Differences in Several Important Proteins Contents between Raw Milk and Reconstituted Milk

Abstract:

The objective of this study was to evaluate the nutritional quality of reconstituted milk by determining concentrations of several important proteins. Difference in protein between raw milk and reconstituted milk was determined with spectrophotometer, HPLC, fluorometry, ELISA, photon correlation spectroscopy. Total undenatured whey protein, β-lactoglobulin, α-lactalbumin, chemically available lysine, insulin-like growth factor-Ⅰ (IGF-Ⅰ), epidermal growth factor (EGF), immunoglobulin G (IgG) contents and casein micelle size were analyzed for both raw milk and reconstituted milk. Results showed that reconstituted milk had a significant decrease (P<0.01) in total undenatured whey protein, β-lactoglobulin, α-lactalbumin, chemically available lysine, IGF-Ⅰ, EGF and IgG. The decrease of casein micelle particle size confirmed that most of the whey protein denatured and associated with the casein micelle occurred in the processing of milk powder manufacture. It is concluded that reconstituted milk has a lower nutritional value than that of raw milk.

• Periodical: Advanced Materials Research (Volumes 343-344)
• Pages: 1000-1006
• DOI: https://doi.org/10.4028/www.scientific.net/AMR.343-344.1000
• Online since: September 2011
• Authors: Rong Fa Guan, Dong Hong Liu, Jia Xin Jiang, Chang Rui, Peng Peng Liu, Xing Qian Ye
• Keywords: Denaturalization, Nutritional Value, Protein, Reconstituted Milk

References

[1] Chen, Y., Yu, S.Z., Wx, Li., Artificial feeding and hospitalization in the first 18 months of life. Pediatric, Pediatrics, vol. 81, no. 1, pp: 58–62, (1988).

[2] Burton, H., Reviews of the progress of Dairy Science: The bacteriological, chemical biochemical and physical changes that can occur in milk at temperatures of 100–150 ºC, J Dairy Res, vol. 51, no. 2, pp: 341–363, (1984).

DOI: 10.1017/s002202990002361x

[3] Jeurnink, T., De Kruif, K., Changes in milk on heating: viscosity measurements, J Dairy Res, vol. 60, no, 2, pp: 139–150, (1993).

DOI: 10.1017/s0022029900027461

[4] Ford, J. E., Hurrell, R.F., Finot, P.A., Storage of milk powders under adverse conditions. 2. Influence on the content of water-soluble vitamins, Brit J Nutr, vol. 49, no. 3, pp: 355-364, (1983).

DOI: 10.1079/bjn19830044

[5] Hurrell, R.F., Finot, P.A., Ford, J.E., Storage of milk powders under adverse conditions. 1. Losses of lysine and of other essential amino acids as determined by chemical and microbiological methods, Brit J Nutr, vol. 49, no. 3, pp: 343-354, (1983).

DOI: 10.1079/bjn19830043

[6] Hall, G., Lingnert, H., Flavor changes in whole milk powder during storage. 1. Odor and flavor profiles of dry milk with additions of antioxidants and stored under air or nitrogen, J Food Quality, vol. 7, no. 4, pp: 131-151, (1984).

DOI: 10.1111/j.1745-4557.1985.tb01056.x

[7] Renner, E., Storage stability and some nutritional aspects of milk powders and ultra high temperature products at high ambient temperatures, J Dairy Res, vol. 55, no. 1, pp: 125-142, (1988).

DOI: 10.1017/s0022029900025942

[8] Min, D.B., Lee, S.H., Lindamood, J.B., Chang, K.S., Reineccius, G.A., Effects of packaging conditions on the flavor stability of dry whole milk, J Food Sci, vol. 54, no. 5, pp: 1222-1224, (1989).

DOI: 10.1111/j.1365-2621.1989.tb05959.x

[9] Chan, S.H., Gray, J.I., Gomaa, E.A., Harte, B.R., Kelly, P.M., Buckley, D.J., Cholesterol oxidation in whole milk powders as influenced by processing and packaging, Food Chem, vol. 47, no. 4, pp: 321-328, (1993).

DOI: 10.1016/0308-8146(93)90171-b

[10] Lowry, O.H., Rosebrough, N.J., Farr, A.L., Randall, R.J., Protein measurement with the Folin phenol reagent, J Biol Chem, vol. 193, no. 1, pp: 265–275, (1951).

DOI: 10.1016/s0021-9258(19)52451-6

[11] Isabel, V.O., Ferreira, Helena, C., Detection and quantification of bovine, ovine and caprine milk percentages in protected denomination of origin cheeses by reversed-phase high-performance liquid chromatography of beta-lactoglobulins, J Chromatogr A, vol. 1015, no. 1-2, pp: 111–118, (2003).

DOI: 10.1016/s0021-9673(03)01261-5

[12] Kummer, A., Kitts, D.D., Li, C.E., Loss, J.N., Skura, B.J., Nakai, S., Quantification of bovine IgG in milk using enzyme-linked immunosorbent assay, Food Agric Immunol, vol. 4, no. 2, pp: 93-102, (1992).

DOI: 10.1080/09540109209354757

[13] Zhao, X., Groenewegen, P.P., McBride, BW., Burton, J. H., Elsasser, T.H., Radioimmunoassay for insulin-like growth factor-I in bovine milk, Can J Anim Sci, vol. 71, no. 3, pp: 669-674, (1991).

DOI: 10.4141/cjas91-082

[14] Katagiri, S., Takahashi, Y., Changes in EGF concentrations during estrous cycle in bovine endometrium and their alterations in repeat breeder cows, Theriogenology, vol. 62, no. 1-2, pp: 103-112, (2004).

DOI: 10.1016/j.theriogenology.2003.08.019

[15] Ferrer, E., Alegría, A., Rosaura, Farré., Abellán, P., Romero, F., "Fluorometric determination of chemically available lysine: Adaptation, validation and application to different milk products, Nahrung, vol. 47, no. 6, pp: 403-407. (2003).

DOI: 10.1002/food.200390090

[16] Anema, S. G., The effect of chymosin on κ-casein-coated polystyrene latex particles and bovine casein micelles, Int Dairy J, vol. 7, no. 8-9, pp: 553-558, (1997).

DOI: 10.1016/s0958-6946(97)00048-4

[17] Chen, W.L., Wang, M.T.H., Liau, C.Y., Ho, J.C., Hong, K.C., Mao, J.T., ß-lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra, J Dairy Sci, vol. 88, no. 5, pp: 1618-1630, (2005).

DOI: 10.3168/jds.s0022-0302(05)72833-2

[18] Li, C.E., Kummer, A., Losso, J.N., Kitts, D.D., Nakai, S., Stability of bovine immunoglobulins to thermal treatment and processing, Food Res Int, vol. 28, no. 1, pp: 9-16, (1995).

DOI: 10.1016/0963-9969(95)93325-o

[19] Miller, M.A., Hildebrandt, J.R., White, T.C., Hammond, B.G., Madsen, K.S., Collier, R.J., Determination of insulin-like growth factor-I (IGF-I) concentrations in raw, pasteurized and heat-treated milk, J. Dairy Sci, vol. 74, no. 9, pp: Suppl. 1, 186, (1989).

[20] Rehman, Z.U., Effect of storage on the available lysine and lactose contents of UHT processed whole and skimmed buffalo milk, Milchwissenschaft, vol. 57, no. 11-12, pp: 629-631, (2002).

[21] Anantharaman, K., Finot, P. A., Nutritional aspects of food proteins in relation to technology, Food Rev Int, vol. 9, no. 4, pp: 629-655, (1993).

DOI: 10.1080/87559129309540981

[22] Morales, F.J., Romero, C., Jiménez-Pérez, S., Evaluation of heat-induced changes in Spanish commercial milk: hydroxymethylfurfural and available lysine content, Int J Food Sci Tech, vol. 31, no. 5, pp: 411–418, (1996).

DOI: 10.1046/j.1365-2621.1996.00357.x

[23] Corredig, M., Dalgleish, D,G., Effect of temperature and pH on the interactions of whey proteins with casein micelles in skim milk, Food Res Int, vol. 29, no. 1, pp: 49–55, (1996).

DOI: 10.1016/0963-9969(95)00058-5

[24] Oldfield, D.J., Singh, H., Taylor, M.W., Pearce, K.N., Heat-induced interactions of β-lactoglobulin and α-lactalbumin with the casein micelle in pH adjusted skim milk, Int Dairy J, vol. 10, no. 8, pp: 509–518, (2000).

DOI: 10.1016/s0958-6946(00)00087-x

[25] Anema, S.G., Li, Y., Effect of pH on the association of denatured whey proteins with casein micelles in heated reconstituted skim milk, J Agr Food Chem, vol. 51, no. 6, pp: 1640-1646, (2003).

DOI: 10.1021/jf025673a

[26] Vasbinder, A.J., Alting, A.C., de Kruif, C.G., Quantification of heat-induced casein-whey protein interactions in milk and its relation to gelation kinetics, Colloid Surface B: Bio, vol. 31, no. 1-4, pp: 115-123, (2003).

DOI: 10.1016/s0927-7765(03)00048-1