메뉴 건너뛰기




Volumn 63, Issue , 2017, Pages 533-544

Unravelling of the water-binding capacity of cold-gelated whey protein microparticles

Author keywords

Cold gelation; Particle particle interactions; Protein microparticles; Time domain nuclear magnetic resonance; Water binding capacity

Indexed keywords

CENTRIFUGATION; EXTRACTION; MIXING; NUCLEAR MAGNETIC RESONANCE; PELLETIZING; PROTEINS; SHEARING; SULFUR COMPOUNDS;

EID: 84991666838     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2016.09.038     Document Type: Article
Times cited : (10)

References (35)
  • 2
    • 0842349573 scopus 로고    scopus 로고
    • Acid-induced cold gelation of globular proteins:  effects of protein aggregate characteristics and disulfide bonding on rheological properties
    • Alting, A.C., Weijers, M., de Hoog, E.H.A., van de Pijpekamp, A.M., C. Stuart, M.A., et al. Acid-induced cold gelation of globular proteins:  effects of protein aggregate characteristics and disulfide bonding on rheological properties. Journal of Agricultural and Food Chemistry 52:3 (2004), 623–631.
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.3 , pp. 623-631
    • Alting, A.C.1    Weijers, M.2    de Hoog, E.H.A.3    van de Pijpekamp, A.M.4    C. Stuart, M.A.5
  • 3
    • 0032870544 scopus 로고    scopus 로고
    • Effects of pH and the gel state on the mechanical properties, moisture contents, and glass transition temperatures of whey protein films
    • Anker, M., Stading, M., Hermansson, A.-M., Effects of pH and the gel state on the mechanical properties, moisture contents, and glass transition temperatures of whey protein films. Journal of Agricultural and Food Chemistry 47:5 (1999), 1878–1886.
    • (1999) Journal of Agricultural and Food Chemistry , vol.47 , Issue.5 , pp. 1878-1886
    • Anker, M.1    Stading, M.2    Hermansson, A.-M.3
  • 4
    • 84897083149 scopus 로고    scopus 로고
    • The potential of aqueous fractionation of lupin seeds for high-protein foods
    • Berghout, J.A.M., Boom, R.M., van der Goot, A.J., The potential of aqueous fractionation of lupin seeds for high-protein foods. Food Chemistry 159 (2014), 64–70.
    • (2014) Food Chemistry , vol.159 , pp. 64-70
    • Berghout, J.A.M.1    Boom, R.M.2    van der Goot, A.J.3
  • 5
    • 13244253788 scopus 로고    scopus 로고
    • Diffusion NMR spectroscopy in supramolecular and combinatorial chemistry: An old parameter—New insights
    • Cohen, Y., Avram, L., Frish, L., Diffusion NMR spectroscopy in supramolecular and combinatorial chemistry: An old parameter—New insights. Angewandte Chemie International Edition 44:4 (2005), 520–554.
    • (2005) Angewandte Chemie International Edition , vol.44 , Issue.4 , pp. 520-554
    • Cohen, Y.1    Avram, L.2    Frish, L.3
  • 6
    • 24344440549 scopus 로고    scopus 로고
    • NMR relaxation and water self-diffusion studies in whey protein solutions and gels
    • Colsenet, R., Mariette, F., Cambert, M., NMR relaxation and water self-diffusion studies in whey protein solutions and gels. Journal of Agricultural and Food Chemistry 53:17 (2005), 6784–6790.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , Issue.17 , pp. 6784-6790
    • Colsenet, R.1    Mariette, F.2    Cambert, M.3
  • 7
    • 54049139546 scopus 로고    scopus 로고
    • The mechanism behind microstructure formation in mixed whey protein–polysaccharide cold-set gels
    • De Jong, S., Klok, H.J., van de Velde, F., The mechanism behind microstructure formation in mixed whey protein–polysaccharide cold-set gels. Food Hydrocolloids 23:3 (2009), 755–764.
    • (2009) Food Hydrocolloids , vol.23 , Issue.3 , pp. 755-764
    • De Jong, S.1    Klok, H.J.2    van de Velde, F.3
  • 8
    • 34047275736 scopus 로고    scopus 로고
    • Charge density of polysaccharide controls microstructure and large deformation properties of mixed gels
    • De Jong, S., van de Velde, F., Charge density of polysaccharide controls microstructure and large deformation properties of mixed gels. Food Hydrocolloids 21:7 (2007), 1172–1187.
    • (2007) Food Hydrocolloids , vol.21 , Issue.7 , pp. 1172-1187
    • De Jong, S.1    van de Velde, F.2
  • 9
    • 79955471374 scopus 로고    scopus 로고
    • Assessment of the effects of fish meal, wheat gluten, soy protein concentrate and feed moisture on extruder system parameters and the technical quality of fish feed
    • Draganovic, V., van der Goot, A.J., Boom, R., Jonkers, J., Assessment of the effects of fish meal, wheat gluten, soy protein concentrate and feed moisture on extruder system parameters and the technical quality of fish feed. Animal Feed Science and Technology 165:3–4 (2011), 238–250.
    • (2011) Animal Feed Science and Technology , vol.165 , Issue.3-4 , pp. 238-250
    • Draganovic, V.1    van der Goot, A.J.2    Boom, R.3    Jonkers, J.4
  • 11
    • 34249039632 scopus 로고    scopus 로고
    • Use of whey proteins for encapsulation and controlled delivery applications
    • Gunasekaran, S., Ko, S., Xiao, L., Use of whey proteins for encapsulation and controlled delivery applications. Journal of Food Engineering 83:1 (2007), 31–40.
    • (2007) Journal of Food Engineering , vol.83 , Issue.1 , pp. 31-40
    • Gunasekaran, S.1    Ko, S.2    Xiao, L.3
  • 12
    • 0036962446 scopus 로고    scopus 로고
    • Quantitative measurement of two-dimensional distribution functions of diffusion and relaxation in grossly inhomogeneous fields
    • Hürlimann, M.D., Venkataramanan, L., Quantitative measurement of two-dimensional distribution functions of diffusion and relaxation in grossly inhomogeneous fields. Journal of Magnetic Resonance 157:1 (2002), 31–42.
    • (2002) Journal of Magnetic Resonance , vol.157 , Issue.1 , pp. 31-42
    • Hürlimann, M.D.1    Venkataramanan, L.2
  • 13
    • 33646436492 scopus 로고
    • Functional properties of the proteins of some Nigerian oilseeds: Conophor seeds and three varieties of melon seeds
    • Ige, M.M., Ogunsua, A.O., Oke, O.L., Functional properties of the proteins of some Nigerian oilseeds: Conophor seeds and three varieties of melon seeds. Journal of Agricultural and Food Chemistry 32:4 (1984), 822–825.
    • (1984) Journal of Agricultural and Food Chemistry , vol.32 , Issue.4 , pp. 822-825
    • Ige, M.M.1    Ogunsua, A.O.2    Oke, O.L.3
  • 14
    • 84987265428 scopus 로고
    • Viscoelastic properties of whey protein gels: Mechanical model and effects of protein concentration on creep
    • Katsuta, K., Rector, D., Kinsella, J.E., Viscoelastic properties of whey protein gels: Mechanical model and effects of protein concentration on creep. Journal of Food Science 55:2 (1990), 516–521.
    • (1990) Journal of Food Science , vol.55 , Issue.2 , pp. 516-521
    • Katsuta, K.1    Rector, D.2    Kinsella, J.E.3
  • 16
    • 0001064628 scopus 로고
    • Microcentrifuge-based method for measuring water-holding of protein gels
    • Kocher, P.N., Foegeding, E.A., Microcentrifuge-based method for measuring water-holding of protein gels. Journal of Food Science 58:5 (1993), 1040–1046.
    • (1993) Journal of Food Science , vol.58 , Issue.5 , pp. 1040-1046
    • Kocher, P.N.1    Foegeding, E.A.2
  • 17
    • 34247639374 scopus 로고    scopus 로고
    • Light-scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and β-lactoglobulin at neutral pH
    • Mahmoudi, N., Mehalebi, S., Nicolai, T., Durand, D., Riaublanc, A., Light-scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and β-lactoglobulin at neutral pH. Journal of Agricultural and Food Chemistry 55:8 (2007), 3104–3111.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.8 , pp. 3104-3111
    • Mahmoudi, N.1    Mehalebi, S.2    Nicolai, T.3    Durand, D.4    Riaublanc, A.5
  • 19
    • 77958529685 scopus 로고    scopus 로고
    • Magnetic resonance imaging (MRI) and relaxation spectrum analysis as methods to investigate swelling in whey protein gels
    • Oztop, M.H., Rosenberg, M., Rosenberg, Y., McCarthy, K.L., McCarthy, M.J., Magnetic resonance imaging (MRI) and relaxation spectrum analysis as methods to investigate swelling in whey protein gels. Journal of Food Science 75:8 (2010), E508–E515.
    • (2010) Journal of Food Science , vol.75 , Issue.8 , pp. E508-E515
    • Oztop, M.H.1    Rosenberg, M.2    Rosenberg, Y.3    McCarthy, K.L.4    McCarthy, M.J.5
  • 20
    • 84908627707 scopus 로고    scopus 로고
    • Effect of crosslink density on the water-binding capacity of whey protein microparticles
    • Peters, J.P.C.M., Luyten, H., Alting, A.C., Boom, R.M., van der Goot, A.J., Effect of crosslink density on the water-binding capacity of whey protein microparticles. Food Hydrocolloids 44 (2015), 277–284.
    • (2015) Food Hydrocolloids , vol.44 , pp. 277-284
    • Peters, J.P.C.M.1    Luyten, H.2    Alting, A.C.3    Boom, R.M.4    van der Goot, A.J.5
  • 21
    • 84944259792 scopus 로고    scopus 로고
    • Time domain nuclear magnetic resonance as a method to determine and characterize the water-binding capacity of whey protein microparticles
    • Peters, J.P.C.M., Vergeldt, F.J., Van As, H., Luyten, H., Boom, R.M., van der Goot, A.J., Time domain nuclear magnetic resonance as a method to determine and characterize the water-binding capacity of whey protein microparticles. Food Hydrocolloids 54:Part A (2016), 170–178.
    • (2016) Food Hydrocolloids , vol.54 , pp. 170-178
    • Peters, J.P.C.M.1    Vergeldt, F.J.2    Van As, H.3    Luyten, H.4    Boom, R.M.5    van der Goot, A.J.6
  • 22
    • 0020176542 scopus 로고
    • A constrained regularization method for inverting data represented by linear algebraic or integral equations
    • Provencher, S.W., A constrained regularization method for inverting data represented by linear algebraic or integral equations. Computer Physics Communications 27:3 (1982), 213–227.
    • (1982) Computer Physics Communications , vol.27 , Issue.3 , pp. 213-227
    • Provencher, S.W.1
  • 23
    • 84916182207 scopus 로고
    • Transport of water across synthetic membranes
    • F. Franks Cambridge University Press
    • Pusch, W., Transport of water across synthetic membranes. Franks, F., (eds.) Water science reviews 3 Water dynamics, Vol. 3, 1988, Cambridge University Press, 278–349.
    • (1988) Water science reviews 3, Water dynamics , vol.3 , pp. 278-349
    • Pusch, W.1
  • 24
    • 21244451938 scopus 로고    scopus 로고
    • Diffusion exchange NMR spectroscopic study of dextran exchange through polyelectrolyte multilayer capsules
    • Qiao, Y., Galvosas, P., Adalsteinsson, T., Schönhoff, M., Callaghan, P.T., Diffusion exchange NMR spectroscopic study of dextran exchange through polyelectrolyte multilayer capsules. The Journal of Chemical Physics 122:21 (2005), 214912.1–214912.9.
    • (2005) The Journal of Chemical Physics , vol.122 , Issue.21 , pp. 214912.1-214912.9
    • Qiao, Y.1    Galvosas, P.2    Adalsteinsson, T.3    Schönhoff, M.4    Callaghan, P.T.5
  • 26
    • 85007029073 scopus 로고    scopus 로고
    • The relationship between the scaling parameter and relaxation time for non-exponential relaxation in disordered systems
    • F. Family M. Daoud H.J. Herrmann H.E. Stanley World Scientific
    • Ryabov, Y.E., Feldman, Y., The relationship between the scaling parameter and relaxation time for non-exponential relaxation in disordered systems. Family, F., Daoud, M., Herrmann, H.J., Stanley, H.E., (eds.) Scaling and disordered systems, 2002, World Scientific, 173–184.
    • (2002) Scaling and disordered systems , pp. 173-184
    • Ryabov, Y.E.1    Feldman, Y.2
  • 28
    • 0035189326 scopus 로고    scopus 로고
    • Improvement and modification of whey protein gel texture using polysaccharides
    • Turgeon, S.L., Beaulieu, M., Improvement and modification of whey protein gel texture using polysaccharides. Food Hydrocolloids 15:4–6 (2001), 583–591.
    • (2001) Food Hydrocolloids , vol.15 , Issue.4-6 , pp. 583-591
    • Turgeon, S.L.1    Beaulieu, M.2
  • 29
    • 0029956010 scopus 로고    scopus 로고
    • Unraveling diffusion constants in biological tissue by combining Carr-Purcell-Meiboom-Gill imaging and pulsed field gradient NMR
    • Van Dusschoten, D., Moonen, C.T.W., de Jager, P.A., Van As, H., Unraveling diffusion constants in biological tissue by combining Carr-Purcell-Meiboom-Gill imaging and pulsed field gradient NMR. Magnetic Resonance in Medicine 36:6 (1996), 907–913.
    • (1996) Magnetic Resonance in Medicine , vol.36 , Issue.6 , pp. 907-913
    • Van Dusschoten, D.1    Moonen, C.T.W.2    de Jager, P.A.3    Van As, H.4
  • 32
    • 0036571437 scopus 로고    scopus 로고
    • Solving Fredholm integrals of the first kind with tensor product structure in 2 and 2.5 dimensions
    • Venkataramanan, L., Song, Y.-Q., Hürlimann, M.D., Solving Fredholm integrals of the first kind with tensor product structure in 2 and 2.5 dimensions. IEEE Transactions on Signal Processing 50:5 (2002), 1017–1026.
    • (2002) IEEE Transactions on Signal Processing , vol.50 , Issue.5 , pp. 1017-1026
    • Venkataramanan, L.1    Song, Y.-Q.2    Hürlimann, M.D.3
  • 33
    • 85168419445 scopus 로고    scopus 로고
    • Sedimentation
    • Marcel Dekker, Inc.
    • Walstra, P., Sedimentation. Physical chemistry of foods, 2003, Marcel Dekker, Inc., 504–514.
    • (2003) Physical chemistry of foods , pp. 504-514
    • Walstra, P.1
  • 34
    • 84985066643 scopus 로고
    • Functional properties of novel proteins: Alfaalfa leaf protein
    • Wang, J.C., Kinsella, J.E., Functional properties of novel proteins: Alfaalfa leaf protein. Journal of Food Science 41:2 (1976), 286–292.
    • (1976) Journal of Food Science , vol.41 , Issue.2 , pp. 286-292
    • Wang, J.C.1    Kinsella, J.E.2
  • 35
    • 33847174684 scopus 로고    scopus 로고
    • Peanut protein concentrate: Production and functional properties as affected by processing
    • Yu, J., Ahmedna, M., Goktepe, I., Peanut protein concentrate: Production and functional properties as affected by processing. Food Chemistry 103:1 (2007), 121–129.
    • (2007) Food Chemistry , vol.103 , Issue.1 , pp. 121-129
    • Yu, J.1    Ahmedna, M.2    Goktepe, I.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.