메뉴 건너뛰기




Volumn 121, Issue 3, 2010, Pages 803-808

Distinction of different heat-treated bovine milks by native-PAGE fingerprinting of their whey proteins

Author keywords

Heat treatment; Milk; Native PAGE; Whey proteins

Indexed keywords

ALPHA LACTALBUMIN; BETA LACTOGLOBULIN; IMMUNOGLOBULIN; MILK PROTEIN; SERUM ALBUMIN;

EID: 77649343083     PISSN: 03088146     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodchem.2009.12.088     Document Type: Article
Times cited : (30)

References (28)
  • 1
    • 29344447987 scopus 로고    scopus 로고
    • Texture and flavour development in Ras cheese made from raw and pasteurised milk
    • Awad S. Texture and flavour development in Ras cheese made from raw and pasteurised milk. Food Chemistry 97 (2006) 394-400
    • (2006) Food Chemistry , vol.97 , pp. 394-400
    • Awad, S.1
  • 2
    • 0002269721 scopus 로고    scopus 로고
    • Bovine beta-lactoglobulin and its variants: A three-dimensional perspective
    • Brussels. Belgium: International Dairy Federation
    • Bewley, M. C., Baker, E. N., Qin, B. Y., Jameson, G. B., & Sawyer, L. (1997). Bovine beta-lactoglobulin and its variants: A three-dimensional perspective. In Food composition (pp. 100-109). Brussels. Belgium: International Dairy Federation.
    • (1997) Food composition , pp. 100-109
    • Bewley, M.C.1    Baker, E.N.2    Qin, B.Y.3    Jameson, G.B.4    Sawyer, L.5
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle protein-dry binding
    • Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle protein-dry binding. Analytical Biochemistry 72 (1976) 248-254
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 0344256463 scopus 로고    scopus 로고
    • Multidimensional analysis of denatured milk proteins by hydrophobic interaction chromatography coupled to a dynamic surface tension detector
    • Bramanti E., Quigley W.W.C., Sortino C., Beni F., Onor M., Raspi G., and Synovec R.E. Multidimensional analysis of denatured milk proteins by hydrophobic interaction chromatography coupled to a dynamic surface tension detector. Journal of Chromatography A 1023 (2004) 79-91
    • (2004) Journal of Chromatography A , vol.1023 , pp. 79-91
    • Bramanti, E.1    Quigley, W.W.C.2    Sortino, C.3    Beni, F.4    Onor, M.5    Raspi, G.6    Synovec, R.E.7
  • 7
    • 0342562818 scopus 로고    scopus 로고
    • Sodium dodecyl sulfate polyacrylamide gel electrophoresis of beta-lactoglobulin variants A, B, and C: Relative mobilities of heated and unheated samples
    • Brussels. Bruxelles. Belgium: International Dairy Federation
    • Brittan, H., Norris, G. E., Lowe, R., Kitson, T. M., & Hill, J. P. (1997). Sodium dodecyl sulfate polyacrylamide gel electrophoresis of beta-lactoglobulin variants A, B, and C: Relative mobilities of heated and unheated samples. In Milk protein polymorphism (pp. 212-216). Brussels. Bruxelles. Belgium: International Dairy Federation.
    • (1997) Milk protein polymorphism , pp. 212-216
    • Brittan, H.1    Norris, G.E.2    Lowe, R.3    Kitson, T.M.4    Hill, J.P.5
  • 8
    • 0037929549 scopus 로고    scopus 로고
    • Effects of polymorph milk proteins on the individual milk protein content of Holstein-Friesian and Simmental cows
    • Cardak A.D., Bartenschlager H., and Geldermann H. Effects of polymorph milk proteins on the individual milk protein content of Holstein-Friesian and Simmental cows. Milchwissenschaft 58 (2003) 235-238
    • (2003) Milchwissenschaft , vol.58 , pp. 235-238
    • Cardak, A.D.1    Bartenschlager, H.2    Geldermann, H.3
  • 9
    • 4243163216 scopus 로고    scopus 로고
    • Distinction between dry and raw milk using monoclonal antibodies prepared against dry milk proteins
    • Chen W.L., Huang M.T., Liu H.C., Li C.W., and Mao S.J.T. Distinction between dry and raw milk using monoclonal antibodies prepared against dry milk proteins. Journal of Dairy Science 87 (2004) 2720-2729
    • (2004) Journal of Dairy Science , vol.87 , pp. 2720-2729
    • Chen, W.L.1    Huang, M.T.2    Liu, H.C.3    Li, C.W.4    Mao, S.J.T.5
  • 10
    • 0032867758 scopus 로고    scopus 로고
    • The mechanisms of the heat-induced interaction of whey proteins with casein micelle in milk
    • Corredig M., and Dalgleish D.G. The mechanisms of the heat-induced interaction of whey proteins with casein micelle in milk. International Dairy Journal 9 (1999) 233-236
    • (1999) International Dairy Journal , vol.9 , pp. 233-236
    • Corredig, M.1    Dalgleish, D.G.2
  • 11
    • 1242336776 scopus 로고    scopus 로고
    • Determination of the heat treatment undergone by milk by following the denaturation of α-lactalbumin with a biosensor
    • Dupont D., Rolet-Répécaud O., and Muller-Renaud S. Determination of the heat treatment undergone by milk by following the denaturation of α-lactalbumin with a biosensor. Journal of Agricultural and Food Chemistry 52 (2004) 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
  • 14
    • 0036319042 scopus 로고    scopus 로고
    • Detection of bovine milk in ovine yoghurt by electrophoresis of para-κ-casein
    • Kaminarides S.E., and Koukiassa P. Detection of bovine milk in ovine yoghurt by electrophoresis of para-κ-casein. Food Chemistry 78 (2002) 53-55
    • (2002) Food Chemistry , vol.78 , pp. 53-55
    • Kaminarides, S.E.1    Koukiassa, P.2
  • 15
    • 0039023206 scopus 로고
    • The primary structure of ovine β-lactoglobulin
    • Kolde H.J., and Braunitzer G. The primary structure of ovine β-lactoglobulin. Milchwissenschaft 38 (1983) 70-72
    • (1983) Milchwissenschaft , vol.38 , pp. 70-72
    • Kolde, H.J.1    Braunitzer, G.2
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli U.K. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970) 680-685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 57749118622 scopus 로고    scopus 로고
    • Comparative study on heat stability and functionality of camel and bovine milk whey proteins
    • Laleye L.C., Jobe B., and Wasesa A.A.H. Comparative study on heat stability and functionality of camel and bovine milk whey proteins. Journal of Dairy Science 91 (2008) 4527-4534
    • (2008) Journal of Dairy Science , vol.91 , pp. 4527-4534
    • Laleye, L.C.1    Jobe, B.2    Wasesa, A.A.H.3
  • 18
    • 0034030911 scopus 로고    scopus 로고
    • Effect of pH on the thermal denaturation of whey proteins in milk
    • Law A.J., and Leaver J. Effect of pH on the thermal denaturation of whey proteins in milk. Journal of Agricultural and Food Chemistry 48 (2000) 672-679
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 672-679
    • Law, A.J.1    Leaver, J.2
  • 20
    • 36649009934 scopus 로고    scopus 로고
    • Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry
    • Losito I., Carbonara T., Monaci L., and Palmisano F. Evaluation of the thermal history of bovine milk from the lactosylation of whey proteins: an investigation by liquid chromatography-electrospray ionization mass spectrometry. Analytical and Bioanalytical Chemistry 389 (2007) 2065-2074
    • (2007) Analytical and Bioanalytical Chemistry , vol.389 , pp. 2065-2074
    • Losito, I.1    Carbonara, T.2    Monaci, L.3    Palmisano, F.4
  • 23
    • 33646588670 scopus 로고    scopus 로고
    • Effects of heat treatment and high pressure on the subsequent lactosylation of β-lactoglobulin
    • Rada-Mendoza M., Villamiel M., Molina E., and Olano A. Effects of heat treatment and high pressure on the subsequent lactosylation of β-lactoglobulin. Food Chemisty 99 (2006) 651-655
    • (2006) Food Chemisty , vol.99 , pp. 651-655
    • Rada-Mendoza, M.1    Villamiel, M.2    Molina, E.3    Olano, A.4
  • 24
    • 0034776414 scopus 로고    scopus 로고
    • Open-tubular capillary electrochromatography of bovine β-lactoglobulin variants A and B using an aptamer stationary phase
    • Rehder M.A., and McGown L.B. Open-tubular capillary electrochromatography of bovine β-lactoglobulin variants A and B using an aptamer stationary phase. Electrophoresis 22 (2001) 3759-3764
    • (2001) Electrophoresis , vol.22 , pp. 3759-3764
    • Rehder, M.A.1    McGown, L.B.2
  • 25
    • 0033013484 scopus 로고    scopus 로고
    • Characterisation of milk samples with various whey protein contents by pyrolysis-mass spectrometry (Py-MS)
    • Schmidt M.A.E., Radovic B.S., Lipp M., Harzer G., and Anklam E. Characterisation of milk samples with various whey protein contents by pyrolysis-mass spectrometry (Py-MS). Food Chemistry 65 (1999) 123-128
    • (1999) Food Chemistry , vol.65 , pp. 123-128
    • Schmidt, M.A.E.1    Radovic, B.S.2    Lipp, M.3    Harzer, G.4    Anklam, E.5
  • 26
    • 0034422798 scopus 로고    scopus 로고
    • Preparative separation and characterization of beta-lactoglobulin genetic variants A and B from bovine milk
    • Valkonen K.H., Marttinen N., and Alatossava T. Preparative separation and characterization of beta-lactoglobulin genetic variants A and B from bovine milk. Milchwissenschaft 55 (2000) 126-129
    • (2000) Milchwissenschaft , vol.55 , pp. 126-129
    • Valkonen, K.H.1    Marttinen, N.2    Alatossava, T.3
  • 27
    • 2342530398 scopus 로고    scopus 로고
    • Evaluation of cheese authenticity and proteolysis by HPLC and urea-polyacrylamide gel electrophoresis
    • Veloso A.C.A., Teixeira N., Peres A.M., Mendonca A., and Ferreira I.M.P.L.V.O. Evaluation of cheese authenticity and proteolysis by HPLC and urea-polyacrylamide gel electrophoresis. Food Chemistry 87 (2004) 289-295
    • (2004) Food Chemistry , vol.87 , pp. 289-295
    • Veloso, A.C.A.1    Teixeira, N.2    Peres, A.M.3    Mendonca, A.4    Ferreira, I.M.P.L.V.O.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.