Kinetic parameters for high-pressure-induced denaturation of lactoferrin in human milk

International Dairy Journal

Volumn 39, Issue 2, 2014, Pages 246-252

  Mayayo, C ^a   Montserrat, M ^a   Ramos, S J ^b   Martinez Lorenzo M J ^c   Calvo, M ^a   Sanchez L ^a   Perez M D ^a  

^a UNIVERSIDAD DE ZARAGOZA   (Spain)

^b Laboratorio del Ebro   (Spain)

^c Banco de Sangre y Tejidos de Aragón ^*  (Spain)

Author keywords

[No Author keywords available]

Indexed keywords

KINETIC PARAMETERS; PROTEINS; RATE CONSTANTS;

COVALENT INTERACTIONS; EFFECT OF HIGH PRESSURE; ENZYME LINKED IMMUNOSORBENT ASSAY; HIGH-PRESSURE PROCESSING; PRESSURE TREATMENTS; PROTEIN AGGREGATION; PROTEIN DENATURATION; THERMAL PASTEURISATION; HUMAN MILK; LACTOFERRIN;

DENATURATION;

EID: 84905923717     PISSN: 09586946     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.idairyj.2014.07.001     Document Type: Article

References (47)

1. Anema S.G., Stockmann R., Lowe E.K. Denaturation of β-lactoglobulin in pressure-treated skim milk. Journal of Agricultural and Food Chemistry 2005, 53:7783-7791.
2. Baker E.N., Baker H.M. Molecular structure, binding properties and dynamics of lactoferrin. Cellular and Molecular Biology 2005, 62:2531-2539.
3. Baker E.N., Baker H.M. Astructural framework for understanding the multifunctional character of lactoferrin. Biochimie 2009, 91:3-10.
4. Ballard O., Morrow A.L. Human milk composition: nutrients and bioactive factors. Pediatric Clinics of North America 2013, 60:49-74.
5. Baranyi J., Pin C., Ross T. Validating and comparing predictive models. International Journal of Food Microbiology 1999, 48:159-166.
6. Björkstén B., Burman L.G., De Château P., Fredrikzon B., Gothefors L., Hernell O. Collecting and banking human milk: to heat or not to heat?. British Medical Journal 1980, 281:765-769.
7. Brisson G., Britten M., Pouliot Y. Heat-induced aggregation of bovine lactoferrin at neutral pH: effect of iron saturation. International Dairy Journal 2007, 17:617-624.
8. Brisson G., Britten M., Pouliot Y. Effect of iron saturation on the recovery of lactoferrin in rennet whey coming from heat-treated skim milk. Journal of Dairy Science 2007, 90:2655-2664.
9. Catty D., Raykundalia C. ELISA and related enzyme immunoassay. Antibodies: A practical approach 1989, Vol. 2:97-154. IRL Press, Oxford, UK.
10. Chang J.C., Chen C.H., Fang L.J., Tsai C.R., Chang Y.C., Wang T.M. Influence of prolonged storage process, pasteurization and heat treatment on biologically-active human milk proteins. Pediatrics Neonatology 2013, 54:360-366.
11. Contador R., Delgado-Adámez J., Delgado F.J., Cava R., Ramírez R. Effect of thermal pasteurisation or high processing on immunoglobulin and leukocyte contents of human milk. International Dairy Journal 2013, 32:1-5.
12. Czank C., Prime D.K., Hartmann B., Simmer K., Hartmann P.E. Retention of the immunological proteins of pasteurized human milk in relation to pasteurizer design and practice. Pediatric Research 2009, 66:374-379.
13. Delgado F.J., Contador R., Álvarez-Barrientos A., Cava R., Delgado-Adámez J., Ramírez R. Effect of high pressure thermal processing on some essential nutrients and immunological components present in breast milk. Innovative Food Science and Emerging Technologies 2013, 19:50-56.
14. Evans T.J., Ryley H.C., Neale L.M., Dodge J.A., Lewarne V.M. Effect of the storage and heat on antimicrobial proteins in human milk. Archives of Disease in Childhood 1978, 53:239-241.
15. Farnaud S., Evans R.W. Lactoferrin: the conductor of the immunological system?. New research on immunology 2005, 47-76. Nova Science Publishers, New York, NY, USA. B.A. Veskler (Ed.).
16. Ford J.E., Law B.A., Marshall V.M.E., Reiter B. Influence of the heat treatment of human milk on some of its protective constituents. Journal of Pediatrics 1977, 90:29-35.
17. Franco I., Castillo E., Pérez M.D., Calvo M., Sánchez L. Effect of bovine lactoferrin addition to milk in yogurt manufacturing. Journal of Dairy Science 2010, 93:4480-4489.
18. Franco I., Castillo E., Pérez M.D., Calvo M., Sánchez L. Effects of hydrostatic high pressure on the structure and antibacterial activity of recombinant human lactoferrin from transgenic rice. Bioscience, Biotechnology and Biochemistry 2011, 76:53-59.
19. Franco I., Pérez M.D., Castillo E., Calvo M., Sánchez L. Effect of high pressure on the structure and antibacterial activity of bovine lactoferrin treated in different media. Journal of Dairy Research 2013, 80:283-290.
20. Hanson L.A., Silfverdal S.A. The mother's immune system is a balanced threat to the fetus, turning to protection of the neonate. Acta Paediatrica 2009, 98:221-228.
21. Haridas M., Anderson B.F., Baker E.N. Structure of human diferric lactoferrin at 2.2Å resolution. Acta Crystallographica Section, D 1995, 51:629-646.
22. Hinrichs J., Rademacher B. High pressure thermal denaturation kinetics of whey proteins. Journal of Dairy Research 2004, 71:480-488.
23. Huppertz T., Fox P.F., Kelly A.L. High pressure-induced denaturation of α-lactalbumin and β-lactoglobulin in bovine milk and whey: a possible mechanism. Journal of Dairy Research 2004, 71:489-495.
24. Lawrence R.M., Lawrence R.A. Breastfeeding: A guide for the medical profession 2011, Elsevier Mosby, Maryland, MO, USA. 7th ed.
25. Legrand D., Pierce A., Elass E., Carpentier M., Mariller C., Mazurier J. Lactoferrin structure and functions. Advances in Experimental Medicine and Biology 2008, 606:163-194.
26. Lönnerdal B. Nutritional and physiologic significance of human milk proteins. American Journal of Clinical Nutrition 2003, 77:1537S-1543S.
27. Lönnerdal B., Forsum E., Hambreus L. Alongitudinal study of the protein, nitrogen and lactose contents of human milk from Swedish well-nourished mothers. American Journal of Clinical Nutrition 1976, 29:1127-1133.
28. López-Fandiño R. Functional improvement of milk whey proteins induced by high hydrostatic pressure. Critical Reviews in Food Science and Nutrition 2006, 46:351-363.
29. Mata L., Sánchez L., Headon D.R., Calvo M. Thermal denaturation of human lactoferrin and its effect on the ability to bind iron. Journal of Agricultural and Food Chemistry 1998, 46:3964-3970.
30. Mazri C., Ramos S.J., Sánchez L., Calvo M. Effect of high pressure treatment on denaturation of bovine β-lactoglobulin and α-lactalbumin. European Food Research and Technology 2012, 234:813-819.
31. Mazri C., Sanchez L., Perez M.D. Effect of high-pressure and heat treatments on denaturation and aggregation of bovine whey proteins: Influence of sulphydryl modifying agents and glycerol. Bulletin of the International Dairy Federation 2014, 472:49-54.
32. Mazri C., Sánchez L., Ramos S.J., Calvo M., Pérez M.D. Effect of high-pressure treatment on denaturation of bovine lactoferrin and lactoperoxidase. Journal of Dairy Science 2012, 95:549-557.
33. Moore S.A., Anderson B.F., Groom C.R., Haridas M., Baker E.N. Three dimensional structure of diferric bovine lactoferrin at 2.8Å resolution. Journal of Molecular Biology 1997, 274:222-236.
34. Opdenakker G., Rudd P.M., Ponting C.P., Dwek R.A. Concepts and principles of glycobiology. Journal of the Federation of American Societies for Experimental Biology 1993, 7:1330-1337.
35. Patel H.A., Singh H., Anema S.G., Creamer L.K. Effects of heat and high hydrostatic pressure on the aggregation of whey proteins concentrate solutions. Food New Zealand 2004, 4:29-35.
36. Patel H.A., Singh H., Anema S.G., Creamer L.K. Effects of heat and high hydrostatic pressure on disulfide bonding interchanges among the proteins in skim milk. Journal of Agricultural and Food Chemistry 2006, 54:3409-3420.
37. Permanyer M., Castellote C., Ramírez-Santana C., Autí C., Pérez-Cano F.J., Castell M., et al. Maintenance of breast milk immunoglobulin A after high-pressure processing. Journal of Dairy Science 2010, 93:877-883.
38. Rastogi N.K., Raghavarao K.S.M.S. Opportunities and challenges in high pressure processing of foods. Critical Reviews in Food Science and Nutrition 2007, 47:69-112.
39. Royer C.A. Revisiting volume changes in pressure-induced protein unfolding. Biochimica et Biophysica Acta 2002, 1595:201-209.
40. Sánchez L., Peiró J.M., Castillo H., Pérez M.D., Ena J.M., Calvo M. Kinetic parameters for denaturation of bovine milk lactoferrin. Journal of Food Science 1992, 57:873-879.
41. Trembay L., Laporte M., Leonil F.J., Dupont D., Raquin P. Quantitation of proteins in milk and milk products. Advanced dairy chemistry 2003, Vol. 1:49-138. Kluwer Academic, New York, NY, USA. P.F. Fox, L.H. McSweeney (Eds.).
42. Tully D.B., Jones F., Tully M.R. Donor milk: what's in it and what's not. Journal of Human Lactation 2001, 17:152-155.
43. Van Veen H.A., Geerts M.E.J., van Berkel P.H.C., Nuijens J.H. The role of N-linked glycosylation in the protection of human and bovine lactoferrin against tryptic proteolysis. European Journal of Biochemistry 2004, 271:678-684.
44. Viazis S., Farkas B.E., Allen J.C. Effects of high-pressure processing on immunoglobulin A and lysozyme activity in human milk. Journal of Human Lactation 2007, 23:253-261.
45. Viazis S., Farkas B.E., Jaykus L.A. Inactivation of bacterial pathogens in human milk by high-pressure processing. Journal of Food Protection 2008, 71:109-118.
46. Ward P.P., Paz E., Conneely O.M. Multifunctional roles of lactoferrin: a critical overview. Cellular and Molecular Life Science 2005, 62:2540-2548.
47. Wehbi Z., Pérez M.D., Sanchez L., Pocovi C., Barbana C., Calvo M. Effect of heat treatment on denaturation of bovine alpha-lactalbumin: determination of kinetic and thermodynamic parameters. Journal of Agricultural and Food Chemistry 2005, 53:9730-9736.