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Volumn 51, Issue , 2015, Pages 251-255

Thermal markers arising from changes in the protein component of milk

Author keywords

BSA; ELISA; Heat treatment; IPF; Milk; Protein aggregates; SDS PAGE; SPF; Thermal marker; UHT; Whey proteins; la; lg

Indexed keywords

BOVINAE;

EID: 84949117092     PISSN: 09567135     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodcont.2014.11.029     Document Type: Review
Times cited : (14)

References (38)
  • 1
    • 0032839314 scopus 로고    scopus 로고
    • Heat-induced deamidation, dephosphorylation and breakdown of caseinate
    • van Boekel M.A.J.S. Heat-induced deamidation, dephosphorylation and breakdown of caseinate. International Dairy Journal 1999, 9:237-241.
    • (1999) International Dairy Journal , vol.9 , pp. 237-241
    • van Boekel, M.A.J.S.1
  • 2
    • 20844436321 scopus 로고    scopus 로고
    • β-Lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra
    • Chen W.L., Hwang M.T., Liau C.Y., Ho J.C., Hong K.C., Mao S.J.T. β-Lactoglobulin is a thermal marker in processed milk as studied by electrophoresis and circular dichroic spectra. Journal of Dairy Science 2005, 88:1618-1630.
    • (2005) Journal of Dairy Science , vol.88 , pp. 1618-1630
    • Chen, W.L.1    Hwang, M.T.2    Liau, C.Y.3    Ho, J.C.4    Hong, K.C.5    Mao, S.J.T.6
  • 3
    • 67649836544 scopus 로고    scopus 로고
    • Use of reducing/non-reducing two dimensional electrophoresis for the study of disulfide-mediated interactions between proteins in raw and heated bovine milk
    • Chevalier F., Hirtz C., Sommerer N., Kelly A.L. Use of reducing/non-reducing two dimensional electrophoresis for the study of disulfide-mediated interactions between proteins in raw and heated bovine milk. Journal of Agricultural and Food Chemistry 2009, 57:5948-5955.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 5948-5955
    • Chevalier, F.1    Hirtz, C.2    Sommerer, N.3    Kelly, A.L.4
  • 4
    • 77953641675 scopus 로고    scopus 로고
    • Proteomic quantification of disulfide-linked polymers in raw and heated bovine milk
    • Chevalier F., Kelly A.L. Proteomic quantification of disulfide-linked polymers in raw and heated bovine milk. Journal of Agricultural and Food Chemistry 2010, 58:7437-7444.
    • (2010) Journal of Agricultural and Food Chemistry , vol.58 , pp. 7437-7444
    • Chevalier, F.1    Kelly, A.L.2
  • 5
    • 0001192133 scopus 로고    scopus 로고
    • Effect of different heat treatments on the strong binding interactions between whey proteins and milk fat globules in whole milk
    • Corredig M., Dalgleish D.G. Effect of different heat treatments on the strong binding interactions between whey proteins and milk fat globules in whole milk. Journal of Dairy Research 1996, 63:441-449.
    • (1996) Journal of Dairy Research , vol.63 , pp. 441-449
    • Corredig, M.1    Dalgleish, D.G.2
  • 6
    • 0032867758 scopus 로고    scopus 로고
    • The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk
    • Corredig M., Dalgleish D.G. The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk. International Dairy Journal 1999, 9:233-236.
    • (1999) International Dairy Journal , vol.9 , pp. 233-236
    • Corredig, M.1    Dalgleish, D.G.2
  • 7
    • 0001488378 scopus 로고
    • Thermal stability and functionality of whey proteins
    • DeVit J.N. Thermal stability and functionality of whey proteins. Journal of Dairy Science 1990, 73:3602-3612.
    • (1990) Journal of Dairy Science , vol.73 , pp. 3602-3612
    • DeVit, J.N.1
  • 8
    • 60849128243 scopus 로고    scopus 로고
    • Formation and properties of the whey protein/κ-casein complexes in heated skim milk-A review
    • Donato L., Guyomarc'h F. Formation and properties of the whey protein/κ-casein complexes in heated skim milk-A review. Dairy Science & Technology 2009, 89:3-29.
    • (2009) Dairy Science & Technology , vol.89 , pp. 3-29
    • Donato, L.1    Guyomarc'h, F.2
  • 9
    • 84921909528 scopus 로고    scopus 로고
    • Quantitation of proteins in milk and milk products
    • Springer, New York City, NY, USA, P.L.H. McSweeney, P.F. Fox (Eds.) Advanced dairy chemistry
    • Dupont D., Croguennec T., Brodkorb A., Kouaouci R. Quantitation of proteins in milk and milk products. Proteins: Basic aspects 2013, Vol. 1A:87-134. Springer, New York City, NY, USA. 4th ed. P.L.H. McSweeney, P.F. Fox (Eds.).
    • (2013) Proteins: Basic aspects , vol.1 A , pp. 87-134
    • Dupont, D.1    Croguennec, T.2    Brodkorb, A.3    Kouaouci, R.4
  • 10
    • 1242336776 scopus 로고    scopus 로고
    • Determination of the heat treatment undergone by milk by following the denaturation of alpha-lactalbumin with a biosensor
    • Dupont D., Rolet- Répécaud O., Muller-Renaud S. Determination of the heat treatment undergone by milk by following the denaturation of alpha-lactalbumin with a biosensor. Journal of Agricultural and Food Chemistry 2004, 52:677-681.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 677-681
    • Dupont, D.1    Rolet-Répécaud, O.2    Muller-Renaud, S.3
  • 12
    • 0032965144 scopus 로고    scopus 로고
    • Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins
    • Friedman M. Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins. Journal of Agricultural and Food Chemistry 1999, 47:1295-1319.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 1295-1319
    • Friedman, M.1
  • 13
    • 0032835191 scopus 로고    scopus 로고
    • Identification of low molar mass peptides released during sterilization of milk
    • Gaucheron F., Mollé D., Briard V., Léonil J. Identification of low molar mass peptides released during sterilization of milk. International Dairy Journal 1999, 9:515-521.
    • (1999) International Dairy Journal , vol.9 , pp. 515-521
    • Gaucheron, F.1    Mollé, D.2    Briard, V.3    Léonil, J.4
  • 14
    • 84949150774 scopus 로고    scopus 로고
    • Dairy chemistry and physics
    • University of Guelph, Guelph, Ontario, CA, Last accessed 22.08.14
    • Goff H.D. Dairy chemistry and physics. The dairy science and technology ebook 2014, University of Guelph, Guelph, Ontario, CA, Last accessed 22.08.14. https://www.uoguelph.ca/foodscience/book-page/milk-proteins.
    • (2014) The dairy science and technology ebook
    • Goff, H.D.1
  • 15
    • 0031582837 scopus 로고    scopus 로고
    • Possible implications of milk pasteurization on the manufacture and sensory quality of ripened cheese
    • Grappin R., Beuvier E. Possible implications of milk pasteurization on the manufacture and sensory quality of ripened cheese. International Dairy Journal 1997, 7:751-761.
    • (1997) International Dairy Journal , vol.7 , pp. 751-761
    • Grappin, R.1    Beuvier, E.2
  • 16
    • 0031935279 scopus 로고    scopus 로고
    • Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions
    • Havea P., Singh H., Creamer L.K., Campanella O.H. Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions. Journal of Dairy Research 1998, 65:79-91.
    • (1998) Journal of Dairy Research , vol.65 , pp. 79-91
    • Havea, P.1    Singh, H.2    Creamer, L.K.3    Campanella, O.H.4
  • 19
    • 33748463955 scopus 로고    scopus 로고
    • Optical biosensor analysis of the heat denaturation of bovine lactoferrin
    • Indyk H.E., McGrail I.J., Watene G.A., Filonzi E.L. Optical biosensor analysis of the heat denaturation of bovine lactoferrin. Food Chemistry 2007, 101:838-844.
    • (2007) Food Chemistry , vol.101 , pp. 838-844
    • Indyk, H.E.1    McGrail, I.J.2    Watene, G.A.3    Filonzi, E.L.4
  • 20
    • 0032801097 scopus 로고    scopus 로고
    • Characterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured a-lactalbumin
    • Jeanson S., Dupont D., Grattard N., Rolet-Répécaud O. Characterization of the heat treatment undergone by milk using two inhibition ELISAs for quantification of native and heat denatured a-lactalbumin. Journal of Agricultural and Food Chemistry 1999, 47:2249-2254.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , pp. 2249-2254
    • Jeanson, S.1    Dupont, D.2    Grattard, N.3    Rolet-Répécaud, O.4
  • 23
    • 35348885358 scopus 로고    scopus 로고
    • Inactivation-denaturation kinetics of bovine milk alkaline phosphatase during mild heating as determined by using a monoclonal antibody-based immunoassay
    • Levieux D., Geneix N., Levieux A. Inactivation-denaturation kinetics of bovine milk alkaline phosphatase during mild heating as determined by using a monoclonal antibody-based immunoassay. Journal of Dairy Research 2007, 74:296-301.
    • (2007) Journal of Dairy Research , vol.74 , pp. 296-301
    • Levieux, D.1    Geneix, N.2    Levieux, A.3
  • 24
  • 25
    • 52649177164 scopus 로고    scopus 로고
    • Detection of pH 4.6 insoluble β-lactoglobulin in heat-treated milk and Mozzarella cheese
    • Manzo C., Pizzano R., Addeo F. Detection of pH 4.6 insoluble β-lactoglobulin in heat-treated milk and Mozzarella cheese. Journal of Agricultural and Food Chemistry 2008, 56:7929-7933.
    • (2008) Journal of Agricultural and Food Chemistry , vol.56 , pp. 7929-7933
    • Manzo, C.1    Pizzano, R.2    Addeo, F.3
  • 26
    • 0026582439 scopus 로고
    • Carbohydrate binding specificity of monoclonal antibodies raised against lactose-protein Maillard adducts
    • Matsuda T., Ishiguro H., Ohkubo I., Sasaki M., Nakamura R. Carbohydrate binding specificity of monoclonal antibodies raised against lactose-protein Maillard adducts. The Journal of Biochemistry 1992, 111:383-387.
    • (1992) The Journal of Biochemistry , vol.111 , pp. 383-387
    • Matsuda, T.1    Ishiguro, H.2    Ohkubo, I.3    Sasaki, M.4    Nakamura, R.5
  • 27
    • 0019762671 scopus 로고
    • The Maillard reaction in food; a critical review from the nutritional standpoint
    • Pergamon Press, Oxford, UK, C. Eriksson (Ed.)
    • Mauron J. The Maillard reaction in food; a critical review from the nutritional standpoint. Maillard reactions in food 1981, 5-35. Pergamon Press, Oxford, UK. C. Eriksson (Ed.).
    • (1981) Maillard reactions in food , pp. 5-35
    • Mauron, J.1
  • 29
    • 33744502150 scopus 로고    scopus 로고
    • Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk
    • Patel H.A., Singh H., Anema S.G., Creamer L.K. Effects of heat and high hydrostatic pressure treatments on disulfide bonding interchanges among the proteins in skim milk. Journal of Agricultural and Food Chemistry 2006, 54:3409-3420.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , pp. 3409-3420
    • Patel, H.A.1    Singh, H.2    Anema, S.G.3    Creamer, L.K.4
  • 30
    • 84865147427 scopus 로고    scopus 로고
    • Occurrence of major whey proteins in the pH 4.6 insoluble protein fraction from UHT-treated milk
    • Pizzano R., Manzo C., Nicolai M.A., Addeo F. Occurrence of major whey proteins in the pH 4.6 insoluble protein fraction from UHT-treated milk. Journal of Agricultural and Food Chemistry 2012, 60:8044-8050.
    • (2012) Journal of Agricultural and Food Chemistry , vol.60 , pp. 8044-8050
    • Pizzano, R.1    Manzo, C.2    Nicolai, M.A.3    Addeo, F.4
  • 33
    • 0000081126 scopus 로고    scopus 로고
    • Specific detection of the Amadori compounds in milk by using polyclonal antibodies raised against a lactosylated peptide
    • Pizzano R., Nicolai M.A., Siciliano R., Addeo F. Specific detection of the Amadori compounds in milk by using polyclonal antibodies raised against a lactosylated peptide. Journal of Agricultural and Food Chemistry 1998, 46:5373-5379.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , pp. 5373-5379
    • Pizzano, R.1    Nicolai, M.A.2    Siciliano, R.3    Addeo, F.4
  • 35
    • 0030037664 scopus 로고    scopus 로고
    • Determination of denatured serum proteins in the casein fraction of heat-treated milk by capillary electrophoresis
    • Recio I., Olieman C. Determination of denatured serum proteins in the casein fraction of heat-treated milk by capillary electrophoresis. Electrophoresis 1996, 17:1228-1233.
    • (1996) Electrophoresis , vol.17 , pp. 1228-1233
    • Recio, I.1    Olieman, C.2
  • 36
    • 0028567981 scopus 로고
    • Amodel for the denaturation and aggregation of β-lactoglobulin
    • Roefs S.P.F.M., De Kruif K.G. Amodel for the denaturation and aggregation of β-lactoglobulin. European Journal of Biochemistry 1994, 226:883-889.
    • (1994) European Journal of Biochemistry , vol.226 , pp. 883-889
    • Roefs, S.P.F.M.1    De Kruif, K.G.2
  • 37
    • 0001770281 scopus 로고
    • Heat-induced changes in casein, including interactions with whey proteins
    • International Dairy Federation, Brussels, BE, P.F. Fox (Ed.)
    • Singh H. Heat-induced changes in casein, including interactions with whey proteins. Heat-induced changes in milk (IDF special issue 9501 1995, 86-104. International Dairy Federation, Brussels, BE. P.F. Fox (Ed.).
    • (1995) Heat-induced changes in milk (IDF special issue 9501 , pp. 86-104
    • Singh, H.1
  • 38
    • 84976097159 scopus 로고
    • Rennet coagulation of heated milk: influence of pH adjustment before or after heating
    • Singh H., Shalabi S.I., Fox P.F., Flynn A., Barry A. Rennet coagulation of heated milk: influence of pH adjustment before or after heating. Journal of Dairy Research 1988, 55:205-215.
    • (1988) Journal of Dairy Research , vol.55 , pp. 205-215
    • Singh, H.1    Shalabi, S.I.2    Fox, P.F.3    Flynn, A.4    Barry, A.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.