Keywords
Denaturation
Bovine whey proteins
Antibacterial activity
Food
Kinetic analysis
How to Cite
Abstract
Lactoferrin, IgG and lactoperoxidase provide health benefits. The antimicrobial properties of these proteins permit the use of them as supplements for nutraceutical products. These properties are vulnerable during processing. High-Pressure (HP) treatment is an appealing option in contrast to the customary heat processing of food. In this research, the impact of HP treatment on the denaturation of proteins present in skim milk and whey, and in buffer, were analyzed over a pressure range of 450 to 700 MPa at 20°C. The process of denaturation was analyzed by kinetic analysis. Denaturation of lactoferrin and IgG were estimated utilizing a sandwich ELISA and radial immunodifussion, individually. Denaturation of lactoperoxidase was recorded by estimating the loss of enzymatic activity. Results obtained indicated that the effect of HP depend widely on the protein. At the point when milk was treated at 500 MPa, higher values of D-value, of 74×102, and 123×102 sec, were recorded for lactoferrin and IgG, respectively. For lactoperoxidase, no loss of activity was seen after 30 min. Lactoferrine and IgG are denatured more slowly in buffer and in milk than in whey. The stability of lactoferrin, IgG and lactoperoxidase is to be considered to use them as bioactive components in food.
References
Anema SG, Stockmann R and Lowe EK. 2005. Denaturation of β-lactoglobulin in pressure-treated skim milk. Journal of Agricultural and Food Chemistry, 53(20): 7783-7791.
Considine T, Patel HA, Anema SG, Singh H and Creamer LK. 2007. Interactions of milk proteins during heat and high hydrostatic pressure treatments. Innovative Food Science & Emerging Technologies, 8(1): 1-23.
Dannenberg F and Kessler HG. 1988. Thermodynamic approach to kinetics of b-lactoglobulin denaturation in heated skim milk and sweet whey. Milchwissenschaf, 43: 139-142.
Felipe X, Capellas M and Law AR. 1997. Comparison of the effects of high-pressure treatments and heat pasteurisation on the whey proteins in goat’s milk. Journal of Agricultural and Food Chemistry, 45(3): 627-631.
Garcia-Graells C, Van Opstal I, Vanmuysen SCM and Michiels CW. 2003. The lactoperoxidase system increases efficacy of high-pressure inactivation of food borne bacteria. International Journal of Food Microbiology, 81(3): 211-221.
Hinrichs J, Rademacher B and Kessler HG. 1996. Reaction kinetics of pressure-induced denaturation of whey proteins. Milchwissenschaft, 51(9): 504-509.
Hinrichs J and Rademacher B. 2005. Kinetics of combined thermal and pressure-induced whey protein denaturation in bovine skim milk. International Dairy Journal, 15(4): 315-323.
Indyk HE, Williams JW and Patel HA. 2008. Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor. International Dairy Journal, 18(4): 359-366.
Johnson FH and Campbell DH. 1945. Retardation of protein denaturation by high pressure. Journal of Cellular and Comparative Physiology, 44: 213-231.
Law AJR, Banks JM, Horne DS, Leaver J and West IG. 1994. Denaturation of the whey protein in heated milk and their incorporation into Cheddar cheese. Milchwissenschaft, 49: 63-66.
Li-Chan E, Kummer A, Losso JN, Kitts DD and Nakai S. 1995. Stability of bovine immunoglobulins to heat treatment and processing. Food Research International, 28(1): 9-16.
Lucisano M, Pompei C, Casiraghi E and Rizzo AM. 1994. Milk pasteurization: evaluation of thermal damage. Italian Journal of Food Science, 6: 185-197.
Ludikhuyze LR, Claeys WL and Hendrickx ME. 2001. Effect of temperature and/or pressure on lactoperoxidase activity in bovine milk and acid whey. Journal of Dairy Research, 68(4): 625-637.
Mainer G, Sánchez L, Ena JM and Calvo M. 1997. Kinetic and thermodynamic parameters for heat denaturation of bovine milk IgG, IgA and IgM. Journal of Food Science, 62(5): 1034-1038.
Mazri C, Ramos SJ, Sánchez L, Calvo M and Pérez MD. 2012a. Reaction kinetics of pressure-induced denaturation of bovine immunoglobulin G. International Dairy Journal, 24(1): 8-12.
Mazri C, Sánchez L, Ramos SJ, Calvo M and Pérez MD. 2012b. Effect of high pressure treatment on denaturation of bovine lactoferrin and lactoperoxidase. Journal of Dairy Science, 95(2): 549-557.
Patel HA, Singh H, Anema SG and Creamer LK. 2004. Effects of heat and high hydrostatic pressure on the aggregation of whey proteins concentrate solutions. Food New Zealand, 4(3): 29-35.
Rademacher B and Kessler HG. 1997. High pressure inactivation of microorganisms and enzymes in milk and milk products. High Pressure Bio-Science and Biotechnology, Leuven, Bélgica, 291-293 p.
Royer CA. 2002. Revisiting volume changes in pressure-induced protein unfolding. Biochimica et Biophysica Acta, 1595(1-2): 201-209.
Sánchez L, Peiró JM, Castillo H, Pérez MD, Ena JM and Calvo M. 1992. Kinetic parameters for denaturation of bovine milk lactoferrin. Journal of Food Science, 57(4): 873-879.
Seyderhelm I, Boguslawski S, Michaelis G and Knorr D. 1996. Pressure induced inactivation of selected food enzymes. Journal of Food Science, 61(2): 308-310.
Tremblay L, Laporte M, Leonil FJ, Dupont D and Raquin P. 2003. Advanced dairy chemistry proteins: Quantitation of proteins in milk and milk products. Volume 1, Kluwer Academic, New York, USA, 49-138 p.
Trujillo AJ, Castro N, Quevedo JM, Argüello A, Capote J and Guamis B. 2007. Effect of high-pressure treatments on microbiological quality and Immunoglobulin G stability of caprine colostrum. Journal of Dairy Science, 90(2): 833-839.
Wehbi Z, Pérez MD, Sanchez L, Pocovi C, Barbana C and Calvo M. 2005. Effect of heat treatment on denaturation of bovine alpha-lactalbumin: determination of kinetic and thermodynamic parameters. Journal of Agricultural and Food Chemistry, 53(25): 9730-9736.
Copyright license for the research articles published in Journal of Research in Biology are as per the license given below
Creative Commons License
Journal of Research in Ecology is licensed under a Creative Commons Attribution 4.0 International (CC BY 4.0). (www.creativecommons.org)
Based on a work at www.jresearchbiology.com
What this License explains us?
You are free to:
Share — copy and redistribute the material in any medium or format
Adapt — remix, transform, and build upon the material
for any purpose, even commercially.
This license is acceptable for Free Cultural Works. The licensor cannot revoke these freedoms as long as you follow the license terms.
[As given in the www.creativecommons.org website]
Under the following terms:
Attribution — You must give appropriate credit, provide a link to the license, and indicate if changes were made. You may do so in any reasonable manner, but not in any way that suggests the licensor endorses you or your use.
No additional restrictions — You may not apply legal terms or technological measures that legally restrict others from doing anything the license permits.