메뉴 건너뛰기




Volumn 66, Issue 1, 2013, Pages 1-6

Effect of lactose on cross-linking of milk proteins during heat treatments

Author keywords

Heat treatment; Lysinoalanine; Maillard reactions; Milk proteins cross linking

Indexed keywords


EID: 84872272637     PISSN: 1364727X     EISSN: 14710307     Source Type: Journal    
DOI: 10.1111/j.1471-0307.2012.00878.x     Document Type: Article
Times cited : (42)

References (32)
  • 1
    • 62449283202 scopus 로고    scopus 로고
    • Cross-linking of proteins in UHT milk during storage at different temperatures
    • Al-Saadi M S J and Deeth C H (2008) Cross-linking of proteins in UHT milk during storage at different temperatures. Australian Journal of Dairy Technology 63 93-99.
    • (2008) Australian Journal of Dairy Technology , vol.63 , pp. 93-99
    • Al-Saadi, M.S.J.1    Deeth, C.H.2
  • 2
    • 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. Journal of Dairy Research 42 89-99.
    • (1975) Journal of Dairy Research , vol.42 , pp. 89-99
    • Andrews, A.T.1
  • 3
    • 0004312989 scopus 로고
    • AOAC (Association of Official Analytical Chemists) 13th edn. Washington, DC: Association of Official Analytical Chemists.
    • AOAC (Association of Official Analytical Chemists) (1980) Official Methods of Analysis, 13th edn. pp 47021-47023. Washington, DC: Association of Official Analytical Chemists.
    • (1980) Official Methods of Analysis , pp. 47021-47023
  • 5
    • 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. International Dairy Journal 9 237-241.
    • (1999) International Dairy Journal , vol.9 , pp. 237-241
    • van Boekel, M.A.J.S.1
  • 6
    • 0001668243 scopus 로고
    • Damage to lysine in food processing: its measurement and significance
    • Carpenter K J (1973) Damage to lysine in food processing: its measurement and significance. Nutritional Abstract Review 43 423-451.
    • (1973) Nutritional Abstract Review , vol.43 , pp. 423-451
    • Carpenter, K.J.1
  • 7
    • 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. International Dairy Journal 9 233-236.
    • (1999) International Dairy Journal , vol.9 , pp. 233-236
    • Corredig, M.1    Dalgleish, D.2
  • 8
    • 0037386648 scopus 로고    scopus 로고
    • Updating on the lysinoalanine content of commercial infant formulae and beicost products
    • D'Agostina A, Boschin G, Rinaldi A and Arnoldi A (2003) Updating on the lysinoalanine content of commercial infant formulae and beicost products. Food Chemistry 4 483-488.
    • (2003) Food Chemistry , vol.4 , pp. 483-488
    • D'Agostina, A.1    Boschin, G.2    Rinaldi, A.3    Arnoldi, A.4
  • 9
    • 0010569105 scopus 로고
    • Protein-protein interactions in food materials
    • Gaonkar A G, ed. New York: Marcel Dekker.
    • Dalgleish D G and Hunt J A (1995) Protein-protein interactions in food materials. In Ingredient Inter-Actions. Effects on Food Quality, pp 199-233. Gaonkar A G, ed. New York: Marcel Dekker.
    • (1995) Ingredient Inter-Actions. Effects on Food Quality , pp. 199-233
    • Dalgleish, D.G.1    Hunt, J.A.2
  • 10
    • 34447498699 scopus 로고    scopus 로고
    • Forty years of furosine - forty years of using Maillard reaction products as indicators of the nutritional quality of foods
    • Erbersdobler H F and Somoza V (2007) Forty years of furosine - forty years of using Maillard reaction products as indicators of the nutritional quality of foods. Molecular Nutrition and Food Research 51 423-430.
    • (2007) Molecular Nutrition and Food Research , vol.51 , pp. 423-430
    • Erbersdobler, H.F.1    Somoza, V.2
  • 11
    • 0033820529 scopus 로고    scopus 로고
    • Determination of lysinoalanine in foods containing milk protein by high performance chromatography after derivatisation with dansyl chloride
    • Faist V, Drusch S, Kiesner C, Elmadfa I and Erbersdobler H F (2000) Determination of lysinoalanine in foods containing milk protein by high performance chromatography after derivatisation with dansyl chloride. International Dairy Journal 10 339-346.
    • (2000) International Dairy Journal , vol.10 , pp. 339-346
    • Faist, V.1    Drusch, S.2    Kiesner, C.3    Elmadfa, I.4    Erbersdobler, H.F.5
  • 13
    • 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. Journal of Agriculture and Food Chemistry 47 1295-1319.
    • (1999) Journal of Agriculture and Food Chemistry , vol.47 , pp. 1295-1319
    • Friedman, M.1
  • 14
    • 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 in Food Science and Technology 13 391-399.
    • (2002) Trends in Food Science and Technology , vol.13 , pp. 391-399
    • Gerrard, J.A.1
  • 15
    • 0003358166 scopus 로고
    • Racemization of amino acid residues in casein roasted with glucose and or methyl linoleate
    • Hayase F, Fato H and Fujimakim M (1979) Racemization of amino acid residues in casein roasted with glucose and or methyl linoleate. Agricultural and Biological Chemistry 43 2459-2465.
    • (1979) Agricultural and Biological Chemistry , vol.43 , pp. 2459-2465
    • Hayase, F.1    Fato, H.2    Fujimakim, M.3
  • 16
    • 0001429097 scopus 로고    scopus 로고
    • Linking proteins using the Maillard reaction and the implications for food processors
    • O'Brien J, Nursten H E, James M, Crabbe C, Ames J M, eds. Cambridge, UK: Royal Society of Chemistry.
    • 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. pp 133-138. O'Brien J, Nursten H E, James M, Crabbe C, Ames J M, eds. Cambridge, UK: Royal Society of Chemistry.
    • (1998) The Maillard Reaction in Foods and Medicine , pp. 133-138
    • Hill, S.1    Easa, A.M.2
  • 17
    • 0000547124 scopus 로고
    • Preparation and properties of a salt solution which simulates milk ultra-filtrate
    • Jenness R and Koops J (1962) Preparation and properties of a salt solution which simulates milk ultra-filtrate. The Netherlands Milk and Dairy Journal 3 153-164.
    • (1962) The Netherlands Milk and Dairy Journal , vol.3 , pp. 153-164
    • Jenness, R.1    Koops, J.2
  • 18
    • 0031435678 scopus 로고    scopus 로고
    • Proteolysis and storage stability of UHT milk as influenced by milk plasmin activity, plasmin/β-lactoglobulin complexation, plasminogen activation and somatic cell count
    • Kelly A L and Foley J (1997) Proteolysis and storage stability of UHT milk as influenced by milk plasmin activity, plasmin/β-lactoglobulin complexation, plasminogen activation and somatic cell count. International Dairy Journal 7 411-420.
    • (1997) International Dairy Journal , vol.7 , pp. 411-420
    • Kelly, A.L.1    Foley, J.2
  • 19
    • 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
  • 20
    • 0042736339 scopus 로고    scopus 로고
    • On the influence of nonenzymatic crosslinking of caseins on the gel strength of yogurt
    • Lauber S D, Klostermeyer H and Henle T (2001) On the influence of nonenzymatic 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
  • 22
    • 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. Bioorganic and Medicinal Chemistry 7 1081-1088.
    • (1999) Bioorganic and Medicinal Chemistry , vol.7 , pp. 1081-1088
    • Lederer, M.O.1    Buhler, H.P.2
  • 23
    • 0002458628 scopus 로고    scopus 로고
    • Age-gelation of UHT milk: Changes that occur during storage on shelf-life and the mechanism by which age-gelation occurs
    • International Dairy Federation Special Issue 9602, Brussels, Belgium: International Dairy Federation.
    • 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, pp 315-325. Brussels, Belgium: International Dairy Federation.
    • (1996) Heat Treatments and Alternative Methods , pp. 315-325
    • McMahon, D.J.1
  • 24
    • 84975945801 scopus 로고
    • Chemical changes in ultraheat-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 ultraheat-treated milk during storage. II. Lactuloselysine and fructoselysine formation by the Maillard reaction. Journal Dairy Research 44 268-277.
    • (1977) Journal Dairy Research , vol.44 , pp. 268-277
    • Moiler, A.B.1    Andrews, A.T.2    Cheeseman, G.C.3
  • 25
    • 1542708098 scopus 로고    scopus 로고
    • Sensitive determination of lysinoalanine for distinguishing natural from imitation Mozzarella cheese
    • Pellegrino L, Resmini P, De Noni I and Masotti F (1996) Sensitive determination of lysinoalanine for distinguishing natural from imitation Mozzarella cheese. Journal of Dairy Science 79 725-734.
    • (1996) Journal of Dairy Science , vol.79 , pp. 725-734
    • Pellegrino, L.1    Resmini, P.2    De Noni, I.3    Masotti, F.4
  • 27
    • 75149162776 scopus 로고    scopus 로고
    • Effect of heat treatment on milk protein functionality at emulsion interfaces. A review
    • Raikos V (2010) Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocolloids 24 259-265.
    • (2010) Food Hydrocolloids , vol.24 , pp. 259-265
    • Raikos, V.1
  • 28
    • 0041865238 scopus 로고
    • Heat and alkaline damage to proteins: racemization and lysinoalanine formation
    • Schwass D E and Finley J F (1984) Heat and alkaline damage to proteins: racemization and lysinoalanine formation. Journal of Agriculture and Food Chemistry 32 1377-1382.
    • (1984) Journal of Agriculture and Food Chemistry , vol.32 , pp. 1377-1382
    • Schwass, D.E.1    Finley, J.F.2
  • 29
    • 0000959875 scopus 로고
    • Modification of food proteins by covalent cross-linking
    • Singh H (1991) Modification of food proteins by covalent cross-linking. Trends in Food Science and Technology 2 196-200.
    • (1991) Trends in Food Science and Technology , vol.2 , pp. 196-200
    • Singh, H.1
  • 30
    • 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. Journal of Dairy Science 76 1882-1894.
    • (1993) Journal of Dairy Science , vol.76 , pp. 1882-1894
    • Venkatachalam, N.1    McMahon, D.J.2    Savello, P.A.3
  • 31
    • 0026320363 scopus 로고
    • Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins
    • Wright H T (1991) Nonenzymatic deamidation of asparaginyl and glutaminyl residues in proteins. Critical Reviews in Biochemistry and Molecular Biology 26 1-52.
    • (1991) Critical Reviews in Biochemistry and Molecular Biology , vol.26 , pp. 1-52
    • Wright, H.T.1
  • 32
    • 0342420522 scopus 로고
    • New cross-links in alkali-treated wool
    • Ziegler K L (1964) New cross-links in alkali-treated wool. Journal of Biological Chemistry 239 2713-2714.
    • (1964) Journal of Biological Chemistry , vol.239 , pp. 2713-2714
    • Ziegler, K.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.