메뉴 건너뛰기




Volumn 7, Issue , 2016, Pages 93-116

Designing Whey Protein-Polysaccharide Particles for Colloidal Stability

Author keywords

Electrostatic interactions; Nutritional beverages; Protein stability; Soluble complexes

Indexed keywords

BEVERAGES; COMPLEXATION; COULOMB INTERACTIONS; POLYSACCHARIDES; SOLS; STABILITY;

EID: 84959928943     PISSN: 19411413     EISSN: 19411421     Source Type: Journal    
DOI: 10.1146/annurev-food-041715-033315     Document Type: Review
Times cited : (100)

References (102)
  • 1
    • 84950426973 scopus 로고
    • The chemical characterization of the test article used in toxicological studies of gum Arabic [Acacia Senegal (L.) Willd]
    • Anderson DMW, Bridgeman MME, Farquhar JGK, NcNab CGA. 1983. The chemical characterization of the test article used in toxicological studies of gum arabic [Acacia senegal (L.) Willd]. Int. Tree Crops J. 2(3-4):245-54
    • (1983) Int. Tree Crops J. , vol.2 , Issue.3-4 , pp. 245-254
    • Anderson, D.M.W.1    Bridgeman, M.M.E.2    Farquhar, J.G.K.3    NcNab, C.G.A.4
  • 2
    • 0015605203 scopus 로고
    • A generalized approach to the fluid dynamics of particulate systems: Part 1. General correlation for fluidization and sedimentation in solid multiparticle systems
    • Barnea E, Mizrahi J. 1973. A generalized approach to the fluid dynamics of particulate systems: Part 1. General correlation for fluidization and sedimentation in solid multiparticle systems. Chem. Eng. J. 5(2):171-89
    • (1973) Chem. Eng. J. , vol.5 , Issue.2 , pp. 171-189
    • Barnea, E.1    Mizrahi, J.2
  • 3
    • 47149106271 scopus 로고    scopus 로고
    • Factors regulating astringency of whey protein beverages
    • Beecher JW, Drake MA, Luck PJ, Foegeding EA. 2008. Factors regulating astringency of whey protein beverages. J. Dairy Sci. 91(7):2553-60
    • (2008) J. Dairy Sci. , vol.91 , Issue.7 , pp. 2553-2560
    • Beecher, J.W.1    Drake, M.A.2    Luck, P.J.3    Foegeding, E.A.4
  • 4
    • 79952538805 scopus 로고    scopus 로고
    • Formation and characterization of lactoferrin/ pectin electrostatic complexes: Impact of composition, pH and thermal treatment
    • Bengoechea C, Jones OG, Guerrero A, McClements DJ. 2011. Formation and characterization of lactoferrin/ pectin electrostatic complexes: impact of composition, pH and thermal treatment. Food Hydrocoll. 25(5):1227-32
    • (2011) Food Hydrocoll. , vol.25 , Issue.5 , pp. 1227-1232
    • Bengoechea, C.1    Jones, O.G.2    Guerrero, A.3    McClements, D.J.4
  • 5
    • 33750958542 scopus 로고    scopus 로고
    • Formation and characterization of amphiphilic conjugates of whey protein isolate (WPI)/xanthan to improve surface activity
    • Benichou A, Aserin A, Lutz R, Garti N. 2007. Formation and characterization of amphiphilic conjugates of whey protein isolate (WPI)/xanthan to improve surface activity. Food Hydrocoll. 21(3):379-91
    • (2007) Food Hydrocoll. , vol.21 , Issue.3 , pp. 379-391
    • Benichou, A.1    Aserin, A.2    Lutz, R.3    Garti, N.4
  • 6
    • 0001119293 scopus 로고
    • Thermal stability of whey proteins - A calorimetric study
    • Bernal V, Jelen P. 1985. Thermal stability of whey proteins - A calorimetric study. J. Dairy Sci. 68(11):2847-52
    • (1985) J. Dairy Sci. , vol.68 , Issue.11 , pp. 2847-2852
    • Bernal, V.1    Jelen, P.2
  • 7
    • 1842741353 scopus 로고    scopus 로고
    • Electrostatic free energy of weakly charged macromolecules in solution and intermacromolecular complexes consisting of oppositely charged polymers
    • Biesheuvel PM, Cohen Stuart MA. 2004. Electrostatic free energy of weakly charged macromolecules in solution and intermacromolecular complexes consisting of oppositely charged polymers. Langmuir 20(7):2785-91
    • (2004) Langmuir , vol.20 , Issue.7 , pp. 2785-2791
    • Biesheuvel, P.M.1    Cohen Stuart, M.A.2
  • 8
    • 0033348496 scopus 로고    scopus 로고
    • Reversible gelation in hydrophobic polyelectrolyte/protein mixtures: An example of cross-links between soft and hard colloids
    • Borrega R, Tribet C, Audebert R. 1999. Reversible gelation in hydrophobic polyelectrolyte/protein mixtures: an example of cross-links between soft and hard colloids. Macromolecules 32(23):7798-806
    • (1999) Macromolecules , vol.32 , Issue.23 , pp. 7798-7806
    • Borrega, R.1    Tribet, C.2    Audebert, R.3
  • 9
    • 67349099595 scopus 로고    scopus 로고
    • Carrageenans: Biological properties, chemical modifications and structural analysis: A review
    • Campo VL, Kawano DF, da Silva DB, Carvalho I. 2009. Carrageenans: biological properties, chemical modifications and structural analysis: a review. Carbohydr. Polym. 77(2):167-80
    • (2009) Carbohydr. Polym. , vol.77 , Issue.2 , pp. 167-180
    • Campo, V.L.1    Kawano, D.F.2    Da Silva, D.B.3    Carvalho, I.4
  • 10
    • 34147144198 scopus 로고    scopus 로고
    • Microencapsulation for the improved delivery of bioactive compounds into foods
    • Champagne CP, Fustier P. 2007. Microencapsulation for the improved delivery of bioactive compounds into foods. Curr. Opin. Biotechnol. 18(2):184-90
    • (2007) Curr. Opin. Biotechnol. , vol.18 , Issue.2 , pp. 184-190
    • Champagne, C.P.1    Fustier, P.2
  • 11
    • 70149114571 scopus 로고    scopus 로고
    • Impact of cosolvents on formation and properties of biopolymer nanoparticles formed by heat treatment of lactoglobulin-pectin complexes
    • ChanasattruW, Jones OG, Decker EA, McClements DJ. 2009. Impact of cosolvents on formation and properties of biopolymer nanoparticles formed by heat treatment of lactoglobulin-pectin complexes. Food Hydrocoll. 23(8):2450-57
    • (2009) Food Hydrocoll. , vol.23 , Issue.8 , pp. 2450-2457
    • Chanasattru, W.1    Jones, O.G.2    Decker, E.A.3    McClements, D.J.4
  • 12
    • 84889101677 scopus 로고    scopus 로고
    • Oil-filled hydrogel particles for reduced-fat food applications: Fabrication, characterization, and properties
    • Chung C, Degner B, Decker EA, McClements DJ. 2013. Oil-filled hydrogel particles for reduced-fat food applications: fabrication, characterization, and properties. Innov. Food Sci. Emerg. Technol. 20:324-34
    • (2013) Innov. Food Sci. Emerg. Technol. , vol.20 , pp. 324-334
    • Chung, C.1    Degner, B.2    Decker, E.A.3    McClements, D.J.4
  • 14
    • 69249089296 scopus 로고    scopus 로고
    • Polyelectrolyte-protein complexation driven by charge regulation
    • da Silva FLB, Jönsson B. 2009. Polyelectrolyte-protein complexation driven by charge regulation. Soft Matter 5(15):2862-68
    • (2009) Soft Matter , vol.5 , Issue.15 , pp. 2862-2868
    • Da Silva, F.L.B.1    Jönsson, B.2
  • 16
    • 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. 2007. Charge density of polysaccharide controls microstructure and large deformation properties of mixed gels. Food Hydrocoll. 21(7):1172-87
    • (2007) Food Hydrocoll. , vol.21 , Issue.7 , pp. 1172-1187
    • De Jong, S.1    Van De Velde, F.2
  • 17
    • 0035177826 scopus 로고    scopus 로고
    • Polysaccharide protein interactions
    • de Kruif CG, Tuinier R. 2001. Polysaccharide protein interactions. Food Hydrocoll. 15(4-6):555-63
    • (2001) Food Hydrocoll. , vol.15 , Issue.4-6 , pp. 555-563
    • De Kruif, C.G.1    Tuinier, R.2
  • 19
    • 42149164796 scopus 로고    scopus 로고
    • Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions
    • Dickinson E. 2008. Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions. Soft Matter 4(5):932-42
    • (2008) Soft Matter , vol.4 , Issue.5 , pp. 932-942
    • Dickinson, E.1
  • 20
    • 0024407137 scopus 로고
    • Sugar alcohols as bulk sweeteners
    • Dills WL. 1989. Sugar alcohols as bulk sweeteners. Annu. Rev. Nutr. 9:161-86
    • (1989) Annu. Rev. Nutr. , vol.9 , pp. 161-186
    • Dills, W.L.1
  • 22
    • 79960801451 scopus 로고    scopus 로고
    • Pectin
    • ed. GO Phillips, PA Williams. Boca Raton, FL: CRC Press. 2nd ed
    • Endreß HU, Christensen SH. 2009. Pectin. In Handbook of Hydrocolloids, ed. GO Phillips, PA Williams, pp. 274-97. Boca Raton, FL: CRC Press. 2nd ed.
    • (2009) Handbook of Hydrocolloids , pp. 274-297
    • Endreß, H.U.1    Christensen, S.H.2
  • 23
    • 84908131340 scopus 로고    scopus 로고
    • Complex coacervation with whey protein isolate and gum Arabic for the microencapsulation of omega-3 rich tuna oil
    • Eratte D, Wang B, Dowling K, Barrow CJ, Adhikari BP. 2014. Complex coacervation with whey protein isolate and gum arabic for the microencapsulation of omega-3 rich tuna oil. Food Funct. 5(11):2743-50
    • (2014) Food Funct. , vol.5 , Issue.11 , pp. 2743-2750
    • Eratte, D.1    Wang, B.2    Dowling, K.3    Barrow, C.J.4    Adhikari, B.P.5
  • 24
    • 1842530304 scopus 로고    scopus 로고
    • Manufacture and use of dairy protein fractions
    • Etzel MR. 2004. Manufacture and use of dairy protein fractions. J. Nutr. 134(4):996S-1002S
    • (2004) J. Nutr. , vol.134 , Issue.4 , pp. 996S-1002S
    • Etzel, M.R.1
  • 26
    • 84886100235 scopus 로고    scopus 로고
    • Design and characterization of soluble biopolymer complexes produced by electrostatic self-assembly of a whey protein isolate and sodium alginate
    • Fioramonti SA, Perez AA, Aríngoli EE, Rubiolo AC, Santiago LG. 2014. Design and characterization of soluble biopolymer complexes produced by electrostatic self-assembly of a whey protein isolate and sodium alginate. Food Hydrocoll. 35:129-36
    • (2014) Food Hydrocoll. , vol.35 , pp. 129-136
    • Fioramonti, S.A.1    Perez, A.A.2    Aríngoli, E.E.3    Rubiolo, A.C.4    Santiago, L.G.5
  • 28
    • 77956612625 scopus 로고    scopus 로고
    • Structural modifications of sugar beet pectin and the relationship of structure to functionality
    • Funami T, NakaumaM, Ishihara S, Tanaka R, Inoue T, Phillips GO. 2011. Structural modifications of sugar beet pectin and the relationship of structure to functionality. Food Hydrocoll. 25(2):221-29
    • (2011) Food Hydrocoll. , vol.25 , Issue.2 , pp. 221-229
    • Funami, T.1    Nakauma, M.2    Ishihara, S.3    Tanaka, R.4    Inoue, T.5    Phillips, G.O.6
  • 29
    • 77953153444 scopus 로고    scopus 로고
    • Stabilization of whey protein isolate-pectin complexes by heat
    • Gentès M-C, St-Gelais D, Turgeon SL. 2010. Stabilization of whey protein isolate-pectin complexes by heat. J. Agric. Food Chem. 58(11):7051-58
    • (2010) J. Agric. Food Chem. , vol.58 , Issue.11 , pp. 7051-7058
    • Gentès, M.-C.1    St-Gelais, D.2    Turgeon, S.L.3
  • 30
    • 0036838148 scopus 로고    scopus 로고
    • Interbiopolymer complexing between lactoglobulin and lowand high-methylated pectin measured by potentiometric titration and ultrafiltration
    • Girard M, Turgeon SL, Gauthier SF. 2002. Interbiopolymer complexing between lactoglobulin and lowand high-methylated pectin measured by potentiometric titration and ultrafiltration. Food Hydrocoll. 16(6):585-91
    • (2002) Food Hydrocoll. , vol.16 , Issue.6 , pp. 585-591
    • Girard, M.1    Turgeon, S.L.2    Gauthier, S.F.3
  • 31
    • 85105747586 scopus 로고    scopus 로고
    • Milk protein-polysaccharide interactions
    • ed. HSingh, M Boland, A Thompson San Diego: Acad. Press. 2nd ed
    • Goh KKT, Sarkar A, Singh H. 2014. Milk protein-polysaccharide interactions. In Milk Proteins, ed. HSingh, M Boland, A Thompson, pp. 387-419. San Diego: Acad. Press. 2nd ed.
    • (2014) Milk Proteins , pp. 387-419
    • Goh, K.K.T.1    Sarkar, A.2    Singh, H.3
  • 32
    • 61449141174 scopus 로고    scopus 로고
    • Gastrointestinal effects of low-digestible carbohydrates
    • Grabitske HA, Slavin JL. 2009. Gastrointestinal effects of low-digestible carbohydrates. Crit. Rev. Food Sci. Nutr. 49(4):327-60
    • (2009) Crit. Rev. Food Sci. Nutr. , vol.49 , Issue.4 , pp. 327-360
    • Grabitske, H.A.1    Slavin, J.L.2
  • 33
    • 0001963343 scopus 로고
    • A P. M. R. Study of the composition and sequence of uronate residues in alginates
    • GrasdalenH, Larsen B, SmidsrødO. 1979. A p. m. R. study of the composition and sequence of uronate residues in alginates. Carbohydr. Res. 68(1):23-31
    • (1979) Carbohydr. Res. , vol.68 , Issue.1 , pp. 23-31
    • Grasdalen, H.1    Larsen, B.2    Smidsrød, O.3
  • 34
    • 77955400715 scopus 로고    scopus 로고
    • Molecular basis for the emulsifying properties of sugar beet pectin studied by atomic forcemicroscopy and force spectroscopy
    • Gromer A, Penfold R, Gunning AP, Kirby AR, MorrisVJ. 2010. Molecular basis for the emulsifying properties of sugar beet pectin studied by atomic forcemicroscopy and force spectroscopy. Soft Matter 6(16):3957-69
    • (2010) Soft Matter , vol.6 , Issue.16 , pp. 3957-3969
    • Gromer, A.1    Penfold, R.2    Gunning, A.P.3    Kirby, A.R.4    Morris, V.J.5
  • 35
    • 4444274244 scopus 로고    scopus 로고
    • Influence of pH and carrageenan type on properties of lactoglobulin stabilized oil-in-water emulsions
    • Gu YS, Decker EA, McClements DJ. 2005. Influence of pH and carrageenan type on properties of lactoglobulin stabilized oil-in-water emulsions. Food Hydrocoll. 19(1):83-91
    • (2005) Food Hydrocoll. , vol.19 , Issue.1 , pp. 83-91
    • Gu, Y.S.1    Decker, E.A.2    McClements, D.J.3
  • 36
    • 47949096510 scopus 로고    scopus 로고
    • Finite size and inner structure controlled by electrostatic screening in globular complexes of proteins and polyelectrolytes
    • Gummel J, Boué F, Clemens D, Cousin F. 2008. Finite size and inner structure controlled by electrostatic screening in globular complexes of proteins and polyelectrolytes. Soft Matter 4(8):1653-64
    • (2008) Soft Matter , vol.4 , Issue.8 , pp. 1653-1664
    • Gummel, J.1    Boué, F.2    Clemens, D.3    Cousin, F.4
  • 37
    • 23644433320 scopus 로고    scopus 로고
    • Characterization of lactoglobulin-chitosan interactions in aqueous solutions: A calorimetry, light scattering, electrophoretic mobility and solubility study
    • Guzey D, McClements DJ. 2006. Characterization of lactoglobulin-chitosan interactions in aqueous solutions: a calorimetry, light scattering, electrophoretic mobility and solubility study. Food Hydrocoll. 20(1):124-31
    • (2006) Food Hydrocoll. , vol.20 , Issue.1 , pp. 124-131
    • Guzey, D.1    McClements, D.J.2
  • 38
    • 0038045562 scopus 로고    scopus 로고
    • Functional properties of whey, whey components, and essential amino acids: Mechanisms underlying health benefits for active people (review)
    • Ha E, Zemel MB. 2003. Functional properties of whey, whey components, and essential amino acids: mechanisms underlying health benefits for active people (review). J. Nutr. Biochem. 14(5):251-58
    • (2003) J. Nutr. Biochem. , vol.14 , Issue.5 , pp. 251-258
    • Ha, E.1    Zemel, M.B.2
  • 39
    • 0000340035 scopus 로고    scopus 로고
    • Effect of pHon the binding oflactoglobulin to sodium polystyrenesulfonate
    • Hallberg RK, Dubin PL. 1998. Effect of pHon the binding oflactoglobulin to sodium polystyrenesulfonate. J. Phys. Chem. B 102(43):8629-33
    • (1998) J. Phys. Chem. B , vol.102 , Issue.43 , pp. 8629-8633
    • Hallberg, R.K.1    Dubin, P.L.2
  • 40
    • 77953156453 scopus 로고    scopus 로고
    • Coated whey protein/alginate microparticles as oral controlled delivery systems for probiotic yeast
    • Hébrard G, Hoffart V, Beyssac E, Cardot JM, Alric M, Subirade M. 2010. Coated whey protein/alginate microparticles as oral controlled delivery systems for probiotic yeast. J. Microencapsul. 27(4):292-302
    • (2010) J. Microencapsul. , vol.27 , Issue.4 , pp. 292-302
    • Hébrard, G.1    Hoffart, V.2    Beyssac, E.3    Cardot, J.M.4    Alric, M.5    Subirade, M.6
  • 41
    • 84908469783 scopus 로고    scopus 로고
    • Effects of chloride, thiocyanate and sulphate salts on lactoglobulin-pectin associative complexes
    • Hirt S, JonesOG. 2014. Effects of chloride, thiocyanate and sulphate salts on lactoglobulin-pectin associative complexes. Int. J. Food Sci. Technol. 49(11):2391-98
    • (2014) Int. J. Food Sci. Technol. , vol.49 , Issue.11 , pp. 2391-2398
    • Hirt, S.1    Jones, O.G.2
  • 42
    • 34447632834 scopus 로고    scopus 로고
    • Formation of hydrogel particles by thermal treatment of lactoglobulin-chitosan complexes
    • Hong YH, McClements DJ. 2007. Formation of hydrogel particles by thermal treatment of lactoglobulin-chitosan complexes. J. Agric. Food Chem. 55(14):5653-60
    • (2007) J. Agric. Food Chem. , vol.55 , Issue.14 , pp. 5653-5660
    • Hong, Y.H.1    McClements, D.J.2
  • 44
    • 0033956297 scopus 로고    scopus 로고
    • Nanosuspensions as a new approach for the formulation for the poorly soluble drug tarazepide
    • Jacobs C, Kayser O, Müller RH. 2000. Nanosuspensions as a new approach for the formulation for the poorly soluble drug tarazepide. Int. J. Pharm. 196(2):161-64
    • (2000) Int. J. Pharm. , vol.196 , Issue.2 , pp. 161-164
    • Jacobs, C.1    Kayser, O.2    Müller, R.H.3
  • 45
    • 0016624572 scopus 로고
    • Structure of the extracellular polysaccharide from Xanthomonas campestris
    • Jansson PE, Kenne L, Lindberg B. 1975. Structure of the extracellular polysaccharide from Xanthomonas campestris. Carbohydr. Res. 45(1):275-82
    • (1975) Carbohydr. Res. , vol.45 , Issue.1 , pp. 275-282
    • Jansson, P.E.1    Kenne, L.2    Lindberg, B.3
  • 46
    • 70450237051 scopus 로고    scopus 로고
    • Thermal analysis of lactoglobulin complexes with pectins or carrageenan for production of stable biopolymer particles
    • Jones O, Decker EA, McClements DJ. 2010a. Thermal analysis of lactoglobulin complexes with pectins or carrageenan for production of stable biopolymer particles. Food Hydrocoll. 24(2-3):239-48
    • (2010) Food Hydrocoll. , vol.24 , Issue.2-3 , pp. 239-248
    • Jones, O.1    Decker, E.A.2    McClements, D.J.3
  • 47
    • 60149105994 scopus 로고    scopus 로고
    • Formation of biopolymer particles by thermal treatment of lactoglobulin-pectin complexes
    • Jones OG, Decker EA, McClements DJ. 2009. Formation of biopolymer particles by thermal treatment of lactoglobulin-pectin complexes. Food Hydrocoll. 23(5):1312-21
    • (2009) Food Hydrocoll. , vol.23 , Issue.5 , pp. 1312-1321
    • Jones, O.G.1    Decker, E.A.2    McClements, D.J.3
  • 48
    • 75149149755 scopus 로고    scopus 로고
    • Effect of polysaccharide charge on formation and properties of biopolymer nanoparticles created by heat treatment of lactoglobulin-pectin complexes
    • Jones OG, Lesmes U, Dubin P, McClements DJ. 2010b. Effect of polysaccharide charge on formation and properties of biopolymer nanoparticles created by heat treatment of lactoglobulin-pectin complexes. Food Hydrocoll. 24(4):374-83
    • (2010) Food Hydrocoll. , vol.24 , Issue.4 , pp. 374-383
    • Jones, O.G.1    Lesmes, U.2    Dubin, P.3    McClements, D.J.4
  • 49
    • 77955781868 scopus 로고    scopus 로고
    • Functional biopolymer particles: Design, fabrication, and applications
    • Jones OG, McClements DJ. 2010a. Functional biopolymer particles: design, fabrication, and applications. Compr. Rev. Food Sci. Food Saf. 9(4):374-97
    • (2010) Compr. Rev. Food Sci. Food Saf. , vol.9 , Issue.4 , pp. 374-397
    • Jones, O.G.1    McClements, D.J.2
  • 50
    • 77953155271 scopus 로고    scopus 로고
    • Biopolymer nanoparticles from heat-treated electrostatic proteinpolysaccharide complexes: Factors affecting particle characteristics
    • Jones OG, McClements DJ. 2010b. Biopolymer nanoparticles from heat-treated electrostatic proteinpolysaccharide complexes: factors affecting particle characteristics. J. Food Sci. 75(2):N36-43
    • (2010) J. Food Sci. , vol.75 , Issue.2 , pp. N36-43
    • Jones, O.G.1    McClements, D.J.2
  • 51
    • 80052501915 scopus 로고    scopus 로고
    • Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein-polysaccharide complexes
    • Jones OG, McClements DJ. 2011. Recent progress in biopolymer nanoparticle and microparticle formation by heat-treating electrostatic protein-polysaccharide complexes. Adv. Colloid Interface Sci. 167(1-2):49-62
    • (2011) Adv. Colloid Interface Sci. , vol.167 , Issue.1-2 , pp. 49-62
    • Jones, O.G.1    McClements, D.J.2
  • 52
    • 84914708768 scopus 로고    scopus 로고
    • Biopolymer-based nanoparticles and microparticles: Fabrication, characterization, and application
    • Joye IJ, McClements DJ. 2014. Biopolymer-based nanoparticles and microparticles: fabrication, characterization, and application. Curr. Opin. Colloid Interface Sci. 19(5):417-427
    • (2014) Curr. Opin. Colloid Interface Sci. , vol.19 , Issue.5 , pp. 417-427
    • Joye, I.J.1    McClements, D.J.2
  • 53
    • 0037897339 scopus 로고    scopus 로고
    • Interactions of lactoglobulin and high-methoxyl pectins in acidified systems
    • Kazmierski M, Wicker L, Corredig M. 2003. Interactions of lactoglobulin and high-methoxyl pectins in acidified systems. J. Food Sci. 68(5):1673-79
    • (2003) J. Food Sci. , vol.68 , Issue.5 , pp. 1673-1679
    • Kazmierski, M.1    Wicker, L.2    Corredig, M.3
  • 54
    • 80052486463 scopus 로고    scopus 로고
    • Complexation and coacervation of polyelectrolyteswith oppositely charged colloids
    • Kizilay E, KayitmazerAB, Dubin PL. 2011. Complexation and coacervation of polyelectrolyteswith oppositely charged colloids. Adv. Colloid Interface Sci. 167(1-2):24-37
    • (2011) Adv. Colloid Interface Sci. , vol.167 , Issue.1-2 , pp. 24-37
    • Kizilay, E.1    Kayitmazer, A.B.2    Dubin, P.L.3
  • 56
    • 84896823108 scopus 로고    scopus 로고
    • Whey protein-pectin complexes as new texturising elements in fat-reduced yoghurt systems
    • Krzeminski A, Prell KA, Busch-Stockfisch M, Weiss J, Hinrichs J. 2014a. Whey protein-pectin complexes as new texturising elements in fat-reduced yoghurt systems. Int. Dairy J. 36(2):118-27
    • (2014) Int. Dairy J. , vol.36 , Issue.2 , pp. 118-127
    • Krzeminski, A.1    Prell, K.A.2    Busch-Stockfisch, M.3    Weiss, J.4    Hinrichs, J.5
  • 57
    • 84886295577 scopus 로고    scopus 로고
    • Environmental response of pectin-stabilized whey protein aggregates
    • Krzeminski A, PrellKA, Weiss J, Hinrichs J. 2014b. Environmental response of pectin-stabilized whey protein aggregates. Food Hydrocoll. 35:332-40
    • (2014) Food Hydrocoll. , vol.35 , pp. 332-340
    • Krzeminski, A.1    Prell, K.A.2    Weiss, J.3    Hinrichs, J.4
  • 58
    • 0034072201 scopus 로고    scopus 로고
    • Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins
    • Kulmyrzaev A, Bryant C, McClements DJ. 2000. Influence of sucrose on the thermal denaturation, gelation, and emulsion stabilization of whey proteins. J. Agric. Food Chem. 48(5):1593-97
    • (2000) J. Agric. Food Chem. , vol.48 , Issue.5 , pp. 1593-1597
    • Kulmyrzaev, A.1    Bryant, C.2    McClements, D.J.3
  • 59
    • 0035062947 scopus 로고    scopus 로고
    • Chemistry and physico-chemistry of phycocolloids
    • Lahaye M. 2001. Chemistry and physico-chemistry of phycocolloids. Cah. Biol. Mar. 42:137-57
    • (2001) Cah. Biol. Mar. , vol.42 , pp. 137-157
    • Lahaye, M.1
  • 60
    • 27544433098 scopus 로고    scopus 로고
    • Formula optimization of a low-fat food system containing whey protein isolate-xanthan gum complexes as fat replacer
    • Laneuville SI, Paquin P, Turgeon SL. 2005. Formula optimization of a low-fat food system containing whey protein isolate-xanthan gum complexes as fat replacer. J. Food Sci. 70(8):S513-19
    • (2005) J. Food Sci. , vol.70 , Issue.8 , pp. S513-S519
    • Laneuville, S.I.1    Paquin, P.2    Turgeon, S.L.3
  • 63
    • 33750943428 scopus 로고    scopus 로고
    • Interactions between furcellaran and the globular proteins bovine serum albumin and lactoglobulin
    • Laos K, Brownsey GJ, Ring SG. 2007. Interactions between furcellaran and the globular proteins bovine serum albumin and lactoglobulin. Carbohydr. Polym. 67(1):116-23
    • (2007) Carbohydr. Polym. , vol.67 , Issue.1 , pp. 116-123
    • Laos, K.1    Brownsey, G.J.2    Ring, S.G.3
  • 64
    • 84863771423 scopus 로고    scopus 로고
    • Complexation of bovine serum albumin and sugar beet pectin: Structural transitions and phase diagram
    • Li X, Fang Y, Al-Assaf S, Phillips GO, Yao X, et al. 2012. Complexation of bovine serum albumin and sugar beet pectin: structural transitions and phase diagram. Langmuir 28(27):10164-76
    • (2012) Langmuir , vol.28 , Issue.27 , pp. 10164-10176
    • Li, X.1    Fang, Y.2    Al-Assaf, S.3    Phillips, G.O.4    Yao, X.5
  • 65
    • 84880301964 scopus 로고    scopus 로고
    • Heat-induced colloidal interactions of whey proteins, sodium caseinate and gum Arabic in binary and ternary mixtures
    • Loveday SM, Ye A, Anema SG, Singh H. 2013. Heat-induced colloidal interactions of whey proteins, sodium caseinate and gum arabic in binary and ternary mixtures. Food Res. Int. 54(1):111-17
    • (2013) Food Res. Int. , vol.54 , Issue.1 , pp. 111-117
    • Loveday, S.M.1    Ye, A.2    Anema, S.G.3    Singh, H.4
  • 66
    • 3042686006 scopus 로고    scopus 로고
    • Therapeutic applications of whey protein
    • Marshall K. 2004. Therapeutic applications of whey protein. Altern. Med. Rev. J. Clin. Ther. 9(2):136-56
    • (2004) Altern. Med. Rev. J. Clin. Ther. , vol.9 , Issue.2 , pp. 136-156
    • Marshall, K.1
  • 67
    • 0025264701 scopus 로고
    • Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids
    • Mascotti DP, Lohman TM. 1990. Thermodynamic extent of counterion release upon binding oligolysines to single-stranded nucleic acids. PNAS 87(8):3142-46
    • (1990) PNAS , vol.87 , Issue.8 , pp. 3142-3146
    • Mascotti, D.P.1    Lohman, T.M.2
  • 69
    • 67650035441 scopus 로고    scopus 로고
    • Structural design principles for delivery of bioactive components in nutraceuticals and functional foods
    • McClements DJ, Decker EA, Park Y, Weiss J. 2009. Structural design principles for delivery of bioactive components in nutraceuticals and functional foods. Crit. Rev. Food Sci. Nutr. 49(6):577-606
    • (2009) Crit. Rev. Food Sci. Nutr. , vol.49 , Issue.6 , pp. 577-606
    • McClements, D.J.1    Decker, E.A.2    Park, Y.3    Weiss, J.4
  • 70
    • 11844303475 scopus 로고    scopus 로고
    • PH-Induced structural transitions during complexation and coacervation of lactoglobulin and acacia gum
    • Mekhloufi G, Sanchez C, Renard D, Guillemin S, Hardy J. 2005. PH-Induced structural transitions during complexation and coacervation of lactoglobulin and acacia gum. Langmuir 21(1):386-94
    • (2005) Langmuir , vol.21 , Issue.1 , pp. 386-394
    • Mekhloufi, G.1    Sanchez, C.2    Renard, D.3    Guillemin, S.4    Hardy, J.5
  • 71
    • 0027765190 scopus 로고
    • Thermal behavior of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity
    • PaulssonMA, Svensson U, Kishore AR, Satyanarayan Naidu A. 1993. Thermal behavior of bovine lactoferrin in water and its relation to bacterial interaction and antibacterial activity. J. Dairy Sci. 76(12):3711-20
    • (1993) J. Dairy Sci. , vol.76 , Issue.12 , pp. 3711-3720
    • Paulsson, M.A.1    Svensson, U.2    Kishore, A.R.3    Satyanarayan Naidu, A.4
  • 72
    • 77956092764 scopus 로고    scopus 로고
    • Fabrication and morphological characterization of biopolymer particles formed by electrostatic complexation of heat treated lactoferrin and anionic polysaccharides
    • Peinado I, Lesmes U, Andrés A, McClements JD. 2010. Fabrication and morphological characterization of biopolymer particles formed by electrostatic complexation of heat treated lactoferrin and anionic polysaccharides. Langmuir 26(12):9827-34
    • (2010) Langmuir , vol.26 , Issue.12 , pp. 9827-9834
    • Peinado, I.1    Lesmes, U.2    Andrés, A.3    McClements, J.D.4
  • 73
    • 0001244556 scopus 로고    scopus 로고
    • Interaction and stabilization of acidified casein dispersions with low and high methoxyl pectins
    • Pereyra R, Schmidt KA, Wicker L. 1997. Interaction and stabilization of acidified casein dispersions with low and high methoxyl pectins. J. Agric. Food Chem. 45(9):3448-51
    • (1997) J. Agric. Food Chem. , vol.45 , Issue.9 , pp. 3448-3451
    • Pereyra, R.1    Schmidt, K.A.2    Wicker, L.3
  • 74
    • 84898000162 scopus 로고    scopus 로고
    • Investigation of molecular interactions between lactoglobulin and sugar beet pectin by multi-detection HPSEC
    • Qi PX, Chau HK, Fishman ML, Wickham ED, Hotchkiss AT. 2014. Investigation of molecular interactions between lactoglobulin and sugar beet pectin by multi-detection HPSEC. Carbohydr. Polym. 107:198-208
    • (2014) Carbohydr. Polym. , vol.107 , pp. 198-208
    • Qi, P.X.1    Chau, H.K.2    Fishman, M.L.3    Wickham, E.D.4    Hotchkiss, A.T.5
  • 75
    • 84866147397 scopus 로고    scopus 로고
    • Effect of whey protein-alginate wall systems on survival ofmicroencapsulated Lactobacillus plantarum in simulated gastrointestinal conditions
    • Rajam R, Karthik P, Parthasarathi S, Joseph GS, Anandharamakrishnan C. 2012. Effect of whey protein-alginate wall systems on survival ofmicroencapsulated Lactobacillus plantarum in simulated gastrointestinal conditions. J. Funct. Foods 4(4):891-98
    • (2012) J. Funct. Foods , vol.4 , Issue.4 , pp. 891-898
    • Rajam, R.1    Karthik, P.2    Parthasarathi, S.3    Joseph, G.S.4    Anandharamakrishnan, C.5
  • 76
    • 33747846583 scopus 로고    scopus 로고
    • Chitin and chitosan: Properties and applications
    • Rinaudo M. 2006. Chitin and chitosan: properties and applications. Prog. Polym. Sci. 31(7):603-32
    • (2006) Prog. Polym. Sci. , vol.31 , Issue.7 , pp. 603-632
    • Rinaudo, M.1
  • 77
    • 84862817005 scopus 로고    scopus 로고
    • Turbidity and rheological properties of bovine serum albumin/pectin coacervates: Effect of salt concentration and initial protein/polysaccharide ratio
    • Ru Q, Wang Y, Lee J, Ding Y, Huang Q. 2012. Turbidity and rheological properties of bovine serum albumin/pectin coacervates: effect of salt concentration and initial protein/polysaccharide ratio. Carbohydr. Polym. 88(3):838-46
    • (2012) Carbohydr. Polym. , vol.88 , Issue.3 , pp. 838-846
    • Ru, Q.1    Wang, Y.2    Lee, J.3    Ding, Y.4    Huang, Q.5
  • 78
    • 84894622246 scopus 로고    scopus 로고
    • Effect of pectin type on association and pH stability of whey protein-pectin complexes
    • Salminen H, Weiss J. 2013. Effect of pectin type on association and pH stability of whey protein-pectin complexes. Food Biophys. 9(1):29-38
    • (2013) Food Biophys. , vol.9 , Issue.1 , pp. 29-38
    • Salminen, H.1    Weiss, J.2
  • 79
    • 33744548946 scopus 로고    scopus 로고
    • Complex coacervation between lactoglobulin and acacia gum: A nucleation and growth mechanism
    • Sanchez C, Mekhloufi G, Renard D. 2006. Complex coacervation between lactoglobulin and acacia gum: a nucleation and growth mechanism. J. Colloid Interface Sci. 299(2):867-73
    • (2006) J. Colloid Interface Sci. , vol.299 , Issue.2 , pp. 867-873
    • Sanchez, C.1    Mekhloufi, G.2    Renard, D.3
  • 80
    • 48749127279 scopus 로고    scopus 로고
    • Core-shell biopolymer nanoparticles produced by electrostatic deposition of beet pectin onto heat-denatured lactoglobulin aggregates
    • Santipanichwong R, Suphantharika M, Weiss J, McClements DJ. 2008. Core-shell biopolymer nanoparticles produced by electrostatic deposition of beet pectin onto heat-denatured lactoglobulin aggregates. J. Food Sci. 73(6):23-30
    • (2008) J. Food Sci. , vol.73 , Issue.6 , pp. 23-30
    • Santipanichwong, R.1    Suphantharika, M.2    Weiss, J.3    McClements, D.J.4
  • 81
    • 0032197212 scopus 로고    scopus 로고
    • Structure and technofunctional properties of proteinpolysaccharide complexes: A review
    • SchmittC, Sanchez C, Desobry-Banon S, Hardy J. 1998. Structure and technofunctional properties of proteinpolysaccharide complexes: a review. Crit. Rev. Food Sci. Nutr. 38(8):689-753
    • (1998) Crit. Rev. Food Sci. Nutr. , vol.38 , Issue.8 , pp. 689-753
    • Schmitt, C.1    Sanchez, C.2    Desobry-Banon, S.3    Hardy, J.4
  • 82
    • 80052477682 scopus 로고    scopus 로고
    • Protein/polysaccharide complexes and coacervates in food systems
    • Schmitt C, Turgeon SL. 2011. Protein/polysaccharide complexes and coacervates in food systems. Adv. Colloid Interface Sci. 167(1-2):63-70
    • (2011) Adv. Colloid Interface Sci. , vol.167 , Issue.1-2 , pp. 63-70
    • Schmitt, C.1    Turgeon, S.L.2
  • 83
    • 0038071858 scopus 로고    scopus 로고
    • Ionic strength dependence of protein-polyelectrolyte interactions
    • Seyrek E, Dubin PL, Tribet C, Gamble EA. 2003. Ionic strength dependence of protein-polyelectrolyte interactions. Biomacromolecules 4(2):273-82
    • (2003) Biomacromolecules , vol.4 , Issue.2 , pp. 273-282
    • Seyrek, E.1    Dubin, P.L.2    Tribet, C.3    Gamble, E.A.4
  • 84
    • 41349108866 scopus 로고    scopus 로고
    • Dissolution of a polyelectrolyte-macroion complex by addition of salt
    • Skepö M, Linse P. 2002. Dissolution of a polyelectrolyte-macroion complex by addition of salt. Phys. Rev. E 66(5):051807
    • (2002) Phys. Rev. E , vol.66 , Issue.5 , pp. 051807
    • Skepö, M.1    Linse, P.2
  • 85
    • 0015002261 scopus 로고
    • Estimation of the relative stiffness of the molecular chain in polyelectrolytes from measurements of viscosity at different ionic strengths
    • Smidsrød O, Haug A. 1971. Estimation of the relative stiffness of the molecular chain in polyelectrolytes from measurements of viscosity at different ionic strengths. Biopolymers 10(7):1213-27
    • (1971) Biopolymers , vol.10 , Issue.7 , pp. 1213-1227
    • Smidsrød, O.1    Haug, A.2
  • 87
    • 80155211192 scopus 로고    scopus 로고
    • Formation and functionality of whey protein isolate-(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes
    • Stone AK, Nickerson MT. 2012. Formation and functionality of whey protein isolate-(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes. Food Hydrocoll. 27(2):271-77
    • (2012) Food Hydrocoll. , vol.27 , Issue.2 , pp. 271-277
    • Stone, A.K.1    Nickerson, M.T.2
  • 88
    • 0001662870 scopus 로고
    • Chemistry of milk protein
    • ed. PF Fox, London: Appl. Sci. Publ
    • Swaisgood HE. 1982. Chemistry of milk protein. In Developments in Dairy Chemistry, ed. PF Fox, pp. 1-59. London: Appl. Sci. Publ.
    • (1982) Developments in Dairy Chemistry , pp. 1-59
    • Swaisgood, H.E.1
  • 89
    • 2142776684 scopus 로고    scopus 로고
    • On the mechanism of stabilisation of acidified milk drinks by pectin
    • Tromp RH, de Kruif CG, van Eijk M, Rolin C. 2004. On the mechanism of stabilisation of acidified milk drinks by pectin. Food Hydrocoll. 18(4):565-72
    • (2004) Food Hydrocoll. , vol.18 , Issue.4 , pp. 565-572
    • Tromp, R.H.1    De Kruif, C.G.2    Van Eijk, M.3    Rolin, C.4
  • 90
    • 77953171338 scopus 로고    scopus 로고
    • Protein + polysaccharide coacervates and complexes: From scientific background to their application as functional ingredients in food products
    • ed. S Kasapis, IT Norton, JB Ubbink, Oxford: Acad. Press
    • Turgeon SL, Laneuville SI. 2009. Protein + polysaccharide coacervates and complexes: from scientific background to their application as functional ingredients in food products. In Modern Biopolymer Science, ed. S Kasapis, IT Norton, JB Ubbink, pp. 327-63. Oxford: Acad. Press
    • (2009) Modern Biopolymer Science , pp. 327-363
    • Turgeon, S.L.1    Laneuville, S.I.2
  • 92
    • 52149109329 scopus 로고    scopus 로고
    • Colloidal delivery systems for micronutrients and nutraceuticals
    • Velikov KP, Pelan E. 2008. Colloidal delivery systems for micronutrients and nutraceuticals. Soft Matter 4(10):1964-80
    • (2008) Soft Matter , vol.4 , Issue.10 , pp. 1964-1980
    • Velikov, K.P.1    Pelan, E.2
  • 93
  • 94
    • 84938851244 scopus 로고    scopus 로고
    • Foaming properties of whey protein isolate and carrageenan mixed systems
    • Wang Z, Zhang S, Vardhanabhuti B. 2015. Foaming properties of whey protein isolate and carrageenan mixed systems. J. Food Sci. 80(8):1893-902
    • (2015) J. Food Sci. , vol.80 , Issue.8 , pp. 1893-1902
    • Wang, Z.1    Zhang, S.2    Vardhanabhuti, B.3
  • 96
    • 11244330472 scopus 로고    scopus 로고
    • Microencapsulation of oils using whey protein/gum Arabic coacervates
    • Weinbreck F, Minor M, de Kruif CG. 2004a. Microencapsulation of oils using whey protein/gum arabic coacervates. J. Microencapsul. 21(6):667-79
    • (2004) J. Microencapsul. , vol.21 , Issue.6 , pp. 667-679
    • Weinbreck, F.1    Minor, M.2    De Kruif, C.G.3
  • 97
    • 0242576090 scopus 로고    scopus 로고
    • Complex formation of whey proteins: Exocellular polysaccharide EPS B40
    • Weinbreck F, Nieuwenhuijse H, Robijn GW, de Kruif CG. 2003b. Complex formation of whey proteins: exocellular polysaccharide EPS B40. Langmuir 19(22):9404-10
    • (2003) Langmuir , vol.19 , Issue.22 , pp. 9404-9410
    • Weinbreck, F.1    Nieuwenhuijse, H.2    Robijn, G.W.3    De Kruif, C.G.4
  • 100
    • 0031405402 scopus 로고    scopus 로고
    • Xanthan gum effects on solubility and emulsification properties of soy protein isolate
    • Xie YR, Hettiarachchy NS. 1997. Xanthan gum effects on solubility and emulsification properties of soy protein isolate. J. Food Sci. 62(6):1101-4
    • (1997) J. Food Sci. , vol.62 , Issue.6 , pp. 1101-1104
    • Xie, Y.R.1    Hettiarachchy, N.S.2
  • 101
    • 84890954551 scopus 로고    scopus 로고
    • Intragastric gelation of whey protein-pectin alters the digestibility of whey protein during in vitro pepsin digestion
    • Zhang S, Vardhanabhuti B. 2014. Intragastric gelation of whey protein-pectin alters the digestibility of whey protein during in vitro pepsin digestion. Food Funct. 5(1):102-10
    • (2014) Food Funct. , vol.5 , Issue.1 , pp. 102-110
    • Zhang, S.1    Vardhanabhuti, B.2
  • 102
    • 84870666233 scopus 로고    scopus 로고
    • Raman spectroscopic characterization of structural changes in heated whey protein isolate upon soluble complex formation with pectin at near neutral pH
    • Zhang S, Zhang Z, LinM, Vardhanabhuti B. 2012. Raman spectroscopic characterization of structural changes in heated whey protein isolate upon soluble complex formation with pectin at near neutral pH. J. Agric. Food Chem. 60(48):12029-35
    • (2012) J. Agric. Food Chem. , vol.60 , Issue.48 , pp. 12029-12035
    • Zhang, S.1    Zhang, Z.2    Lin, M.3    Vardhanabhuti, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.