Proteins and Peptides in Fermented Dairy Products

Authors

  • Wanling Tian

DOI:

https://doi.org/10.54097/mb51n925

Keywords:

peptides; fermented dairy products; function; regulatory mechanisms.

Abstract

Peptides in fermented dairy products have gained significant attention due to their diverse bioactive properties and health benefits. Derived from milk proteins such as casein and whey, these peptides exhibit antioxidant, antihypertensive, antimicrobial, and immunomodulatory effects, enhancing both nutritional and functional qualities of fermented milk. The production and activity of these peptides are influenced by fermentation conditions, microbial strains, and enzymatic processes. Advances in biotechnology, including high-throughput screening and molecular modeling, have enabled targeted optimization of peptide functionality. Clinical studies highlight their potential in managing hypertension and improving immune responses, offering natural alternatives to traditional therapeutics. Future research aims to address challenges in stability and industrial-scale production while exploring broader applications in functional foods and biomedicine.

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References

[1] E. B.-M. Daliri, B. H. Lee, and D. H. Oh, “Current Perspectives on Antihypertensive Probiotics,” Probiotics Antimicrob. Proteins, vol. 9, no. 2, pp. 91–101, Jun. 2017, doi: 10.1007/s12602-016-9241-y.

[2] N. Auestad and D. K. Layman, “Dairy bioactive proteins and peptides: a narrative review,” Nutr. Rev., vol. 79, pp. 36–47, Dec. 2021, doi: 10.1093/nutrit/nuab097.

[3] Á. A. Fekete, C. Giromini, Y. Chatzidiakou, D. I. Givens, and J. A. Lovegrove, “Whey protein lowers systolic blood pressure and Ca-caseinate reduces serum TAG after a high-fat meal in mildly hypertensive adults,” Sci. Rep., vol. 8, no. 1, p. 5026, Mar. 2018, doi: 10.1038/s41598-018-23333-2.

[4] S. Chakrabarti, S. Guha, and K. Majumder, “Food-Derived Bioactive Peptides in Human Health: Challenges and Opportunities,” Nutrients, vol. 10, no. 11, p. 1738, Nov. 2018, doi: 10.3390/nu10111738.

[5] D. Caccavo et al., “Antimicrobial and immunoregulatory functions of lactoferrin and its potential therapeutic application,” J. ENDOTOXIN Res., vol. 8, no. 6, pp. 403–417, 2002, doi: 10.1179/096805102125001000.

[6] Y. Nakamura, N. Yamamoto, K. Sakai, A. Okubo, S. Yamazaki, and T. Takano, “Purification and Characterization of Angiotensin I-Converting Enzyme Inhibitors from Sour Milk,” J. Dairy Sci., vol. 78, no. 4, pp. 777–783, Apr. 1995, doi: 10.3168/jds. S0022-0302(95)76689-9.

[7] G. R. Rama et al., “From in silico to in vitro: Hydrolysis of cheese whey to obtain peptides with anti-aging and anti-hypertensive activities,” Biocatal. Agric. Biotechnol., vol. 57, p. 103093, Apr. 2024, doi: 10.1016/j.bcab.2024.103093.

[8] C. G. De Kruif and C. Holt, “Casein Micelle Structure, Functions and Interactions,” in Advanced Dairy Chemistry—1 Proteins: Part A / Part B, P. F. Fox and P. L. H. McSweeney, Eds., Boston, MA: Springer US, 2003, pp. 233–276. doi: 10.1007/978-1-4419-8602-3_5.

[9] A. B. Shazly et al., “Fractionation and identification of novel antioxidant peptides from buffalo and bovine casein hydrolysates,” Food Chem., vol. 232, pp. 753–762, Oct. 2017, doi: 10.1016/j.foodchem.2017.04.071.

[10] B. Lönnerdal and S. Iyer, “Lactoferrin: Molecular Structure and Biological Function,” Annu. Rev. Nutr., vol. 15, no. 1, pp. 93–110, Jul. 1995, doi: 10.1146/annurev.nu.15.070195.000521.

[11] B. Lönnerdal, “Nutritional and physiologic significance of human milk proteins,” Am. J. Clin. Nutr., vol. 77, no. 6, pp. 1537S-1543S, Jun. 2003, doi: 10.1093/ajcn/77.6.1537S.

[12] M. Tomita, W. Bellamy, M. Takase, K. Yamauchi, H. Wakabayashi, and K. Kawase, “Potent Antibacterial Peptides Generated by Pepsin Digestion of Bovine Lactoferrin,” J. Dairy Sci., vol. 74, no. 12, pp. 4137–4142, Dec. 1991, doi: 10.3168/jds. S0022-0302(91)78608-6.

[13] R. T. Ellison and T. J. Giehl, “Killing of gram-negative bacteria by lactoferrin and lysozyme.,” J. Clin. Invest., vol. 88, no. 4, pp. 1080–1091, Oct. 1991, doi: 10.1172/JCI115407.

[14] B. Murray and R. FitzGerald, “Angiotensin Converting Enzyme Inhibitory Peptides Derived from Food Proteins: Biochemistry, Bioactivity and Production,” Curr. Pharm. Des., vol. 13, no. 8, pp. 773–791, Mar. 2007, doi: 10.2174/138161207780363068.

[15] R. J. FitzGerald, B. A. Murray, and D. J. Walsh, “Hypotensive Peptides from Milk Proteins,” J. Nutr., vol. 134, no. 4, pp. 980S-988S, Apr. 2004, doi: 10.1093/jn/134.4.980S.

[16] F. Tonolo et al., “Identification of New Peptides from Fermented Milk Showing Antioxidant Properties: Mechanism of Action,” ANTIOXIDANTS, vol. 9, no. 2, p. 117, Feb. 2020, doi: 10.3390/antiox9020117.

[17] B. Wang, Y. P. Timilsena, E. Blanch, and B. Adhikari, “Lactoferrin: Structure, function, denaturation and digestion,” Crit. Rev. Food Sci. Nutr., vol. 59, no. 4, pp. 580–596, Feb. 2019, doi: 10.1080/10408398.2017.1381583.

[18] Q. Rascon-Cruz, E. A. Espinoza-Sanchez, T. S. Siqueiros-Cendon, S. I. Nakamura-Bencomo, S. Arevalo-Gallegos, and B. F. Iglesias-Figueroa, “Lactoferrin: A Glycoprotein Involved in Immunomodulation, Anticancer, and Antimicrobial Processes,” MOLECULES, vol. 26, no. 1, p. 205, Jan. 2021, doi: 10.3390/molecules26010205.

[19] H. Korhonen, P. Marnila, and H. S. Gill, “Milk immunoglobulins and complement factors,” Br. J. Nutr., vol. 84, no. S1, pp. 75–80, Nov. 2000, doi: 10.1017/S0007114500002282.

[20] T. Hu et al., “Antioxidant effect of Lactobacillus fermentum HFY02-fermented soy milk on D-galactose-induced aging mouse model,” FOOD Sci. Hum. WELLNESS, vol. 11, no. 5, pp. 1362–1372, Sep. 2022, doi: 10.1016/j.fshw.2022.04.036.

[21] D. B. Kell, E. L. Heyden, and E. Pretorius, “The Biology of Lactoferrin, an Iron-Binding Protein That Can Help Defend Against Viruses and Bacteria,” Front. Immunol., vol. 11, p. 1221, May 2020, doi: 10.3389/fimmu.2020.01221.

[22] A. C. Carpenter, T. P. Saborido, and G. D. Stanwood, “Development of Hyperactivity and Anxiety Responses in Dopamine Transporter-Deficient Mice,” Dev. Neurosci., vol. 34, no. 2–3, pp. 250–257, Sep. 2012, doi: 10.1159/000336824.

[23] S. L. Hyman et al., “Identification, Evaluation, and Management of Children with Autism Spectrum Disorder,” Pediatrics, vol. 145, no. 1, Jan. 2020, doi: 10.1542/peds.2019-3447.

[24] A. Sinopoli, C. Isonne, M. M. Santoro, and V. Baccolini, “The effects of orally administered lactoferrin in the prevention and management of viral infections: A systematic review,” Rev. Med. Virol., vol. 32, no. 1, p. e2261, Jan. 2022, doi: 10.1002/rmv.2261.

[25] T. Zhe et al., “Bimetallic-MOF-derived crystalline–amorphous interfacial sites for highly efficient nitrite sensing,” Food Chem., vol. 402, p. 134228, Feb. 2023, doi: 10.1016/j.foodchem.2022.134228.

[26] M. A. Alvarez-Olguin et al., “Bioaccessibility and Bioavailability of ACE Inhibitory Peptides from Fermented Milk with Lactococcus lactis NRRL B-50571 after an Ex Vivo Absorption Model,” ACS Food Sci. Technol., vol. 3, no. 7, pp. 1269–1277, 2023, doi: 10.1021/acsfoodscitech.3c00148.

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Published

05-09-2025