Non-Thermal Processing in Dairy: A Review on High Hydrostatic Pressure Effects on Milk Proteins
Authors
Dr. Ruchi Verma
Department of Food Processing and Technology, School of Vocational Studies and Applied Science, Gautam Buddha University, Greater Noida (U.P) (IN)
Ms. Munazza Aslam Khan
Department of Food Processing and Technology, School of Vocational Studies and Applied Science, Gautam Buddha University, Greater Noida (U.P) (IN)
Article Information
DOI: 10.51583/IJLTEMAS.2025.140500051
Subject Category: Food Processing and Technology
Volume/Issue: 14/5 | Page No: 484-494
Publication Timeline
Submitted: 2025-06-11
Published: 2025-06-11
Abstract
Abstract: High Hydrostatic Pressure (HHP) processing is a promising non-thermal food preservation technique that enhances microbial safety and shelf-life while maintaining the nutritional and sensory quality of products. In the dairy industry, HHP significantly influences the structure and functionality of milk proteins. The application of high pressure (typically 100–600 MPa) induces conformational changes, affecting protein solubility, denaturation, and aggregation. Caseins remain relatively stable under pressure, whereas whey proteins like β-lactoglobulin and α-lactalbumin undergo notable structural alterations, which can modify their functional and nutritional properties. These changes may lead to improved digestibility, emulsification, foaming, and even reduced allergenicity. HHP processing thus offers potential advantages in developing value-added and hypoallergenic dairy products. However, optimal pressure conditions must be carefully tailored to preserve desired qualities while minimizing negative impacts. This review explores the mechanisms and implications of HHP on milk proteins, highlighting its relevance in modern dairy processing.
Keywords
Milk Proteins, Casein, Whey Protein, Denaturation, Digestibility
This article is licensed under a Creative Commons Attribution 4.0 International License (CC BY 4.0).
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References
1. Anema, S. G. (2008). Effect of milk processing on protein interactions and functionality. International Dairy Journal, 18(7), 787–800. [Google Scholar] [Crossref]
2. Anema, S. G., & Li, Y. (2003). Effect of pH on the association of caseins in high-pressure-treated skim milk. International Dairy Journal, 13(8), 603–611. [Google Scholar] [Crossref]
3. Bahram, S., Rezaei, M., Soltani, M., & Kamali, A. (2014). Antimicrobial activity of whey protein-based edible films incorporated with oregano essential oil. Journal of Food Processing and Preservation, 38(3), 1095–1102. [Google Scholar] [Crossref]
4. Balasubramaniam, V. M., Martínez-Monteagudo, S. I., & Gupta, R. (2015). Principles and application of high pressure-based technologies in the food industry. Trends in Food Science & Technology, 45(1), 1-10. [Google Scholar] [Crossref]
5. Chaudhary, V., Kajla , P., Kumari, P., Bangar, S.P., Rusu, A., Trif Jose, M (2022). Milk protein-based active edible packaging for food applications: An eco-friendly approach. REVIEW article: Nutrition and Food Science Technology. [Google Scholar] [Crossref]
6. Chawla, R., Patil, G. R., & Singh, A. K. (2011). High hydrostatic pressure technology in dairy processing: A review. Journal of Food Science and Technology, 48(3), 260–268. [Google Scholar] [Crossref]
7. Chicón, R., Belloque, J., & López-Fandiño, R. (2008). The effect of high pressure on bovine lactoferrin: Influence on functional properties. International Dairy Journal, 18(5), 451–457. [Google Scholar] [Crossref]
8. Considine, K. M., Kelly, A. L., Fitzgerald, G. F., Hill, C., & Sleator, R. D. (2008). High-pressure processing – effects on microbial food safety and food quality. FEMS Microbiology Letters, 281(1), 1–9. [Google Scholar] [Crossref]
9. Corredig, M., Dalgleish, D. G., & Alexander, M. (2004). Structural changes of milk proteins induced by high pressure. Food Research International, 37(5), 595–601. [Google Scholar] [Crossref]
10. Dumay, E., Cheftel, J. C., & Poncet, C. (2013). High pressure processing of milk: Effects on casein micelle structure and functionality. Dairy Science & Technology, 93(5), 447–458. [Google Scholar] [Crossref]
11. Ejeahalaka, C. N., & On, N. (2020). Functional properties of milk protein concentrates in bakery and confectionery products. Journal of Food Science and Technology, 57(5), 1500–1507. [Google Scholar] [Crossref]
12. Farahnaky, H., Olatunde, A., Truong, O.O. (2022). Enhancing the Biological Activities of Food Protein-Derived Peptides Using Non-Thermal Technologies: A Review. Foods. 11, 18-23. [Google Scholar] [Crossref]
13. Food & Nutrition Research. (2023). Milk and dairy products – a scoping review for Nordic Nutrition Recommendations 2022. [Google Scholar] [Crossref]
14. Food and Agriculture Organization of the United Nations (FAO). (2024). Dairy Market Review. Overview of global market developments in 2024. [Google Scholar] [Crossref]
15. Fox, P. F., & Brodkorb, A. (2008). The casein micelle: Historical aspects, current concepts and significance. International Dairy Journal, 18(7), 677–684. [Google Scholar] [Crossref]
16. Fraj, N. D., et al. (2021). Casein micelles as nanocarriers for bioactive compounds. Journal of Dairy Science, 104(3), 2415–2425. [Google Scholar] [Crossref]
17. Franzoi, M., Jeong, H., Park, Y.-S., & Yoon, S.-S. (2019). Protein composition of bovine milk. Journal of Dairy Science, 102(10), 1–11. [Google Scholar] [Crossref]
18. Ganju, L., Salvi, V. P., & Saluja, D. (2009). Effect of high pressure on bovine immunoglobulin structure and function. Journal of Dairy Research, 76(3), 348–355. [Google Scholar] [Crossref]
19. Gharbi, N., Marciniak, A., & Doyen, A. (2022). Factors affecting the modification of bovine milk proteins in high hydrostatic pressure processing: An updated review. Comprehensive Reviews in Food Science and Food Safety, 21(5), 4274–4293. [Google Scholar] [Crossref]
20. Goyal, A., Sharma, V., Upadhyay, N., Sihag, M., & Kaushik, R. (2024). High Pressure Processing and Its Impact on Milk Proteins: A Review. Research & Reviews: Journal of Dairy Science and Technology, 2(1). [Google Scholar] [Crossref]
21. Harmsen, M. M., & De Jong, J. M. (2009). Bovine serum albumin interactions and stability. Journal of Agricultural and Food Chemistry, 57(8), 2976–2982. [Google Scholar] [Crossref]
22. Harvard T.H. Chan School of Public Health. (2021). The nutrition source – Milk. [Google Scholar] [Crossref]
23. Healthline. (2019). Milk 101: Nutrition Facts and Health Effects. [Google Scholar] [Crossref]
24. Hemar, Y., et al. (2020). Impact of high-pressure processing on the bioactive compounds of milk: A comprehensive review. Frontiers in Nutrition, 7, 583. [Google Scholar] [Crossref]
25. Heremans, K. (2002). High pressure effects on proteins and other biomolecules. Annual Review of Biophysics and Biomolecular Structure, 31, 1–24. [Google Scholar] [Crossref]
26. Huppertz, T., (2010). Improving the safety and quality of milk (pp. 373-399). Netherlands: Woodhead Publishing. [Google Scholar] [Crossref]
27. Huppertz, T., Fox, P. F., & Kelly, A. L. (2004). High pressure-induced changes in bovine milk: A review. International Dairy Journal, 14(7), 559–568. [Google Scholar] [Crossref]
28. Huppertz, T., Fox, P. F., & Kelly, A. L. (2006). Effects of high pressure on the rennet coagulation of milk. International Dairy Journal, 16(6), 625–630. [Google Scholar] [Crossref]
29. Huppertz, T., Fox, P. F., de Kruif, K. G., & Kelly, A. L. (2006). High pressure-induced changes in bovine milk proteins: A review. Biochimica et Biophysica Acta (BBA) - Proteins and Proteomics, 1764(3), 593–598. [Google Scholar] [Crossref]
30. Kato, Y., Matsuda, T., & Watanabe, K. (2000). Pressure-induced denaturation of bovine serum albumin. Bioscience, Biotechnology, and Biochemistry, 64(6), 1214–1218. [Google Scholar] [Crossref]
31. Koker, A., Ozturkoglu-Budak, S., & Alpas, H. (2023). Effects of high hydrostatic pressure on antimicrobial protein stability and the rheological and shelf-life properties of donkey milk. Journal of Dairy Research, 90(4), 1–9. [Google Scholar] [Crossref]
32. Korhonen, H. (2009). Milk-derived bioactive peptides: From science to applications. Journal of Functional Foods, 1(2), 177–187. [Google Scholar] [Crossref]
33. Kume, T., & Hayakawa, I. (1999). High pressure effects on immunoglobulin activity in milk. Food Science and Technology International, 5(3), 239–243. [Google Scholar] [Crossref]
34. Landim, A. P. M., Tiburski, J. H., Mellinger, C. G., Juliano, P., & Rosenthal, A. (2023). Potential Application of High Hydrostatic Pressure on the Production of Hydrolyzed Proteins with Antioxidant and Antihypertensive Properties and Low Allergenicity: A Review. Foods, 12(3), 630. [Google Scholar] [Crossref]
35. Lidsen. (2023). Nutritional Composition, Functionality and Health Benefits of Milk. [Google Scholar] [Crossref]
36. Lopandic, Zelger, Bánszky,Lechner and Prillinger, K. (2006). Identification of yeasts associated with milk products using traditional and molecular techniques. Food Microbiology, 341-350. [Google Scholar] [Crossref]
37. Lopez-Fandiño, R., Otte, J., & van Camp, J. (2007). Physiological, chemical and technological aspects of milk protein-derived peptides with antihypertensive activity. International Dairy Journal, 17(11), 1277–1293. [Google Scholar] [Crossref]
38. Lund, D. (2003). Predicting the impact of food processing on food constituents. Journal Of Food Engineering, 56(2-3), 113-117. [Google Scholar] [Crossref]
39. Messens, W., Van Camp, J., & Huyghebaert, A. (1997). The use of high pressure to modify the functionality of food proteins. Trends in Food Science & Technology, 8(4), 107–112. [Google Scholar] [Crossref]
40. Ozturk, M., Serdaroğlu, M., & Özdemir, N. (2010). Effect of high pressure processing on functional properties of whey proteins. Food and Bioproducts Processing, 88(2–3), 165–173. [Google Scholar] [Crossref]
41. Perez-Baena, I., Gómez-Ruiz, J. A., & Ramos, M. (2009). Peptides obtained by digestion of milk proteins and by microbial proteolysis. Dairy Science & Technology, 89(3), 319–338. [Google Scholar] [Crossref]
42. Pierce, A., Colavizza, D., Benaissa, M., Maes, P., Tissot, J. D., & Mazurier, J. (2009). Lactoferrin structure and function. BioMetals, 22(5), 777–784. [Google Scholar] [Crossref]
43. San Martín-González, M. F., Barbosa-Cánovas, G. V., & Swanson, B. G. (2007). Milk processing by high hydrostatic pressure. Critical Reviews in Food Science and Nutrition, 47(6), 501–513. [Google Scholar] [Crossref]
44. Schmidt, D. G., & van den Berg, G. (2015). Changes in milk protein interactions under high pressure. International Journal of Food Science & Technology, 50(1), 1–8. [Google Scholar] [Crossref]
45. Sultan, S., et al. (2014). Bioactive peptides from milk proteins: A review. International Journal of Dairy Technology, 67(4), 483–491. [Google Scholar] [Crossref]
46. Sunkesula, V. (2021). Nonfood applications for dairy proteins intrigue scientists. Dairy Foods. [Google Scholar] [Crossref]
47. Tetra Pak. (n.d.). Casein. Dairy Processing Handbook. [Google Scholar] [Crossref]
48. Torrezan, R., Mazzotti, C. B., & Vicente, A. A. (2007). Behavior of bovine serum albumin under high pressure. High Pressure Research, 27(2), 235–243. [Google Scholar] [Crossref]
49. User, S. (2020). Home. Retrieved 30 August 2020, from https://www.dairysafe.vic.gov.au/ [Google Scholar] [Crossref]
50. Wakabayashi, H., Takase, M., & Tomita, M. (2006). Lactoferrin function in gastrointestinal immunity. Current Pharmaceutical Design, 12(7), 827–831. [Google Scholar] [Crossref]
51. Wan, J., Zhong, Q., & Davidson, P. M. (2009). Impact of high-pressure processing on the antimicrobial activity of lactoferrin against foodborne pathogens. Journal of Food Protection, 72(3), 555–560. [Google Scholar] [Crossref]
52. Xu, F., et al. (2023). Effects of Ultra-High-Pressure Jet Processing on Casein Structure and Curdling Properties of Skimmed Bovine Milk. Molecules, 28(5), 2396. [Google Scholar] [Crossref]
53. Yalcin, A. S. (2006). Therapeutic potential of milk whey. Beverages, 3(3), 31. [Google Scholar] [Crossref]
54. Ye, A., Singh, H., & Taylor, M. W. (2004). Characterization of protein interactions in milk during heat and high pressure treatments using dynamic light scattering. Food Hydrocolloids, 18(6), 1033–1043. [Google Scholar] [Crossref]
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