메뉴 건너뛰기




Volumn 77, Issue , 2018, Pages 397-406

Partial replacement of whey proteins by rapeseed proteins in heat-induced gelled systems: Effect of pH

Author keywords

DSC analysis; Gel microstructure; Mixed system; Rapeseed protein isolate; Synergistic gels; Whey protein isolate

Indexed keywords

DIFFERENTIAL SCANNING CALORIMETRY; FOOD PRODUCTS; GELATION; GELS; MIXING; OILSEEDS; PRODUCT DESIGN; RHEOLOGY;

EID: 85033665351     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.10.016     Document Type: Article
Times cited : (52)

References (61)
  • 1
    • 57849103415 scopus 로고    scopus 로고
    • Quantitative analysis of confocal laser scanning microscopy images of heat-set globular protein gels
    • Ako, K., Durand, D., Nicolai, T., Becu, L., Quantitative analysis of confocal laser scanning microscopy images of heat-set globular protein gels. Food Hydrocolloids 23:4 (2009), 1111–1119, 10.1016/j.foodhyd.2008.09.003.
    • (2009) Food Hydrocolloids , vol.23 , Issue.4 , pp. 1111-1119
    • Ako, K.1    Durand, D.2    Nicolai, T.3    Becu, L.4
  • 2
    • 0036377752 scopus 로고    scopus 로고
    • Calorimetric studies of thermal denaturation of β -lactoglobulin in the presence of polysaccharides
    • Baeza, R.I., Pilosof, A.M.R., Calorimetric studies of thermal denaturation of β -lactoglobulin in the presence of polysaccharides. LWT - Food Science and Technology 35:5 (2002), 393–399, 10.1006/fstl.2001.0862.
    • (2002) LWT - Food Science and Technology , vol.35 , Issue.5 , pp. 393-399
    • Baeza, R.I.1    Pilosof, A.M.R.2
  • 3
    • 79954995800 scopus 로고    scopus 로고
    • The effect of protein concentration and heat treatment temperature on micellar casein–soy protein mixtures
    • Beliciu, C.M., Moraru, C.I., The effect of protein concentration and heat treatment temperature on micellar casein–soy protein mixtures. Food Hydrocolloids 25:6 (2011), 1448–1460, 10.1016/j.foodhyd.2011.01.011.
    • (2011) Food Hydrocolloids , vol.25 , Issue.6 , pp. 1448-1460
    • Beliciu, C.M.1    Moraru, C.I.2
  • 4
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study
    • Boye, J., Alli, I., Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: A differential scanning calorimetric study. Food Research International 33:8 (2000), 673–682.
    • (2000) Food Research International , vol.33 , Issue.8 , pp. 673-682
    • Boye, J.1    Alli, I.2
  • 5
    • 0642302370 scopus 로고    scopus 로고
    • Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B
    • Boye, J., Ma, C.-Y., Ismail, A., Harwalkar, V., Kalab, M., Molecular and microstructural studies of thermal denaturation and gelation of β-lactoglobulins A and B. Journal of Agricultural and Food Chemistry 45:5 (1997), 1608–1618.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , Issue.5 , pp. 1608-1618
    • Boye, J.1    Ma, C.-Y.2    Ismail, A.3    Harwalkar, V.4    Kalab, M.5
  • 6
    • 22544442178 scopus 로고    scopus 로고
    • Differential scanning calorimetry in life science: Thermodynamics, stability, molecular recognition and application in drug design
    • Bruylants, G., Wouters, J., Michaux, C., Differential scanning calorimetry in life science: Thermodynamics, stability, molecular recognition and application in drug design. Current Medicinal Chemistry 12:17 (2005), 2011–2020.
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.17 , pp. 2011-2020
    • Bruylants, G.1    Wouters, J.2    Michaux, C.3
  • 7
    • 85025568567 scopus 로고
    • Structural properties of single and mixed milk/soya protein systems
    • Chronakis, I.S., Kasapis, S., Structural properties of single and mixed milk/soya protein systems. Food Hydrocolloids 7:6 (1993), 459–478.
    • (1993) Food Hydrocolloids , vol.7 , Issue.6 , pp. 459-478
    • Chronakis, I.S.1    Kasapis, S.2
  • 8
    • 0036838127 scopus 로고    scopus 로고
    • Gelation properties of soya and whey protein isolate mixtures
    • Comfort, S., Howell, N.K., Gelation properties of soya and whey protein isolate mixtures. Food Hydrocolloids 16:6 (2002), 661–672.
    • (2002) Food Hydrocolloids , vol.16 , Issue.6 , pp. 661-672
    • Comfort, S.1    Howell, N.K.2
  • 9
    • 84892959719 scopus 로고    scopus 로고
    • Heat-induced aggregation of whey proteins in aqueous solutions below their isoelectric point
    • Cornacchia, L., Forquenot de la Fortelle, C., Venema, P., Heat-induced aggregation of whey proteins in aqueous solutions below their isoelectric point. Journal of Agricultural and Food Chemistry 62:3 (2014), 733–741, 10.1021/jf404456q.
    • (2014) Journal of Agricultural and Food Chemistry , vol.62 , Issue.3 , pp. 733-741
    • Cornacchia, L.1    Forquenot de la Fortelle, C.2    Venema, P.3
  • 11
    • 84876738736 scopus 로고    scopus 로고
    • Denaturation of whey proteins as a function of heat, pH and protein concentration
    • Dissanayake, M., Ramchandran, L., Donkor, O.N., Vasiljevic, T., Denaturation of whey proteins as a function of heat, pH and protein concentration. International Dairy Journal 31:2 (2013), 93–99, 10.1016/j.idairyj.2013.02.002.
    • (2013) International Dairy Journal , vol.31 , Issue.2 , pp. 93-99
    • Dissanayake, M.1    Ramchandran, L.2    Donkor, O.N.3    Vasiljevic, T.4
  • 12
    • 85078385118 scopus 로고    scopus 로고
    • Scientific Opinion on the safety of “rapeseed protein isolate” as a Novel Food ingredient
    • 3420-n/a
    • Efsa Panel on Dietetic Products, N., & Allergies, Scientific Opinion on the safety of “rapeseed protein isolate” as a Novel Food ingredient. EFSA Journal, 11(10), 2013, 10.2903/j.efsa.2013.3420 3420-n/a.
    • (2013) EFSA Journal , vol.11 , Issue.10
    • Efsa Panel on Dietetic Products, N., & Allergies,1
  • 13
    • 0033829342 scopus 로고    scopus 로고
    • Rheology of κ-carrageenan and β-lactoglobulin mixed gels
    • Eleya, M.O., Turgeon, S., Rheology of κ-carrageenan and β-lactoglobulin mixed gels. Food Hydrocolloids 14:1 (2000), 29–40.
    • (2000) Food Hydrocolloids , vol.14 , Issue.1 , pp. 29-40
    • Eleya, M.O.1    Turgeon, S.2
  • 14
    • 0000171769 scopus 로고    scopus 로고
    • Factors determining fracture stress and strain of fine-stranded whey protein gels
    • Errington, A.D., Foegeding, E.A., Factors determining fracture stress and strain of fine-stranded whey protein gels. Journal of Agricultural and Food Chemistry 46:8 (1998), 2963–2967.
    • (1998) Journal of Agricultural and Food Chemistry , vol.46 , Issue.8 , pp. 2963-2967
    • Errington, A.D.1    Foegeding, E.A.2
  • 17
    • 84973465879 scopus 로고    scopus 로고
    • The microstructure and rheology of homogeneous and phase separated gelatine gels
    • Ersch, C., van der Linden, E., Venema, P., Martin, A., The microstructure and rheology of homogeneous and phase separated gelatine gels. Food Hydrocolloids 61 (2016), 311–317, 10.1016/j.foodhyd.2016.05.022.
    • (2016) Food Hydrocolloids , vol.61 , pp. 311-317
    • Ersch, C.1    van der Linden, E.2    Venema, P.3    Martin, A.4
  • 18
    • 33846219578 scopus 로고    scopus 로고
    • Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry
    • Fitzsimons, S.M., Mulvihill, D.M., Morris, E.R., Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocolloids 21:4 (2007), 638–644, 10.1016/j.foodhyd.2006.07.007.
    • (2007) Food Hydrocolloids , vol.21 , Issue.4 , pp. 638-644
    • Fitzsimons, S.M.1    Mulvihill, D.M.2    Morris, E.R.3
  • 19
    • 0001772345 scopus 로고    scopus 로고
    • Effect of pH and ionic strength on the heat stability of rapeseed 12S globulin (cruciferin) by the ANS fluorescence method
    • Folawiyo, Y.L., Apenten, R.K.O., Effect of pH and ionic strength on the heat stability of rapeseed 12S globulin (cruciferin) by the ANS fluorescence method. Journal of the Science of Food and Agriculture 70:2 (1996), 241–246.
    • (1996) Journal of the Science of Food and Agriculture , vol.70 , Issue.2 , pp. 241-246
    • Folawiyo, Y.L.1    Apenten, R.K.O.2
  • 20
    • 0042532737 scopus 로고    scopus 로고
    • Protein self-association in solution: The bovine beta -lactoglobulin dimer and octamer
    • Gottschalk, M., Nilsson, H., Roos, H., Halle, B., Protein self-association in solution: The bovine beta -lactoglobulin dimer and octamer. Protein Science 12:11 (2003), 2404–2411, 10.1110/ps.0305903.
    • (2003) Protein Science , vol.12 , Issue.11 , pp. 2404-2411
    • Gottschalk, M.1    Nilsson, H.2    Roos, H.3    Halle, B.4
  • 21
    • 64549152144 scopus 로고    scopus 로고
    • Heat-induced whey protein gels: Protein− protein interactions and functional properties
    • Havea, P., Watkinson, P., Kuhn-Sherlock, B., Heat-induced whey protein gels: Protein− protein interactions and functional properties. Journal of Agricultural and Food Chemistry 57:4 (2009), 1506–1512.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , Issue.4 , pp. 1506-1512
    • Havea, P.1    Watkinson, P.2    Kuhn-Sherlock, B.3
  • 22
    • 84962691539 scopus 로고    scopus 로고
    • Mixing whey and soy proteins: Consequences for the gel mechanical response and water holding
    • Jose, J., Pouvreau, L., Martin, A.H., Mixing whey and soy proteins: Consequences for the gel mechanical response and water holding. Food Hydrocolloids 60 (2016), 216–224, 10.1016/j.foodhyd.2016.03.031.
    • (2016) Food Hydrocolloids , vol.60 , pp. 216-224
    • Jose, J.1    Pouvreau, L.2    Martin, A.H.3
  • 23
    • 42149116945 scopus 로고    scopus 로고
    • Phase separation in biopolymer gels: A low- to high-solid exploration of structural morphology and functionality
    • Kasapis, S., Phase separation in biopolymer gels: A low- to high-solid exploration of structural morphology and functionality. Critical Reviews in Food Science and Nutrition 48:4 (2008), 341–359, 10.1080/10408390701347769.
    • (2008) Critical Reviews in Food Science and Nutrition , vol.48 , Issue.4 , pp. 341-359
    • Kasapis, S.1
  • 24
    • 0023765564 scopus 로고
    • Enhanced thermodynamic stability of β-lactoglobulin at low pH. A possible mechanism
    • Kella, N.K.D., Kinsella, J.E., Enhanced thermodynamic stability of β-lactoglobulin at low pH. A possible mechanism. Biochemical Journal 255:1 (1988), 113–118.
    • (1988) Biochemical Journal , vol.255 , Issue.1 , pp. 113-118
    • Kella, N.K.D.1    Kinsella, J.E.2
  • 25
    • 84953312081 scopus 로고    scopus 로고
    • The effect of pH on the gelling behaviour of canola and soy protein isolates
    • Kim, J.H.J., Varankovich, N.V., Nickerson, M.T., The effect of pH on the gelling behaviour of canola and soy protein isolates. Food Research International 81 (2016), 31–38, 10.1016/j.foodres.2015.12.029.
    • (2016) Food Research International , vol.81 , pp. 31-38
    • Kim, J.H.J.1    Varankovich, N.V.2    Nickerson, M.T.3
  • 26
    • 84994128815 scopus 로고    scopus 로고
    • Nature of protein-protein interactions during the gelation of canola protein isolate networks
    • Kim, J.H., Varankovich, N.V., Stone, A.K., Nickerson, M.T., Nature of protein-protein interactions during the gelation of canola protein isolate networks. Food Research International 89:Pt 1 (2016), 408–414, 10.1016/j.foodres.2016.08.018.
    • (2016) Food Research International , vol.89 , pp. 408-414
    • Kim, J.H.1    Varankovich, N.V.2    Stone, A.K.3    Nickerson, M.T.4
  • 28
    • 77956116048 scopus 로고    scopus 로고
    • Gelation: Principles, models and applications to proteins
    • (Elsevier Burlington, MA)
    • van der Linden, E., Foegeding, E.A., Gelation: Principles, models and applications to proteins. Modern Biopolymer Science, 2009, 29–91 (Elsevier Burlington, MA).
    • (2009) Modern Biopolymer Science , pp. 29-91
    • van der Linden, E.1    Foegeding, E.A.2
  • 29
    • 77956007153 scopus 로고    scopus 로고
    • Effect of sesame protein isolate in partial replacement of milk protein on the rheological, textural and microstructural characteristics of fresh cheese
    • Lu, X., Schmitt, D., Chen, S., Effect of sesame protein isolate in partial replacement of milk protein on the rheological, textural and microstructural characteristics of fresh cheese. International Journal of Food Science & Technology 45:7 (2010), 1368–1377, 10.1111/j.1365-2621.2010.02262.x.
    • (2010) International Journal of Food Science & Technology , vol.45 , Issue.7 , pp. 1368-1377
    • Lu, X.1    Schmitt, D.2    Chen, S.3
  • 30
    • 84987277514 scopus 로고
    • Studies of thermal denaturation of oat globulin by differential scanning calorimetry
    • Ma, C.Y., Harwalkar, V., Studies of thermal denaturation of oat globulin by differential scanning calorimetry. Journal of Food Science 53:2 (1988), 531–534.
    • (1988) Journal of Food Science , vol.53 , Issue.2 , pp. 531-534
    • Ma, C.Y.1    Harwalkar, V.2
  • 31
    • 84960938776 scopus 로고    scopus 로고
    • Gelatin increases the coarseness of whey protein gels and impairs water exudation from the mixed gel at low temperatures
    • Martin, A.H., Bakhuizen, E., Ersch, C., Urbonaite, V., de Jongh, H.H.J., Pouvreau, L., Gelatin increases the coarseness of whey protein gels and impairs water exudation from the mixed gel at low temperatures. Food Hydrocolloids 56 (2016), 236–244, 10.1016/j.foodhyd.2015.12.019.
    • (2016) Food Hydrocolloids , vol.56 , pp. 236-244
    • Martin, A.H.1    Bakhuizen, E.2    Ersch, C.3    Urbonaite, V.4    de Jongh, H.H.J.5    Pouvreau, L.6
  • 32
    • 84960111522 scopus 로고    scopus 로고
    • Modulating the aggregation behaviour to restore the mechanical response of acid induced mixed gels of sodium caseinate and soy proteins
    • Martin, A.H., de los Reyes Jiménez, M.L., Pouvreau, L., Modulating the aggregation behaviour to restore the mechanical response of acid induced mixed gels of sodium caseinate and soy proteins. Food Hydrocolloids 58 (2016), 215–223, 10.1016/j.foodhyd.2016.02.029.
    • (2016) Food Hydrocolloids , vol.58 , pp. 215-223
    • Martin, A.H.1    de los Reyes Jiménez, M.L.2    Pouvreau, L.3
  • 33
    • 0028087108 scopus 로고
    • Thermal gelation and denaturation of bovine β-lactoglobulins A and B
    • McSwiney, M., Singh, H., Campanella, O., Creamer, L.K., Thermal gelation and denaturation of bovine β-lactoglobulins A and B. Journal of Dairy Research 61:2 (1994), 221–232.
    • (1994) Journal of Dairy Research , vol.61 , Issue.2 , pp. 221-232
    • McSwiney, M.1    Singh, H.2    Campanella, O.3    Creamer, L.K.4
  • 34
    • 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., 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 43:1 (1995), 46–52.
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , Issue.1 , pp. 46-52
    • Monahan, F.J.1    German, J.B.2    Kinsella, J.E.3
  • 35
    • 0025869830 scopus 로고
    • Structural analysis of the small chain of the 2S albumin, napin nIII, from rapeseed. Chemical and spectroscopic evidence of an intramolecular bond formation
    • Monsalve, R.I., Villalba, M., López-Otín, C., Rodríguez, R., Structural analysis of the small chain of the 2S albumin, napin nIII, from rapeseed. Chemical and spectroscopic evidence of an intramolecular bond formation. Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology 1078:2 (1991), 265–272.
    • (1991) Biochimica et Biophysica Acta (BBA)-Protein Structure and Molecular Enzymology , vol.1078 , Issue.2 , pp. 265-272
    • Monsalve, R.I.1    Villalba, M.2    López-Otín, C.3    Rodríguez, R.4
  • 36
    • 85016440410 scopus 로고    scopus 로고
    • Effect of the pH and NaCl on the microstructure and rheology of mixtures of whey protein isolate and casein micelles upon heating
    • Nguyen, B.T., Chassenieux, C., Nicolai, T., Schmitt, C., Effect of the pH and NaCl on the microstructure and rheology of mixtures of whey protein isolate and casein micelles upon heating. Food Hydrocolloids 70 (2017), 114–122, 10.1016/j.foodhyd.2017.03.013.
    • (2017) Food Hydrocolloids , vol.70 , pp. 114-122
    • Nguyen, B.T.1    Chassenieux, C.2    Nicolai, T.3    Schmitt, C.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., Qvist, K., Involvement of disulfide bonds in bovine β-lactoglobulin B gels set thermally at various pH. Journal of Food Science 65:3 (2000), 384–389.
    • (2000) Journal of Food Science , vol.65 , Issue.3 , pp. 384-389
    • Otte, J.1    Zakora, M.2    Qvist, K.3
  • 38
    • 0001253172 scopus 로고
    • Thermal stability of whey proteins studied by differential scanning calorimetry
    • Paulsson, M., Hegg, P.-O., Castberg, H., Thermal stability of whey proteins studied by differential scanning calorimetry. Thermochimica Acta 95:2 (1985), 435–440.
    • (1985) Thermochimica Acta , vol.95 , Issue.2 , pp. 435-440
    • Paulsson, M.1    Hegg, P.-O.2    Castberg, H.3
  • 39
    • 85006039262 scopus 로고    scopus 로고
    • Structural properties of cruciferin and napin of Brassica napus (canola) show distinct responses to changes in pH and temperature
    • Perera, S.P., McIntosh, T.C., Wanasundara, J.P., Structural properties of cruciferin and napin of Brassica napus (canola) show distinct responses to changes in pH and temperature. Plants (Basel), 5(3), 2016, 10.3390/plants5030036.
    • (2016) Plants (Basel) , vol.5 , Issue.3
    • Perera, S.P.1    McIntosh, T.C.2    Wanasundara, J.P.3
  • 41
    • 0344444635 scopus 로고    scopus 로고
    • Relations between rheological properties and network structure of soy protein gels
    • Renkema, J.M.S., Relations between rheological properties and network structure of soy protein gels. Food Hydrocolloids 18:1 (2004), 39–47, 10.1016/s0268-005x(03)00040-7.
    • (2004) Food Hydrocolloids , vol.18 , Issue.1 , pp. 39-47
    • Renkema, J.M.S.1
  • 42
    • 19944379827 scopus 로고    scopus 로고
    • Heat-induced soy-whey proteins interactions: formation of soluble and insoluble protein complexes
    • Roesch, R.R., Corredig, M., Heat-induced soy-whey proteins interactions: formation of soluble and insoluble protein complexes. Journal of Agricultural and Food Chemistry 53:9 (2005), 3476–3482.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.9 , pp. 3476-3482
    • Roesch, R.R.1    Corredig, M.2
  • 43
    • 0033846408 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration
    • Schokker, E., Singh, H., Pinder, D., Creamer, L., Heat-induced aggregation of β-lactoglobulin AB at pH 2.5 as influenced by ionic strength and protein concentration. International Dairy Journal 10:4 (2000), 233–240.
    • (2000) International Dairy Journal , vol.10 , Issue.4 , pp. 233-240
    • Schokker, E.1    Singh, H.2    Pinder, D.3    Creamer, L.4
  • 44
    • 0031673060 scopus 로고    scopus 로고
    • Heat-induced gelation of rapeseed proteins: Effect of protein interaction and acetylation
    • Schwenke, K.D., Dahme, A., Wolter, T., Heat-induced gelation of rapeseed proteins: Effect of protein interaction and acetylation. Journal of the American Oil Chemists’ Society 75:1 (1998), 83–87.
    • (1998) Journal of the American Oil Chemists’ Society , vol.75 , Issue.1 , pp. 83-87
    • Schwenke, K.D.1    Dahme, A.2    Wolter, T.3
  • 45
    • 84984525542 scopus 로고
    • Isolation of the 12 S globulin from Rapeseed (Brassica napus L.) and characterization as a “neutral” protein on seed proteins. Part 13
    • Schwenke, K., Raab, B., Linow, K.J., Pahtz, W., Uhlig, J., Isolation of the 12 S globulin from Rapeseed (Brassica napus L.) and characterization as a “neutral” protein on seed proteins. Part 13. Molecular Nutrition & Food Research 25:3 (1981), 271–280.
    • (1981) Molecular Nutrition & Food Research , vol.25 , Issue.3 , pp. 271-280
    • Schwenke, K.1    Raab, B.2    Linow, K.J.3    Pahtz, W.4    Uhlig, J.5
  • 46
    • 85009450685 scopus 로고    scopus 로고
    • Modeling water partition in composite gels of BSA with gelatin following thermal treatment
    • Semasaka, C., Katopo, L., Buckow, R., Kasapis, S., Modeling water partition in composite gels of BSA with gelatin following thermal treatment. Food Hydrocolloids 76 (2018), 141–149.
    • (2018) Food Hydrocolloids , vol.76 , pp. 141-149
    • Semasaka, C.1    Katopo, L.2    Buckow, R.3    Kasapis, S.4
  • 47
    • 0000326329 scopus 로고
    • Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate
    • Shimada, K., Cheftel, J.C., Sulfhydryl group/disulfide bond interchange reactions during heat-induced gelation of whey protein isolate. Journal of Agricultural and Food Chemistry 37:1 (1989), 161–168.
    • (1989) Journal of Agricultural and Food Chemistry , vol.37 , Issue.1 , pp. 161-168
    • Shimada, K.1    Cheftel, J.C.2
  • 48
    • 79952535599 scopus 로고    scopus 로고
    • Influence of green tea polyphenols on the colloidal stability and gelation of WPC
    • von Staszewski, M., Jagus, R.J., Pilosof, A.M.R., Influence of green tea polyphenols on the colloidal stability and gelation of WPC. Food Hydrocolloids 25:5 (2011), 1077–1084, 10.1016/j.foodhyd.2010.10.004.
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 1077-1084
    • von Staszewski, M.1    Jagus, R.J.2    Pilosof, A.M.R.3
  • 49
    • 84866179422 scopus 로고    scopus 로고
    • Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity
    • von Staszewski, M., Jara, F.L., Ruiz, A.L.T.G., Jagus, R.J., Carvalho, J.E., Pilosof, A.M.R., Nanocomplex formation between β-lactoglobulin or caseinomacropeptide and green tea polyphenols: Impact on protein gelation and polyphenols antiproliferative activity. Journal of Functional Foods 4:4 (2012), 800–809, 10.1016/j.jff.2012.05.008.
    • (2012) Journal of Functional Foods , vol.4 , Issue.4 , pp. 800-809
    • von Staszewski, M.1    Jara, F.L.2    Ruiz, A.L.T.G.3    Jagus, R.J.4    Carvalho, J.E.5    Pilosof, A.M.R.6
  • 50
    • 84925506236 scopus 로고    scopus 로고
    • Study on the gel properties and secondary structure of soybean protein isolate/egg white composite gels
    • Su, Y., Dong, Y., Niu, F., Wang, C., Liu, Y., Yang, Y., Study on the gel properties and secondary structure of soybean protein isolate/egg white composite gels. European Food Research and Technology 240:2 (2014), 367–378, 10.1007/s00217-014-2336-3.
    • (2014) European Food Research and Technology , vol.240 , Issue.2 , pp. 367-378
    • Su, Y.1    Dong, Y.2    Niu, F.3    Wang, C.4    Liu, Y.5    Yang, Y.6
  • 51
    • 84900832584 scopus 로고    scopus 로고
    • Gelling properties of protein fractions and protein isolate extracted from Australian canola meal
    • Tan, S.H., Mailer, R.J., Blanchard, C.L., Agboola, S.O., Day, L., Gelling properties of protein fractions and protein isolate extracted from Australian canola meal. Food Research International 62 (2014), 819–828, 10.1016/j.foodres.2014.04.055.
    • (2014) Food Research International , vol.62 , pp. 819-828
    • Tan, S.H.1    Mailer, R.J.2    Blanchard, C.L.3    Agboola, S.O.4    Day, L.5
  • 52
    • 41949117726 scopus 로고    scopus 로고
    • Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin
    • Tolkach, A., Kulozik, U., Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin. Le Lait 87:4–5 (2007), 301–315.
    • (2007) Le Lait , vol.87 , Issue.4-5 , pp. 301-315
    • Tolkach, A.1    Kulozik, U.2
  • 53
    • 84953397953 scopus 로고    scopus 로고
    • Relation between gel stiffness and water holding for coarse and fine-stranded protein gels
    • Urbonaite, V., van der Kaaij, S., de Jongh, H.H.J., Scholten, E., Ako, K., van der Linden, E., et al. Relation between gel stiffness and water holding for coarse and fine-stranded protein gels. Food Hydrocolloids 56 (2016), 334–343, 10.1016/j.foodhyd.2015.12.011.
    • (2016) Food Hydrocolloids , vol.56 , pp. 334-343
    • Urbonaite, V.1    van der Kaaij, S.2    de Jongh, H.H.J.3    Scholten, E.4    Ako, K.5    van der Linden, E.6
  • 54
    • 1542269110 scopus 로고    scopus 로고
    • Rheological characteristics of commercial canola protein isolate–κ-carrageenan systems
    • Uruakpa, F.O., Arntfield, S.D., Rheological characteristics of commercial canola protein isolate–κ-carrageenan systems. Food Hydrocolloids 18:3 (2004), 419–427, 10.1016/j.foodhyd.2003.07.001.
    • (2004) Food Hydrocolloids , vol.18 , Issue.3 , pp. 419-427
    • Uruakpa, F.O.1    Arntfield, S.D.2
  • 55
    • 20444370994 scopus 로고    scopus 로고
    • The physico-chemical properties of commercial canola protein isolate-guar gum gels
    • Uruakpa, F.O., Arntfield, S.D., The physico-chemical properties of commercial canola protein isolate-guar gum gels. International Journal of Food Science and Technology 40:6 (2005), 643–653, 10.1111/j.1365-2621.2005.00975.x.
    • (2005) International Journal of Food Science and Technology , vol.40 , Issue.6 , pp. 643-653
    • Uruakpa, F.O.1    Arntfield, S.D.2
  • 56
    • 84939893232 scopus 로고    scopus 로고
    • Solubility, heat-induced gelation and pepsin susceptibility of cruciferin protein as affected by subunit composition
    • Withana-Gamage, T.S., Hegedus, D.D., Qiu, X., Wanasundara, J., Solubility, heat-induced gelation and pepsin susceptibility of cruciferin protein as affected by subunit composition. Food Biophysics 10:2 (2014), 103–115, 10.1007/s11483-014-9370-3.
    • (2014) Food Biophysics , vol.10 , Issue.2 , pp. 103-115
    • Withana-Gamage, T.S.1    Hegedus, D.D.2    Qiu, X.3    Wanasundara, J.4
  • 57
    • 84884601077 scopus 로고    scopus 로고
    • Synergistic enhancement in the co-gelation of salt-soluble pea proteins and whey proteins
    • Wong, D., Vasanthan, T., Ozimek, L., Synergistic enhancement in the co-gelation of salt-soluble pea proteins and whey proteins. Food Chemistry 141:4 (2013), 3913–3919, 10.1016/j.foodchem.2013.05.082.
    • (2013) Food Chemistry , vol.141 , Issue.4 , pp. 3913-3919
    • Wong, D.1    Vasanthan, T.2    Ozimek, L.3
  • 58
    • 34547104814 scopus 로고    scopus 로고
    • The effect of instant green tea on the foaming and rheological properties of egg albumen proteins
    • Wu, W., Clifford, M., Howell, N.K., The effect of instant green tea on the foaming and rheological properties of egg albumen proteins. Journal of the Science of Food and Agriculture 87:10 (2007), 1810–1819, 10.1002/jsfa.2809.
    • (2007) Journal of the Science of Food and Agriculture , vol.87 , Issue.10 , pp. 1810-1819
    • Wu, W.1    Clifford, M.2    Howell, N.K.3
  • 59
    • 41749090899 scopus 로고    scopus 로고
    • Comparative structural, emulsifying, and biological properties of 2 major canola proteins, cruciferin and napin
    • Wu, J., Muir, A.D., Comparative structural, emulsifying, and biological properties of 2 major canola proteins, cruciferin and napin. Journal of Food Science 73:3 (2008), C210–C216, 10.1111/j.1750-3841.2008.00675.x.
    • (2008) Journal of Food Science , vol.73 , Issue.3 , pp. C210-C216
    • Wu, J.1    Muir, A.D.2
  • 60
    • 84897447256 scopus 로고    scopus 로고
    • Impacts of pH and heating temperature on formation mechanisms and properties of thermally induced canola protein gels
    • Yang, C., Wang, Y., Vasanthan, T., Chen, L., Impacts of pH and heating temperature on formation mechanisms and properties of thermally induced canola protein gels. Food Hydrocolloids 40 (2014), 225–236, 10.1016/j.foodhyd.2014.03.011.
    • (2014) Food Hydrocolloids , vol.40 , pp. 225-236
    • Yang, C.1    Wang, Y.2    Vasanthan, T.3    Chen, L.4
  • 61
    • 0032029073 scopus 로고    scopus 로고
    • Protein separations using membrane filtration: New opportunities for whey fractionation
    • Zydney, A.L., Protein separations using membrane filtration: New opportunities for whey fractionation. International Dairy Journal 8:3 (1998), 243–250.
    • (1998) International Dairy Journal , vol.8 , Issue.3 , pp. 243-250
    • Zydney, A.L.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.