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Volumn 63, Issue 3, 2008, Pages 93-99

Cross-linking of proteins and other changes in UHT milk during storage at different temperatures

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EID: 62449283202     PISSN: 00049433     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (36)

References (27)
  • 1
    • 84972029240 scopus 로고
    • Properties of aseptically packed ultra-high-temperature milk. III. Formation of polymerized protein during storage at various temperatures
    • Andrews, A.T. (1975), Properties of aseptically packed ultra-high-temperature milk. III. Formation of polymerized protein during storage at various temperatures. J. Dairy Res. 42, 89-99.
    • (1975) J. Dairy Res , vol.42 , pp. 89-99
    • Andrews, A.T.1
  • 2
    • 0032867758 scopus 로고    scopus 로고
    • The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk
    • Corredig, M. and Dalgleish, D. (1999), The mechanisms of the heat-induced interaction of whey proteins with casein micelles in milk. Int. Dairy J. 9, 233-236.
    • (1999) Int. Dairy J , vol.9 , pp. 233-236
    • Corredig, M.1    Dalgleish, D.2
  • 3
    • 0010569105 scopus 로고
    • Protein-protein interactions in food materials
    • Ed. A.G. Gaonkar, Marcel Dekker, NewYork, pp
    • Dalgleish, D.G. and Hunt, J.A. (1995), Protein-protein interactions in food materials. In Ingredient Interactions. Effects on Food Quality (Ed. A.G. Gaonkar). Marcel Dekker, NewYork, pp. 199-233.
    • (1995) Ingredient Interactions. Effects on Food Quality , pp. 199-233
    • Dalgleish, D.G.1    Hunt, J.A.2
  • 4
    • 0029994516 scopus 로고    scopus 로고
    • Breaking the curse of the AGEs
    • Drickamer, K. (1996), Breaking the curse of the AGEs. Nature 382,211-212.
    • (1996) Nature , vol.382 , pp. 211-212
    • Drickamer, K.1
  • 5
    • 0013087662 scopus 로고
    • Importance of cross-linking reactions in proteins
    • Feeney, R.E. and Whitaker, J.R. (1988), Importance of cross-linking reactions in proteins. Adv. Cereal Sci. Technol. 9,21-43.
    • (1988) Adv. Cereal Sci. Technol , vol.9 , pp. 21-43
    • Feeney, R.E.1    Whitaker, J.R.2
  • 6
    • 2842525944 scopus 로고    scopus 로고
    • Food browning and its prevention: An overview
    • Friedman, M. (1996), Food browning and its prevention: An overview. J. Agric. Food Chem. 44, 631-653.
    • (1996) J. Agric. Food Chem , vol.44 , pp. 631-653
    • Friedman, M.1
  • 7
    • 0032965144 scopus 로고    scopus 로고
    • Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins
    • Friedman, M. (1999), Chemistry, biochemistry, nutrition, and microbiology of lysinoalanine, lanthionine, and histidinoalanine in food and other proteins. J. Agric. Food Chem. 47, 1295-1319.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 1295-1319
    • Friedman, M.1
  • 8
    • 34347233365 scopus 로고    scopus 로고
    • Effects of storage temperature on physico-chemical characteristics of semi-skimmed UHT milk
    • Gaucher, I, Molle, D., Gagnaire, V and Gaucheron, F. (2008), Effects of storage temperature on physico-chemical characteristics of semi-skimmed UHT milk. Food Hydrocolloids 22, 130-143.
    • (2008) Food Hydrocolloids , vol.22 , pp. 130-143
    • Gaucher, I.1    Molle, D.2    Gagnaire, V.3    Gaucheron, F.4
  • 9
    • 0036980061 scopus 로고    scopus 로고
    • Protein-protein crosslinking in food: Methods, consequences, applications
    • Gerrard, J.A. (2002), Protein-protein crosslinking in food: methods, consequences, applications. Trends Food Sci. Technol. 13,391-399.
    • (2002) Trends Food Sci. Technol , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 10
    • 0037586322 scopus 로고
    • Effect of raw milk quality on ultra-high temperature processed milk
    • Gillis, W.T., Cartledge, M.F., Rodriguez, I.R. and Suares, E.J. (1985), Effect of raw milk quality on ultra-high temperature processed milk. J. Dairy Sci. 68, 2875-2879.
    • (1985) J. Dairy Sci , vol.68 , pp. 2875-2879
    • Gillis, W.T.1    Cartledge, M.F.2    Rodriguez, I.R.3    Suares, E.J.4
  • 11
    • 62449149464 scopus 로고    scopus 로고
    • Henle, T., Walter, A.W. and Klostermeyer, H. (1996), Irreversible crosslinking of casein during storage of UHT-treated skim milk. In Heat Treatments and Alternative Methods. International Dairy Federation Special Issue 9602, International Dairy Federation, Brussels, Belgium, pp. 290-298.
    • Henle, T., Walter, A.W. and Klostermeyer, H. (1996), Irreversible crosslinking of casein during storage of UHT-treated skim milk. In Heat Treatments and Alternative Methods. International Dairy Federation Special Issue 9602, International Dairy Federation, Brussels, Belgium, pp. 290-298.
  • 12
    • 0001429097 scopus 로고    scopus 로고
    • Linking proteins using the Maillard reaction and the implications for food processors
    • Eds. J. O'Brien, H.E. Nursten, M. James, C. Crabbe and J.M. Ames, Royal Society of Chemistry, Cambridge, UK, pp
    • Hill, S. and Easa, A.M. (1998), Linking proteins using the Maillard reaction and the implications for food processors. In The Maillard Reaction in Foods and Medicine. (Eds. J. O'Brien, H.E. Nursten, M. James, C. Crabbe and J.M. Ames). Royal Society of Chemistry, Cambridge, UK, pp. 133-138.
    • (1998) The Maillard Reaction in Foods and Medicine , pp. 133-138
    • Hill, S.1    Easa, A.M.2
  • 13
    • 85010247744 scopus 로고
    • Studies on milk proteins II. Colorimetric determination of the partial hydrolysis of the proteins in milk
    • Hull, M.E. (1947), Studies on milk proteins II. Colorimetric determination of the partial hydrolysis of the proteins in milk. J. Dairy Sci. 30, 881-884.
    • (1947) J. Dairy Sci , vol.30 , pp. 881-884
    • Hull, M.E.1
  • 14
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K. (1970), Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 15
    • 0042736339 scopus 로고    scopus 로고
    • On the influence of non-enzymatic crosslinking of caseins on the gel strength of yogurt
    • Lauber, S.D., Klostermeyer, H. and Henle, Th. (2001), On the influence of non-enzymatic crosslinking of caseins on the gel strength of yogurt. Nahrung/Food 45, 215-217.
    • (2001) Nahrung/Food , vol.45 , pp. 215-217
    • Lauber, S.D.1    Klostermeyer, H.2    Henle, T.3
  • 16
    • 0242691177 scopus 로고    scopus 로고
    • Cross-linking of proteins by Maillard processes - characterization and detection of a lysine-arginine cross-link derived from D-glucose
    • Lederer, M.O. and Buhler, H.P. (1999), Cross-linking of proteins by Maillard processes - characterization and detection of a lysine-arginine cross-link derived from D-glucose. Bioorg. Med. Chem. 7, 1081-1088.
    • (1999) Bioorg. Med. Chem , vol.7 , pp. 1081-1088
    • Lederer, M.O.1    Buhler, H.P.2
  • 17
    • 62449157815 scopus 로고    scopus 로고
    • McMahon, D.J. (1996), Age-gelation of UHT milk: Changes that occur during storage on shelf-life and the mechanism by which age-gelation occurs. In Heat Treatments and Alternative Methods. International Dairy Federation Special Issue 9602, International Dairy Federation, Brussels, Belgium, pp 315-325.
    • McMahon, D.J. (1996), Age-gelation of UHT milk: Changes that occur during storage on shelf-life and the mechanism by which age-gelation occurs. In Heat Treatments and Alternative Methods. International Dairy Federation Special Issue 9602, International Dairy Federation, Brussels, Belgium, pp 315-325.
  • 18
    • 85025791486 scopus 로고
    • Effect of storage temperature on age gelation of ultra-high temperature milk processed by direct and indirect heating systems
    • Manji, B., Kakuda, Y. and Arnott, D.R. (1986), Effect of storage temperature on age gelation of ultra-high temperature milk processed by direct and indirect heating systems. J. Dairy Sci. 69, 2994-3001.
    • (1986) J. Dairy Sci , vol.69 , pp. 2994-3001
    • Manji, B.1    Kakuda, Y.2    Arnott, D.R.3
  • 19
    • 84975945801 scopus 로고
    • Chemical changes in ultra-heat-treated milk during storage. II. Lactuloselysine and fructoselysine formation by the Maillard reaction
    • Moiler, A.B., Andrews, A.T. and Cheeseman, G.C. (1977), Chemical changes in ultra-heat-treated milk during storage. II. Lactuloselysine and fructoselysine formation by the Maillard reaction. J. Dairy Res. 44, 268-277.
    • (1977) J. Dairy Res , vol.44 , pp. 268-277
    • Moiler, A.B.1    Andrews, A.T.2    Cheeseman, G.C.3
  • 20
    • 0012186582 scopus 로고
    • Thermal denaturation of whey protein
    • Pearce, R.J. (1989), Thermal denaturation of whey protein. IDF Bull. 238, 17-23.
    • (1989) IDF Bull , vol.238 , pp. 17-23
    • Pearce, R.J.1
  • 21
  • 22
    • 0023956290 scopus 로고
    • Storage stability and some nutritional aspects of milk powders and ultra high temperature products at high ambient temperature
    • Renner, E. (1988), Storage stability and some nutritional aspects of milk powders and ultra high temperature products at high ambient temperature. J. Dairy Res. 55, 125-142.
    • (1988) J. Dairy Res , vol.55 , pp. 125-142
    • Renner, E.1
  • 23
    • 0000959875 scopus 로고
    • Modification of food proteins by covalent cross-linking
    • Singh, H. (1991), Modification of food proteins by covalent cross-linking. Trends Food Sci. Technol. 2 196-200.
    • (1991) Trends Food Sci. Technol , vol.2 , pp. 196-200
    • Singh, H.1
  • 24
    • 0001347880 scopus 로고
    • Heat stability of milk: Aggregation and dissociation of protein at ultra-high temperatures
    • Singh, H. and Latham, J. (1993), Heat stability of milk: Aggregation and dissociation of protein at ultra-high temperatures. Int. Dairy J. 3, 225-235.
    • (1993) Int. Dairy J , vol.3 , pp. 225-235
    • Singh, H.1    Latham, J.2
  • 25
    • 0032839314 scopus 로고    scopus 로고
    • Heat-induced deamidation, dephosphorylation and breakdown of caseinate
    • van Boekel, M.A.J.S. (1999), Heat-induced deamidation, dephosphorylation and breakdown of caseinate. Int. Dairy J. 9,237-241.
    • (1999) Int. Dairy J , vol.9 , pp. 237-241
    • van Boekel, M.A.J.S.1
  • 26
    • 0027636472 scopus 로고
    • Role of protein and lactose interactions in the age gelation of ultra-high-temperature processed concentrated skim milk
    • Venkatachalam, N., McMahon, D.J. and Savello, P.A. (1993), Role of protein and lactose interactions in the age gelation of ultra-high-temperature processed concentrated skim milk. J. Dairy Sci. 76, 1882-1894.
    • (1993) J. Dairy Sci , vol.76 , pp. 1882-1894
    • Venkatachalam, N.1    McMahon, D.J.2    Savello, P.A.3
  • 27
    • 85005521340 scopus 로고
    • Inactivation of heat resistant proteases in normal UHT sterilized skim milk by a low temperature treatment
    • West F.B., Adams D.M. and Speck M.L. (1978), Inactivation of heat resistant proteases in normal UHT sterilized skim milk by a low temperature treatment. J. Dairy Sci. 61, 1078-1084.
    • (1978) J. Dairy Sci , vol.61 , pp. 1078-1084
    • West, F.B.1    Adams, D.M.2    Speck, M.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.