manufacturing, 69, 449–488. https://doi.org/10.1002/9780470113554.ch69
33. Pocius, P.A., Clark, J.H., Baumrucker, C.R. (1981). glutathione in bovine blood: Possible source of amino acids for milk protein synthesis. Journal of Dairy Science, 64(7), 1551–1554. https://doi.org/10.3168/jds.S0022-0302(81)82724-5
34. Posati, L.P., Orr, M.L. (1976). Composition of food. dairy and egg products, raw-processed-prepared. In Agricultural Handbook.
35. Rachman, A. B., Maheswari, R. R. A., Bachroem, M. S. (2015). Composition and isolation of lactoferrin from colostrum and milk of various goat breeds. Procedia Food Science, 3, 200–210. https://doi.org/10.1016/j.profoo.2015.01.022
36. Stojanovska, S., Gruevska, N., Tomovska, J., Tasevska, J., Krstanovski, A., Menkovska, M. (2017). Maillard reaction and lactose structural changes during milk processing. Chemistry Research Journal, 2(6), 139–145. Talukder, S., Kerrisk, K.L., Gabai, G., Fukutomi, A., Celi, P. (2015). Changes in milk oxidative stress biomarkers in lactating dairy cows with ovulatory and an-ovulatory oestrous cycles. Animal Reproduction Science, 158, 86–95. https://doi.org/10.1016/j.anireprosci.2015.05.004
37. Villamiel, M., De Jong, P. (2000). Influence of high-intensity ultrasound and heat treatment in continuous flow on fat, proteins, and native enzymes of milk. Journal of Agricultural and Food Chemistry, 48(2), 472–478. https://doi.org/10.1021/jf990181s
38. Wang, F., Zhang, Y.Q. (2015). Bioconjugation of Silk Fibroin Nanoparticles with Enzyme and Peptide and Their Characterization. In Advances in Protein Chemistry and Structural Biology (1st ed., Vol. 98). Elsevier Inc. https://doi.org/10.1016/bs.apcsb.2014.11.005