메뉴 건너뛰기




Volumn 95, Issue 4, 2009, Pages 627-635

Physicochemical changes in whey protein concentrate texturized by reactive supercritical fluid extrusion

Author keywords

Physicochemical changes; Supercritical fluid extrusion; Texturized whey protein concentrate

Indexed keywords

APPARENT VISCOSITY; LARGE PARTICLES; MEAN DIAMETER; NON-COVALENT INTERACTION; PH MODIFICATION; PHYSICOCHEMICAL CHANGES; PROTEIN SOLUBILITY; SOLUBLE PROTEINS; SULFHYDRYL; SUPERCRITICAL FLUID EXTRUSION; TEXTURIZED WHEY PROTEIN CONCENTRATE; WHEY PROTEIN CONCENTRATE;

EID: 69249218963     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2009.06.030     Document Type: Article
Times cited : (34)

References (54)
  • 3
  • 8
    • 0002112253 scopus 로고    scopus 로고
    • Gelation of globular proteins
    • Hill S.E., Leward D.A., and Mitchell J.R. (Eds), Aspen Publishers, Inc, Maryland, USA
    • Clark A.H. Gelation of globular proteins. In: Hill S.E., Leward D.A., and Mitchell J.R. (Eds). Functional Properties of Food Macromolecules (1998), Aspen Publishers, Inc, Maryland, USA 77-138
    • (1998) Functional Properties of Food Macromolecules , pp. 77-138
    • Clark, A.H.1
  • 9
    • 0009278294 scopus 로고
    • Twin-screw extrusion texturization of acid and alkali denatured soy proteins
    • Dahl S.R., and Villota R. Twin-screw extrusion texturization of acid and alkali denatured soy proteins. Journal of Food Science 56 (1991) 1002-1007
    • (1991) Journal of Food Science , vol.56 , pp. 1002-1007
    • Dahl, S.R.1    Villota, R.2
  • 10
    • 85007844131 scopus 로고
    • Effects of various heat treatments on structure and solubility of whey proteins
    • deWit J.N., and Klarenbeek G. Effects of various heat treatments on structure and solubility of whey proteins. Journal of Dairy Science 67 (1984) 2701-2710
    • (1984) Journal of Dairy Science , vol.67 , pp. 2701-2710
    • deWit, J.N.1    Klarenbeek, G.2
  • 11
    • 0013869260 scopus 로고
    • Sulphydryl groups and the N->R conformational change in β-lactoglobulin
    • Dunnill P., and Green D.W. Sulphydryl groups and the N->R conformational change in β-lactoglobulin. Journal of Molecular Biology 5 (1965) 147-151
    • (1965) Journal of Molecular Biology , vol.5 , pp. 147-151
    • Dunnill, P.1    Green, D.W.2
  • 13
    • 21244502615 scopus 로고    scopus 로고
    • Effect of extrusion cooking on protein modification in wheat flour
    • Fisher T. Effect of extrusion cooking on protein modification in wheat flour. European Food Research and Technology 218 (2004) 128-132
    • (2004) European Food Research and Technology , vol.218 , pp. 128-132
    • Fisher, T.1
  • 14
    • 0019063552 scopus 로고
    • Degradation of protein disulphide bonds in dilute alkali
    • Florence T.M. Degradation of protein disulphide bonds in dilute alkali. Biochemistry 189 (1980) 507-520
    • (1980) Biochemistry , vol.189 , pp. 507-520
    • Florence, T.M.1
  • 15
    • 0038996091 scopus 로고
    • Effects of extrusion upon soy concentrate solubility
    • Hager D.F. Effects of extrusion upon soy concentrate solubility. Journal of Agricultural and Food Chemistry 32 (1984) 293-296
    • (1984) Journal of Agricultural and Food Chemistry , vol.32 , pp. 293-296
    • Hager, D.F.1
  • 16
    • 0019039524 scopus 로고
    • Measurement of thermal denaturation of β-Lactoglobulin at pH 2.5
    • Harwalkar V.R. Measurement of thermal denaturation of β-Lactoglobulin at pH 2.5. Journal of Dairy Science 63 104 (1980) 3-1051
    • (1980) Journal of Dairy Science , vol.63 , Issue.104 , pp. 3-1051
    • Harwalkar, V.R.1
  • 17
    • 0019039146 scopus 로고
    • Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5
    • Harwalkar V.R. Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5. Journal of Dairy Science 63 105 (1980) 2-1057
    • (1980) Journal of Dairy Science , vol.63 , Issue.105 , pp. 2-1057
    • Harwalkar, V.R.1
  • 19
    • 0000401845 scopus 로고
    • Properties of extruded whey protein concentrate and cereal flour blends
    • Kim C.H., and Maga J.A. Properties of extruded whey protein concentrate and cereal flour blends. Labensmittel-Wissenchaftund-Technologie 20 (1987) 311-318
    • (1987) Labensmittel-Wissenchaftund-Technologie , vol.20 , pp. 311-318
    • Kim, C.H.1    Maga, J.A.2
  • 21
    • 0034030911 scopus 로고    scopus 로고
    • Effect of pH on the thermal denaturation of whey proteins in milk
    • Law A.J.R., 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.R.1    Leaver, J.2
  • 23
    • 0004905335 scopus 로고
    • Molecular transformations of proteinaceous foods during extrusion processing
    • Ledward D.A., and Tester R.F. Molecular transformations of proteinaceous foods during extrusion processing. Trends in Food Science and Technology 5 (1994) 117-120
    • (1994) Trends in Food Science and Technology , vol.5 , pp. 117-120
    • Ledward, D.A.1    Tester, R.F.2
  • 24
    • 0000031953 scopus 로고    scopus 로고
    • Effect of extrusion temperature on solubility and molecular weight distribution of wheat flour proteins
    • Li M., and Lee T.C. Effect of extrusion temperature on solubility and molecular weight distribution of wheat flour proteins. Journal of Agricultural and Food Chemistry 44 (1996) 763-768
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 763-768
    • Li, M.1    Lee, T.C.2
  • 25
    • 0028527498 scopus 로고
    • Microparticulation of whey protein: related factors affecting the solubility
    • Lieske B., and Konrad G. Microparticulation of whey protein: related factors affecting the solubility. Labensmittel-Untersuchung und-Forschung 199 (1994) 289-293
    • (1994) Labensmittel-Untersuchung und-Forschung , vol.199 , pp. 289-293
    • Lieske, B.1    Konrad, G.2
  • 26
    • 34547683519 scopus 로고    scopus 로고
    • Protein-protein interactions in high moisture-extruded meat analogs and heat-induced soy protein gels
    • Liu K.S., and Hsieh F.H. Protein-protein interactions in high moisture-extruded meat analogs and heat-induced soy protein gels. Journal of American Oil Chemists' Society 84 (2007) 741-748
    • (2007) Journal of American Oil Chemists' Society , vol.84 , pp. 741-748
    • Liu, K.S.1    Hsieh, F.H.2
  • 27
    • 84988070741 scopus 로고
    • Gelling properties of whey protein isolate: influence of calcium removal by dialysis or diafiltration at acid and neutral pH
    • Lupano C.E., Dumay E., and Cheftel J.C. Gelling properties of whey protein isolate: influence of calcium removal by dialysis or diafiltration at acid and neutral pH. International Journal of Food Science and Technology 27 (1992) 615-628
    • (1992) International Journal of Food Science and Technology , vol.27 , pp. 615-628
    • Lupano, C.E.1    Dumay, E.2    Cheftel, J.C.3
  • 29
    • 49649095118 scopus 로고    scopus 로고
    • Rheological characterizations of texturized whey protein concentrate-based powders produced by reactive supercritical fluid extrusion
    • Manoi K., and Rizvi S.S.H. Rheological characterizations of texturized whey protein concentrate-based powders produced by reactive supercritical fluid extrusion. Food Research International 41 (2008) 786-796
    • (2008) Food Research International , vol.41 , pp. 786-796
    • Manoi, K.1    Rizvi, S.S.H.2
  • 30
    • 0002695025 scopus 로고
    • Reactivity, functionality, and extrusion performance of native and chemically modified whey proteins
    • Kokini J.L., Ho C.T., and Karwe M.V. (Eds), Marcel Dekker, Inc, New York, NY, USA
    • Martinez-Serna M.D., and Villota R. Reactivity, functionality, and extrusion performance of native and chemically modified whey proteins. In: Kokini J.L., Ho C.T., and Karwe M.V. (Eds). Food Extrusion Science and Technology (1992), Marcel Dekker, Inc, New York, NY, USA 387-414
    • (1992) Food Extrusion Science and Technology , pp. 387-414
    • Martinez-Serna, M.D.1    Villota, R.2
  • 31
    • 0016662215 scopus 로고
    • Conformational change in bovine β-lactoglobulin at low pH
    • Mills O.E., and Creamer L.K.A. Conformational change in bovine β-lactoglobulin at low pH. Biochimica et Biophysica Acta 379 (1975) 618-626
    • (1975) Biochimica et Biophysica Acta , vol.379 , pp. 618-626
    • Mills, O.E.1    Creamer, L.K.A.2
  • 32
    • 84974356927 scopus 로고
    • Properties of whey protein concentrate prepared by heating under acidic conditions
    • Modler H.W., and Emmons D.B. Properties of whey protein concentrate prepared by heating under acidic conditions. Journal of Dairy Science 60 (1977) 177-184
    • (1977) Journal of Dairy Science , vol.60 , pp. 177-184
    • Modler, H.W.1    Emmons, D.B.2
  • 33
    • 0002915720 scopus 로고
    • Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins
    • Monahan F.J., German J.B., and Kinsella J.E. Effect of pH and temperature on protein unfolding and thiol/disulfide interchange reactions during heat-induced gelation of whey proteins. Journal of Agricultural and Food Chemistry 43 (1995) 46-52
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 34
    • 0022143848 scopus 로고
    • Structure modification and functionality of whey proteins: quantitative structure-activity relationship approach
    • Nakai S., and Chan L. Structure modification and functionality of whey proteins: quantitative structure-activity relationship approach. Journal of Dairy Science 68 (1985) 2763-2772
    • (1985) Journal of Dairy Science , vol.68 , pp. 2763-2772
    • Nakai, S.1    Chan, L.2
  • 36
    • 30844447180 scopus 로고    scopus 로고
    • Properties of whey protein isolates extruded under acidic and alkaline conditions
    • Onwulata C.I., Isobe S., Tomasula P.M., and Cooke P.H. Properties of whey protein isolates extruded under acidic and alkaline conditions. Journal of Dairy Science 89 (2006) 71-81
    • (2006) Journal of Dairy Science , vol.89 , pp. 71-81
    • Onwulata, C.I.1    Isobe, S.2    Tomasula, P.M.3    Cooke, P.H.4
  • 37
    • 0034089645 scopus 로고    scopus 로고
    • Involvement of disulfide bonds in bovine β-lactoglobulin B gels set thermally at various pH
    • Otte J., Zakora M., and Qvist K.B. Involvement of disulfide bonds in bovine β-lactoglobulin B gels set thermally at various pH. Journal of Food Science 65 (2000) 384-389
    • (2000) Journal of Food Science , vol.65 , pp. 384-389
    • Otte, J.1    Zakora, M.2    Qvist, K.B.3
  • 39
    • 10844264089 scopus 로고
    • Protein-protein interactions in the extrusion of soya at various temperatures and moisture contents
    • Prudêncio-Ferreira S.H., and Arêas J.A. Protein-protein interactions in the extrusion of soya at various temperatures and moisture contents. Journal of Food Science 58 (1993) 378-381
    • (1993) Journal of Food Science , vol.58 , pp. 378-381
    • Prudêncio-Ferreira, S.H.1    Arêas, J.A.2
  • 40
    • 84907421742 scopus 로고
    • Gelation of soy protein isolates in acidic conditions. Effect of pH and protein concentration
    • Puppo M.C., Lupano C.E., and Añón M.C. Gelation of soy protein isolates in acidic conditions. Effect of pH and protein concentration. Journal of Agricultural and Food Chemistry 43 (1995) 2356-2361
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2356-2361
    • Puppo, M.C.1    Lupano, C.E.2    Añón, M.C.3
  • 42
    • 0040941719 scopus 로고
    • Viscous behavior of whey protein concentrate dispersions
    • Rattray W., and Jelen P. Viscous behavior of whey protein concentrate dispersions. International Dairy Journal 5 (1995) 673-684
    • (1995) International Dairy Journal , vol.5 , pp. 673-684
    • Rattray, W.1    Jelen, P.2
  • 43
    • 0032831016 scopus 로고    scopus 로고
    • Extrusion chemistry of wheat flour proteins: II. Sulfhydryl-disulfide content and protein structural changes
    • Rebello C.A., and Schaich K.M. Extrusion chemistry of wheat flour proteins: II. Sulfhydryl-disulfide content and protein structural changes. Cereal Chemistry 76 (1999) 756-763
    • (1999) Cereal Chemistry , vol.76 , pp. 756-763
    • Rebello, C.A.1    Schaich, K.M.2
  • 45
    • 69249237598 scopus 로고
    • Effect of alkaline treatment of soy protein on sulfur amino acid bioavailability
    • Robbins K.R., and Ballew J.E. Effect of alkaline treatment of soy protein on sulfur amino acid bioavailability. Journal of Food Science 47 (1982) 2070-2071
    • (1982) Journal of Food Science , vol.47 , pp. 2070-2071
    • Robbins, K.R.1    Ballew, J.E.2
  • 47
    • 0000441851 scopus 로고
    • Texture characteristics, protein solubility, and sulfhydryl group/disulfide bond contents of heat-induced gels of whey protein isolate
    • Shimada K., and Cheftel J.C. Texture characteristics, protein solubility, and sulfhydryl group/disulfide bond contents of heat-induced gels of whey protein isolate. Journal of Agricultural and Food Chemistry 36 (1988) 1018-1025
    • (1988) Journal of Agricultural and Food Chemistry , vol.36 , pp. 1018-1025
    • Shimada, K.1    Cheftel, J.C.2
  • 48
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate
    • Shimada K., and Cheftel J.C. Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. Journal of Agricultural and Food Chemistry 37 (1989) 161-168
    • (1989) Journal of Agricultural and Food Chemistry , vol.37 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 49
    • 0003817488 scopus 로고
    • Protein product base
    • European Patent Specification EP 0 250 623 B1
    • Singer, N.S., Yamamoto, S., Latella, J., 1990. Protein product base. European Patent Specification EP 0 250 623 B1.
    • (1990)
    • Singer, N.S.1    Yamamoto, S.2    Latella, J.3
  • 52
    • 0000222757 scopus 로고
    • Molecular transformations of starch and protein during twin-screw extrusion processing of cornmeal
    • Kokini J.L., Chi-Tang H., and Karwe M.V. (Eds), Marcel Dekker, Inc, New York, USA
    • Wasserman B.P., Wen L.F., and Chan K.Y. Molecular transformations of starch and protein during twin-screw extrusion processing of cornmeal. In: Kokini J.L., Chi-Tang H., and Karwe M.V. (Eds). Food Extrusion Science and Technology (1992), Marcel Dekker, Inc, New York, USA 325-333
    • (1992) Food Extrusion Science and Technology , pp. 325-333
    • Wasserman, B.P.1    Wen, L.F.2    Chan, K.Y.3
  • 53
    • 84974326036 scopus 로고
    • Heat-induced changes in sulfhydryl and disulfide levels of β-lactoglobulin A and formation of polymers
    • Watanabe K., and Klostemeyer H. Heat-induced changes in sulfhydryl and disulfide levels of β-lactoglobulin A and formation of polymers. Journal of Dairy Research 43 (1976) 411-418
    • (1976) Journal of Dairy Research , vol.43 , pp. 411-418
    • Watanabe, K.1    Klostemeyer, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.