메뉴 건너뛰기




Volumn 87, Issue 6, 2007, Pages 535-554

Whey protein interactions in acidic cold-set gels at different pH values

Author keywords

Cold gelation; Glucono delta lactone; Protein interactions; Whey proteins

Indexed keywords


EID: 41849095663     PISSN: 19585586     EISSN: 19585594     Source Type: Journal    
DOI: 10.1051/lait:2007032     Document Type: Article
Times cited : (40)

References (32)
  • 2
    • 0038362143 scopus 로고    scopus 로고
    • Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels
    • Alting A.C., Hamer R.J., de Kruif C.G., Paques M., Visschers R.W., Number of thiol groups rather than the size of the aggregates determines the hardness of cold set whey protein gels, Food Hydrocoll. 17 (2003) 469-479.
    • (2003) Food Hydrocoll , vol.17 , pp. 469-479
    • Alting, A.C.1    Hamer, R.J.2    de Kruif, C.G.3    Paques, M.4    Visschers, R.W.5
  • 4
    • 0002420091 scopus 로고    scopus 로고
    • Determining water and fat holding
    • Hall G.M, Ed, Chapman & Hall, London
    • Barbut S., Determining water and fat holding, in: Hall G.M. (Ed.), Methods of testing prote in functionality, Chapman & Hall, London, 1996, pp. 187-225.
    • (1996) Methods of testing prote in functionality , pp. 187-225
    • Barbut, S.1
  • 5
    • 30744434157 scopus 로고    scopus 로고
    • The effect of the glucono-delta-lactone/caseinate ratio on sodium casemate gelation
    • Braga A.L.M., Menossi M., Cunha R.L., The effect of the glucono-delta-lactone/caseinate ratio on sodium casemate gelation, Int. Dairy J. 16 (2006) 389-398.
    • (2006) Int. Dairy J , vol.16 , pp. 389-398
    • Braga, A.L.M.1    Menossi, M.2    Cunha, R.L.3
  • 6
    • 0029329199 scopus 로고
    • Thermal isoelectric precipitation of Alpha-Lactalbumin from a whey-protein concentrate - influence of protein-calcium complexation
    • Bramaud C., Aimar P., Daufin G., Thermal isoelectric precipitation of Alpha-Lactalbumin from a whey-protein concentrate - influence of protein-calcium complexation, Biotechnol. Bioeng. 47 (1995) 121-130.
    • (1995) Biotechnol. Bioeng , vol.47 , pp. 121-130
    • Bramaud, C.1    Aimar, P.2    Daufin, G.3
  • 7
    • 0343907278 scopus 로고    scopus 로고
    • Whey protein fractionation: Isoelectric precipitation of alpha-lactalbumin under gentle heat treatment
    • Bramaud C., Aimar P., Daufin G., Whey protein fractionation: Isoelectric precipitation of alpha-lactalbumin under gentle heat treatment, Biotechnol. Bioeng. 56 (1997) 391-397.
    • (1997) Biotechnol. Bioeng , vol.56 , pp. 391-397
    • Bramaud, C.1    Aimar, P.2    Daufin, G.3
  • 8
    • 0032053268 scopus 로고    scopus 로고
    • Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey
    • Bryant C.M., McClements D.J., Molecular basis of protein functionality with special consideration of cold-set gels derived from heat-denatured whey, Trends Food Sci. Technol. 9 (1998) 143-151.
    • (1998) Trends Food Sci. Technol , vol.9 , pp. 143-151
    • Bryant, C.M.1    McClements, D.J.2
  • 9
    • 34748907965 scopus 로고    scopus 로고
    • The effects of acidification rate, pH and ageing time on the acidic cold set gelation of whey proteins
    • Cavallieri A.L.F., Cunha R.L., The effects of acidification rate, pH and ageing time on the acidic cold set gelation of whey proteins, Food. Hydrocoll. 22 (2007) 439-448.
    • (2007) Food. Hydrocoll , vol.22 , pp. 439-448
    • Cavallieri, A.L.F.1    Cunha, R.L.2
  • 11
    • 41849137180 scopus 로고
    • Eletrophoretic and chromatographic methods for assessing protein purity
    • Copeland R.A, Ed, Chapman & Hall, New York, USA
    • Copeland R.A., Eletrophoretic and chromatographic methods for assessing protein purity, in: Copeland R.A. (Ed.), Methods for protein analysis: A practical guide to laboratory proticols, Chapman & Hall, New York, USA, 1990, pp. 59-98.
    • (1990) Methods for protein analysis: A practical guide to laboratory proticols , pp. 59-98
    • Copeland, R.A.1
  • 12
    • 1842421130 scopus 로고    scopus 로고
    • Aggregation and gelation of bovine betalactoglobulin, alpha-lactalbumin, and serum albumin
    • Paris N, Kato A, Creamer L.K, Pearce J, Eds, Chemical Soc, Washington
    • Gezimati J., Singh H., Creamer L.K., Aggregation and gelation of bovine betalactoglobulin, alpha-lactalbumin, and serum albumin, in: Paris N., Kato A., Creamer L.K., Pearce J. (Eds.), Macromolecular Interactions in Food Technology, Amer. Chemical Soc., Washington, 1996, pp. 113-123.
    • (1996) Macromolecular Interactions in Food Technology, Amer , pp. 113-123
    • Gezimati, J.1    Singh, H.2    Creamer, L.K.3
  • 13
    • 0034768130 scopus 로고    scopus 로고
    • Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    • Havea P., Singh H., Creamer L.K., Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment, J. Dairy Res. 68 (2001) 483-497.
    • (2001) J. Dairy Res , vol.68 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 14
    • 0037205642 scopus 로고    scopus 로고
    • Heatinduced aggregation of whey proteins: Comparison of cheese WPC with acid WPC and relevance of mineral composition
    • Havea P., Singh H., Creamer L.K., Heatinduced aggregation of whey proteins: Comparison of cheese WPC with acid WPC and relevance of mineral composition., J. Agric. Food Chem. 50 (2002) 4674-4681.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 4674-4681
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 15
    • 4043124555 scopus 로고    scopus 로고
    • The roles of disulphide and non-covalent bonding in the functional properties of heat-induced whey protein gels
    • Havea P., Carr A.J., Creamer L.K., The roles of disulphide and non-covalent bonding in the functional properties of heat-induced whey protein gels, J. Dairy Res. 71 (2004) 330-339.
    • (2004) J. Dairy Res , vol.71 , pp. 330-339
    • Havea, P.1    Carr, A.J.2    Creamer, L.K.3
  • 16
    • 0000928084 scopus 로고
    • Determination of reducing sugar and carboydrates: Phenol sulfuric test
    • Whistler R.L, Wolfrom. M.L, Eds, Academic Press, New York, USA
    • Hodge J.R., Hofreiter B.T., Determination of reducing sugar and carboydrates: Phenol sulfuric test, in: Whistler R.L., Wolfrom. M.L. (Eds.), Methods in Carbohidrate Chemistry, Academic Press, New York, USA, 1962. pp. 380-394.
    • (1962) Methods in Carbohidrate Chemistry , pp. 380-394
    • Hodge, J.R.1    Hofreiter, B.T.2
  • 17
    • 0000008542 scopus 로고    scopus 로고
    • Heatinduced aggregation of β-Lactoglobulin: Role of the free thiol group and dissulphide bonds
    • Hoffmann M.A.M., van Mil P.J.J.M., Heatinduced aggregation of β-Lactoglobulin: Role of the free thiol group and dissulphide bonds, J. Agric. Food Chem. 45 (1997) 2942-2948.
    • (1997) J. Agric. Food Chem , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    van Mil, P.J.J.M.2
  • 18
    • 0036230909 scopus 로고    scopus 로고
    • Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment
    • Hong Y.H., Creamer L.K., Changed protein structures of bovine β-lactoglobulin B and α-lactalbumin as a consequence of heat treatment, Int. Dairy J. 12 (2002) 345-359.
    • (2002) Int. Dairy J , vol.12 , pp. 345-359
    • Hong, Y.H.1    Creamer, L.K.2
  • 19
    • 0000362470 scopus 로고    scopus 로고
    • Effects of preheating on properties of aggregates and of cold-set gels of whey protein isolate
    • Ju Z.Y., Kilara A., Effects of preheating on properties of aggregates and of cold-set gels of whey protein isolate, J. Agric. Food Chem. 46 (1998) 3604-3608.
    • (1998) J. Agric. Food Chem , vol.46 , pp. 3604-3608
    • Ju, Z.Y.1    Kilara, A.2
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophages
    • Laemmli U.K., Cleavage of structural proteins during assembly of head of bacteriophages, Nature 227 (1970) 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 21344483892 scopus 로고
    • Effect of heat-treatments in very acidic conditions on whey-protein isolate properties
    • Lupano C.E., Effect of heat-treatments in very acidic conditions on whey-protein isolate properties, J. Dairy Sci. 77 (1994) 2191-2198.
    • (1994) J. Dairy Sci , vol.77 , pp. 2191-2198
    • Lupano, C.E.1
  • 23
    • 0033865978 scopus 로고    scopus 로고
    • Gelation of mixed systems whey protein concentrate-gluten in acidic conditions
    • Lupano C.E., Gelation of mixed systems whey protein concentrate-gluten in acidic conditions, Food Res. Int. 33 (2000) 691-696.
    • (2000) Food Res. Int , vol.33 , pp. 691-696
    • Lupano, C.E.1
  • 24
    • 84988070741 scopus 로고
    • Gelling properties of whey-protein isolate - influence of calcium removal by dialysis or diafiltration at acid or neutral pH
    • Lupano C.E., Dumay E., Cheftel J.C., Gelling properties of whey-protein isolate - influence of calcium removal by dialysis or diafiltration at acid or neutral pH, Int. J. Food Sci. Technol. 27 (1992) 615-628.
    • (1992) Int. J. Food Sci. Technol , vol.27 , pp. 615-628
    • Lupano, C.E.1    Dumay, E.2    Cheftel, J.C.3
  • 25
    • 0012469075 scopus 로고    scopus 로고
    • Gelation of whey protein concentrate in acidic conditions: Effect of pH
    • Lupano C.E., Renzi L.A., Romera V., Gelation of whey protein concentrate in acidic conditions: Effect of pH, J. Agric. Food Chem. 44 (1996) 3010-3014.
    • (1996) J. Agric. Food Chem , vol.44 , pp. 3010-3014
    • Lupano, C.E.1    Renzi, L.A.2    Romera, V.3
  • 26
    • 0027347215 scopus 로고
    • Whey protein concentrates and isolates: Processing and functional properties
    • Morr C.V., Ha E.Y.W., Whey protein concentrates and isolates: Processing and functional properties, Crit. Rev. Food Sci. Nutr. 33 (1993) 431-476.
    • (1993) Crit. Rev. Food Sci. Nutr , vol.33 , pp. 431-476
    • Morr, C.V.1    Ha, E.Y.W.2
  • 27
    • 84907421742 scopus 로고
    • Gelation of soybean protein isolates in acidic conditions - effect of pH and proteinconcentration
    • Puppo M.C., Lupano C.E., Anon M.C., Gelation of soybean protein isolates in acidic conditions - effect of pH and proteinconcentration, J. Agric. Food Chem. 43 (1995) 2356-2361.
    • (1995) J. Agric. Food Chem , vol.43 , pp. 2356-2361
    • Puppo, M.C.1    Lupano, C.E.2    Anon, M.C.3
  • 28
    • 0034462997 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin
    • Schokker E.P., Singh H., Creamer L.K., Heat-induced aggregation of β-lactoglobulin A and B with α-lactalbumin, Int. Dairy J. 10 (2000) 843-853.
    • (2000) Int. Dairy J , vol.10 , pp. 843-853
    • Schokker, E.P.1    Singh, H.2    Creamer, L.K.3
  • 29
    • 0000441851 scopus 로고
    • Texture characteristics, protein solubility, and sulfhydrylgroup disulfide bond contents of heatinduced gels of whey-protein isolate
    • Shimada K., Cheftel J.C., Texture characteristics, protein solubility, and sulfhydrylgroup disulfide bond contents of heatinduced gels of whey-protein isolate, J. Agric. Food Chem. 36 (1988) 1018-1025.
    • (1988) J. Agric. Food Chem , vol.36 , pp. 1018-1025
    • Shimada, K.1    Cheftel, J.C.2
  • 31
    • 0032876123 scopus 로고    scopus 로고
    • Rheological properies and characterization of polymerized whey protein isolates
    • Vardhanabhuti B., Foegeding A., Rheological properies and characterization of polymerized whey protein isolates, J. Agric. Food Chem. 47 (1999) 3649-3655.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 3649-3655
    • Vardhanabhuti, B.1    Foegeding, A.2
  • 32
    • 0002049507 scopus 로고    scopus 로고
    • Solubility
    • Hall G.M, Ed, Chapman & Hall, London, UK
    • Vojdani I., Solubility, in: Hall G.M. (Ed.), Methods of testing protein functionality, Chapman & Hall, London, UK, 1996, pp. 11-55.
    • (1996) Methods of testing protein functionality , pp. 11-55
    • Vojdani, I.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.