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Volumn 75, Issue , 2018, Pages 157-163

Effect of alginate size, mannuronic/guluronic acid content and pH on particle size, thermodynamics and composition of complexes with β-lactoglobulin

Author keywords

[No Author keywords available]

Indexed keywords

DYNAMIC LIGHT SCATTERING; PARTICLE SIZE; PROTEINS; THERMODYNAMICS;

EID: 85029430501     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.09.001     Document Type: Article
Times cited : (26)

References (38)
  • 1
    • 77955045224 scopus 로고    scopus 로고
    • Thermodynamic characterization of acacia gum-beta-lactoglobulin complex coacervation
    • Aberkane, L., Jasniewski, J., Gaiani, C., Scher, J., Sanchez, C., Thermodynamic characterization of acacia gum-beta-lactoglobulin complex coacervation. Langmuir 26:15 (2010), 12523–12533 https://doi.org/10.1021/la100705d.
    • (2010) Langmuir , vol.26 , Issue.15 , pp. 12523-12533
    • Aberkane, L.1    Jasniewski, J.2    Gaiani, C.3    Scher, J.4    Sanchez, C.5
  • 2
    • 12344272183 scopus 로고    scopus 로고
    • Aggregation across the length-scales in beta-lactoglobulin
    • Bromley, E.H.C., Krebs, M.R.H., Donald, A.M., Aggregation across the length-scales in beta-lactoglobulin. Faraday Discussions 128 (2005), 13–27 https://doi.org/10.1039/b403014a.
    • (2005) Faraday Discussions , vol.128 , pp. 13-27
    • Bromley, E.H.C.1    Krebs, M.R.H.2    Donald, A.M.3
  • 3
    • 0004907667 scopus 로고    scopus 로고
    • Bovine beta-lactoglobulin at 1.8 angstrom resolution - still an enigmatic lipocalin
    • Brownlow, S., Cabral, J.H.M., Cooper, R., Flower, D.R., Yewdall, S.J., Polikarpov, I., Sawyer, L., Bovine beta-lactoglobulin at 1.8 angstrom resolution - still an enigmatic lipocalin. Structure 5:4 (1997), 481–495 https://doi.org/10.1016/S0969-2126(97)00205-0.
    • (1997) Structure , vol.5 , Issue.4 , pp. 481-495
    • Brownlow, S.1    Cabral, J.H.M.2    Cooper, R.3    Flower, D.R.4    Yewdall, S.J.5    Polikarpov, I.6    Sawyer, L.7
  • 5
    • 0032708244 scopus 로고    scopus 로고
    • Molecular mass distribution of sodium alginate by high-performance size-exclusion chromatography
    • Ci, S.X., Huynh, T.H., Louie, L.W., Yang, A., Beals, B.J., Ron, N., Desai, N.P., Molecular mass distribution of sodium alginate by high-performance size-exclusion chromatography. Journal of Chromatography A 864:2 (1999), 199–210 https://doi.org/10.1016/S0021-9673(99)01029-8.
    • (1999) Journal of Chromatography A , vol.864 , Issue.2 , pp. 199-210
    • Ci, S.X.1    Huynh, T.H.2    Louie, L.W.3    Yang, A.4    Beals, B.J.5    Ron, N.6    Desai, N.P.7
  • 6
    • 0033778182 scopus 로고    scopus 로고
    • New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay
    • Collini, M., D'Alfonso, L., Baldini, G., New insight on beta-lactoglobulin binding sites by 1-anilinonaphthalene-8-sulfonate fluorescence decay. Protein Science 9:10 (2000), 1968–1974.
    • (2000) Protein Science , vol.9 , Issue.10 , pp. 1968-1974
    • Collini, M.1    D'Alfonso, L.2    Baldini, G.3
  • 7
    • 84968754584 scopus 로고    scopus 로고
    • Coacervation and precipitation in polysaccharide-protein systems
    • Comert, F., Malanowski, A.J., Azarikia, F., Dubin, P.L., Coacervation and precipitation in polysaccharide-protein systems. Soft Matter 12:18 (2016), 4154–4161 https://doi.org/10.1039/c6sm00044d.
    • (2016) Soft Matter , vol.12 , Issue.18 , pp. 4154-4161
    • Comert, F.1    Malanowski, A.J.2    Azarikia, F.3    Dubin, P.L.4
  • 8
    • 0024611630 scopus 로고
    • pH dependent emulsifying properties of beta-Lactoglobulin
    • Das, K.P., Kinsella, J.E., pH dependent emulsifying properties of beta-Lactoglobulin. Journal of Dispersion Science and Technology 10:1 (1989), 77–102 https://doi.org/10.1080/01932698908943160.
    • (1989) Journal of Dispersion Science and Technology , vol.10 , Issue.1 , pp. 77-102
    • Das, K.P.1    Kinsella, J.E.2
  • 10
    • 0028714906 scopus 로고
    • Alginic acid gels - the effect of alginate chemical-composition and molecular-weight
    • Draget, K.I., Braek, G.S., Smidrod, O., Alginic acid gels - the effect of alginate chemical-composition and molecular-weight. Carbohydrate Polymers 25:1 (1994), 31–38 https://doi.org/10.1016/0144-8617(94)90159-7.
    • (1994) Carbohydrate Polymers , vol.25 , Issue.1 , pp. 31-38
    • Draget, K.I.1    Braek, G.S.2    Smidrod, O.3
  • 11
    • 33749946901 scopus 로고
    • Colorimetric method for determination of sugars and related substances
    • Dubois, M., Gilles, K.A., Hamilton, J.K., Rebers, P.A., Smith, F., Colorimetric method for determination of sugars and related substances. Analytical Chemistry 28:3 (1956), 350–356 https://doi.org/10.1021/ac60111a017.
    • (1956) Analytical Chemistry , vol.28 , Issue.3 , pp. 350-356
    • Dubois, M.1    Gilles, K.A.2    Hamilton, J.K.3    Rebers, P.A.4    Smith, F.5
  • 12
    • 84896762430 scopus 로고    scopus 로고
    • Protein-selective coacervation with hyaluronic acid
    • Du, X., Dubin, P.L., Hoagland, D.A., Sun, L., Protein-selective coacervation with hyaluronic acid. Biomacromolecules 15:3 (2014), 726–734 https://doi.org/10.1021/bm500041a.
    • (2014) Biomacromolecules , vol.15 , Issue.3 , pp. 726-734
    • Du, X.1    Dubin, P.L.2    Hoagland, D.A.3    Sun, L.4
  • 14
    • 0036838148 scopus 로고    scopus 로고
    • Interbiopolymer complexing between beta-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration
    • Girard, M., Turgeon, S.L., Gauthier, S.F., Interbiopolymer complexing between beta-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration. Food Hydrocolloids 16:6 (2002), 585–591 https://doi.org/10.1016/S0268-005X(02)00020-6.
    • (2002) Food Hydrocolloids , vol.16 , Issue.6 , pp. 585-591
    • Girard, M.1    Turgeon, S.L.2    Gauthier, S.F.3
  • 15
    • 0141854286 scopus 로고    scopus 로고
    • Quantification of the interactions between beta-lactoglobulin and pectin through capillary electrophoresis analysis
    • Girard, M., Turgeon, S.L., Gauthier, S.F., Quantification of the interactions between beta-lactoglobulin and pectin through capillary electrophoresis analysis. Journal of Agricultural and Food Chemistry 51:20 (2003), 6043–6049 https://doi.org/10.1021/jf034266b.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , Issue.20 , pp. 6043-6049
    • Girard, M.1    Turgeon, S.L.2    Gauthier, S.F.3
  • 16
    • 0038154252 scopus 로고    scopus 로고
    • Thermodynamic parameters of beta-lactoglobulin-pectin complexes assessed by isothermal titration calorimetry
    • Girard, M., Turgeon, S.L., Gauthier, S.F., Thermodynamic parameters of beta-lactoglobulin-pectin complexes assessed by isothermal titration calorimetry. Journal of Agricultural and Food Chemistry 51:15 (2003), 4450–4455 https://doi.org/10.1021/jf0259359.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , Issue.15 , pp. 4450-4455
    • Girard, M.1    Turgeon, S.L.2    Gauthier, S.F.3
  • 17
    • 32944461715 scopus 로고    scopus 로고
    • Characterization of beta-lactoglobulin-sodium alginate interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study
    • Harnsilawat, T., Pongsawatmanit, R., McClements, D.J., Characterization of beta-lactoglobulin-sodium alginate interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study. Food Hydrocolloids 20:5 (2006), 577–585 https://doi.org/10.1016/j.foodhyd.2005.05.005.
    • (2006) Food Hydrocolloids , vol.20 , Issue.5 , pp. 577-585
    • Harnsilawat, T.1    Pongsawatmanit, R.2    McClements, D.J.3
  • 18
    • 84974808079 scopus 로고    scopus 로고
    • Structural characterization of sodium alginate and calcium alginate
    • Hecht, H., Srebnik, S., Structural characterization of sodium alginate and calcium alginate. Biomacromolecules 17:6 (2016), 2160–2167 https://doi.org/10.1021/acs.biomac.6b00378.
    • (2016) Biomacromolecules , vol.17 , Issue.6 , pp. 2160-2167
    • Hecht, H.1    Srebnik, S.2
  • 19
    • 84874005326 scopus 로고    scopus 로고
    • Beta-lactoglobuline-sodium alginate interaction as affected by polysaccharide depolymerization using high intensity ultrasound
    • Hosseini, S.M.H., Emam-Djomeh, Z., Razavi, S.H., Moosavi-Movahedi, A.A., Saboury, A.A., Atri, M.S., et al. Beta-lactoglobuline-sodium alginate interaction as affected by polysaccharide depolymerization using high intensity ultrasound. Food Hydrocolloids 32:2 (2013), 235–244 https://doi.org/10.1016/j.foodhyd.2013.01.002.
    • (2013) Food Hydrocolloids , vol.32 , Issue.2 , pp. 235-244
    • Hosseini, S.M.H.1    Emam-Djomeh, Z.2    Razavi, S.H.3    Moosavi-Movahedi, A.A.4    Saboury, A.A.5    Atri, M.S.6
  • 20
    • 84928348898 scopus 로고    scopus 로고
    • Nanocomplexes arising from protein-polysaccharide electrostatic interaction as a promising carrier for nutraceutical compounds
    • Hosseini, S.M.H., Emam-Djomeh, Z., Sabatino, P., Van der Meeren, P., Nanocomplexes arising from protein-polysaccharide electrostatic interaction as a promising carrier for nutraceutical compounds. Food Hydrocolloids 50 (2015), 16–26 https://doi.org/10.1016/j.foodhyd.2015.04.006.
    • (2015) Food Hydrocolloids , vol.50 , pp. 16-26
    • Hosseini, S.M.H.1    Emam-Djomeh, Z.2    Sabatino, P.3    Van der Meeren, P.4
  • 21
    • 0031573855 scopus 로고    scopus 로고
    • The effects of alginate molecular structure and formulation variables on the physical characteristics of alginate raft systems
    • Johnson, F.A., Craig, D.Q.M., Mercer, A.D., Chauhan, S., The effects of alginate molecular structure and formulation variables on the physical characteristics of alginate raft systems. International Journal of Pharmaceutics 159:1 (1997), 35–42 https://doi.org/10.1016/S0378-5173(97)00266-4.
    • (1997) International Journal of Pharmaceutics , vol.159 , Issue.1 , pp. 35-42
    • Johnson, F.A.1    Craig, D.Q.M.2    Mercer, A.D.3    Chauhan, S.4
  • 22
    • 78650386372 scopus 로고    scopus 로고
    • Fibrillation of beta-lactoglobulin at low pH in the presence of a complexing anionic polysaccharide
    • Jones, O.G., Adamcik, J., Handschin, S., Bolisetty, S., Mezzenga, R., Fibrillation of beta-lactoglobulin at low pH in the presence of a complexing anionic polysaccharide. Langmuir 26:22 (2010), 17449–17458 https://doi.org/10.1021/la1026619.
    • (2010) Langmuir , vol.26 , Issue.22 , pp. 17449-17458
    • Jones, O.G.1    Adamcik, J.2    Handschin, S.3    Bolisetty, S.4    Mezzenga, R.5
  • 23
    • 84946780112 scopus 로고    scopus 로고
    • Complex coacervation of hyaluronic acid and chitosan: Effects of pH, ionic strength, charge density, chain length and the charge ratio
    • Kayitmazer, A.B., Koksal, A.F., Iyilik, E.K., Complex coacervation of hyaluronic acid and chitosan: Effects of pH, ionic strength, charge density, chain length and the charge ratio. Soft Matter 11:44 (2015), 8605–8612 https://doi.org/10.1039/c5sm01829c.
    • (2015) Soft Matter , vol.11 , Issue.44 , pp. 8605-8612
    • Kayitmazer, A.B.1    Koksal, A.F.2    Iyilik, E.K.3
  • 24
    • 0041386471 scopus 로고    scopus 로고
    • Influence of chain stiffness on the interaction of polyelectrolytes with oppositely charged micelles and proteins
    • Kayitmazer, A.B., Seyrek, E., Dubin, P.L., Staggemeier, B.A., Influence of chain stiffness on the interaction of polyelectrolytes with oppositely charged micelles and proteins. Journal of Physical Chemistry B 107:32 (2003), 8158–8165 https://doi.org/10.1021/jp034065a.
    • (2003) Journal of Physical Chemistry B , vol.107 , Issue.32 , pp. 8158-8165
    • Kayitmazer, A.B.1    Seyrek, E.2    Dubin, P.L.3    Staggemeier, B.A.4
  • 25
    • 0031999033 scopus 로고    scopus 로고
    • Large-scale preparation of beta-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography
    • Kristiansen, K.R., Otte, J., Ipsen, R., Qvist, K.B., Large-scale preparation of beta-lactoglobulin A and B by ultrafiltration and ion-exchange chromatography. International Dairy Journal 8:2 (1998), 113–118 https://doi.org/10.1016/S0958-6946(98)00028-4.
    • (1998) International Dairy Journal , vol.8 , Issue.2 , pp. 113-118
    • Kristiansen, K.R.1    Otte, J.2    Ipsen, R.3    Qvist, K.B.4
  • 26
    • 0028549352 scopus 로고
    • Complex-formation between polyelectrolyte and oppositely charged mixed micelles - static and dynamic light-scattering study of the effect of polyelectrolyte molecular-weight and concentration
    • Li, Y.J., Xia, J.L., Dubin, P.L., Complex-formation between polyelectrolyte and oppositely charged mixed micelles - static and dynamic light-scattering study of the effect of polyelectrolyte molecular-weight and concentration. Macromolecules 27:24 (1994), 7049–7055 https://doi.org/10.1021/ma00102a007.
    • (1994) Macromolecules , vol.27 , Issue.24 , pp. 7049-7055
    • Li, Y.J.1    Xia, J.L.2    Dubin, P.L.3
  • 27
    • 78650250860 scopus 로고    scopus 로고
    • Electrophoretic mobility of a colloidal particle with constant surface charge density
    • Makino, K., Ohshima, H., Electrophoretic mobility of a colloidal particle with constant surface charge density. Langmuir 26:23 (2010), 18016–18019 https://doi.org/10.1021/la1035745.
    • (2010) Langmuir , vol.26 , Issue.23 , pp. 18016-18019
    • Makino, K.1    Ohshima, H.2
  • 28
    • 0141445050 scopus 로고
    • Characterization of alignate composition and block-structure by circular-dichroism
    • Morris, E.R., Rees, D.A., Thom, D., Characterization of alignate composition and block-structure by circular-dichroism. Carbohydrate Research 81:2 (1980), 305–314 https://doi.org/10.1016/S0008-6215(00)85661-X.
    • (1980) Carbohydrate Research , vol.81 , Issue.2 , pp. 305-314
    • Morris, E.R.1    Rees, D.A.2    Thom, D.3
  • 29
    • 84857235755 scopus 로고    scopus 로고
    • Cloning and characterization of a novel oligoalginate lyase from a newly isolated bacterium Sphingomonas sp MJ-3
    • Park, H.H., Kam, N., Lee, E.Y., Kim, H.S., Cloning and characterization of a novel oligoalginate lyase from a newly isolated bacterium Sphingomonas sp MJ-3. Marine Biotechnology 14:2 (2012), 189–202 https://doi.org/10.1007/s10126-011-9402-7.
    • (2012) Marine Biotechnology , vol.14 , Issue.2 , pp. 189-202
    • Park, H.H.1    Kam, N.2    Lee, E.Y.3    Kim, H.S.4
  • 30
    • 84924709531 scopus 로고    scopus 로고
    • Properties of beta-lactoglobulin/alginate mixtures as a function of component ratio, pH and applied shear
    • Qomarudin, Q., Orbell, J.D., Ramchandran, L., Gray, S.R., Stewart, M.B., Vasiljevic, T., Properties of beta-lactoglobulin/alginate mixtures as a function of component ratio, pH and applied shear. Food Research International 71 (2015), 23–31 https://doi.org/10.1016/j.foodres.2015.02.024.
    • (2015) Food Research International , vol.71 , pp. 23-31
    • Qomarudin, Q.1    Orbell, J.D.2    Ramchandran, L.3    Gray, S.R.4    Stewart, M.B.5    Vasiljevic, T.6
  • 31
    • 0034769732 scopus 로고    scopus 로고
    • Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3
    • Sakurai, K., Oobatake, M., Goto, Y., Salt-dependent monomer-dimer equilibrium of bovine beta-lactoglobulin at pH 3. Protein Science 10:11 (2001), 2325–2335 https://doi.org/10.1110/ps.17001.
    • (2001) Protein Science , vol.10 , Issue.11 , pp. 2325-2335
    • Sakurai, K.1    Oobatake, M.2    Goto, Y.3
  • 33
    • 70350045005 scopus 로고    scopus 로고
    • Whey protein isolate-chitosan interactions: A calorimetric and spectroscopy study
    • de Souza, H.K.S., Bai, G., Goncalves, M., do, P., Bastos, M., Whey protein isolate-chitosan interactions: A calorimetric and spectroscopy study. Thermochimica Acta 495:1–2 (2009), 108–114 https://doi.org/10.1016/j.tca.2009.06.008.
    • (2009) Thermochimica Acta , vol.495 , Issue.1-2 , pp. 108-114
    • de Souza, H.K.S.1    Bai, G.2    Goncalves, M.3    do, P.4    Bastos, M.5
  • 34
    • 0035824880 scopus 로고    scopus 로고
    • Characterization of pH-induced transitions of beta-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies
    • Taulier, N., Chalikian, T.V., Characterization of pH-induced transitions of beta-lactoglobulin: Ultrasonic, densimetric, and spectroscopic studies. Journal of Molecular Biology 314:4 (2001), 873–889 https://doi.org/10.1006/jmbi.2001.5188.
    • (2001) Journal of Molecular Biology , vol.314 , Issue.4 , pp. 873-889
    • Taulier, N.1    Chalikian, T.V.2
  • 35
    • 0033734435 scopus 로고    scopus 로고
    • Polyelectrolyte-micelle coacervation: Effects of micelle surface charge density, polymer molecular weight, and polymer/surfactant ratio
    • Wang, Y.L., Kimura, K., Dubin, P.L., Jaeger, W., Polyelectrolyte-micelle coacervation: Effects of micelle surface charge density, polymer molecular weight, and polymer/surfactant ratio. Macromolecules 33:9 (2000), 3324–3331 https://doi.org/10.1021/ma991886y.
    • (2000) Macromolecules , vol.33 , Issue.9 , pp. 3324-3331
    • Wang, Y.L.1    Kimura, K.2    Dubin, P.L.3    Jaeger, W.4
  • 36
    • 0037734293 scopus 로고    scopus 로고
    • Complex coacervation of whey proteins and gum Arabic
    • Weinbreck, F., de Vries, R., Schrooyen, P., de Kruif, C.G., Complex coacervation of whey proteins and gum Arabic. Biomacromolecules 4:2 (2003), 293–303 https://doi.org/10.1021/bm025667n.
    • (2003) Biomacromolecules , vol.4 , Issue.2 , pp. 293-303
    • Weinbreck, F.1    de Vries, R.2    Schrooyen, P.3    de Kruif, C.G.4
  • 37
    • 0033759340 scopus 로고    scopus 로고
    • Alginate lyase: Review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications
    • Wong, T.Y., Preston, L.A., Schiller, N.L., Alginate lyase: Review of major sources and enzyme characteristics, structure-function analysis, biological roles, and applications. Annual Review of Microbiology 54 (2000), 289–340 https://doi.org/10.1146/annurev.micro.54.1.289.
    • (2000) Annual Review of Microbiology , vol.54 , pp. 289-340
    • Wong, T.Y.1    Preston, L.A.2    Schiller, N.L.3
  • 38
    • 60249086704 scopus 로고    scopus 로고
    • Interactions between bovine serum albumin and alginate: An evaluation of alginate as protein carrier
    • Zhao, Y., Li, F., Carvajal, M.T., Harris, M.T., Interactions between bovine serum albumin and alginate: An evaluation of alginate as protein carrier. Journal of Colloid and Interface Science 332:2 (2009), 345–353 https://doi.org/10.1016/j.jcis.2008.12.048.
    • (2009) Journal of Colloid and Interface Science , vol.332 , Issue.2 , pp. 345-353
    • Zhao, Y.1    Li, F.2    Carvajal, M.T.3    Harris, M.T.4


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