메뉴 건너뛰기




Volumn 55, Issue , 2016, Pages 89-99

On the complexation of whey proteins

Author keywords

Electrostatic interactions; Heteroprotein association; Ionic strength; Milk proteins; Molecular modeling; pH

Indexed keywords


EID: 84947556525     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2015.11.010     Document Type: Article
Times cited : (29)

References (94)
  • 2
    • 84940923088 scopus 로고    scopus 로고
    • Structure and functions of lactoferrin as ingredient in infant formulas
    • Aly E., Ros G., Frontela C. Structure and functions of lactoferrin as ingredient in infant formulas. Journal of Food Research 2013, 2(4):25-36.
    • (2013) Journal of Food Research , vol.2 , Issue.4 , pp. 25-36
    • Aly, E.1    Ros, G.2    Frontela, C.3
  • 4
    • 0344084441 scopus 로고    scopus 로고
    • Non-food applications of milk components and dairy co-products: a review
    • Audica J.-L., Chaufera B., Daufin G. Non-food applications of milk components and dairy co-products: a review. Le Lait 2003, 83:417-438.
    • (2003) Le Lait , vol.83 , pp. 417-438
    • Audica, J.-L.1    Chaufera, B.2    Daufin, G.3
  • 7
    • 68949206934 scopus 로고    scopus 로고
    • Springer Science Business Media, New York, Z. Bösze (Ed.)
    • Bioactive components of milk 2008, Springer Science Business Media, New York. 1st ed. Z. Bösze (Ed.).
    • (2008) Bioactive components of milk
  • 8
    • 33744487675 scopus 로고    scopus 로고
    • Monte Carlo and modified Tanford-Kirkwood results for macromolecular electrostatics calculations
    • de Carvalho S.J., Ghiotto R.T., da Silva F.L.B. Monte Carlo and modified Tanford-Kirkwood results for macromolecular electrostatics calculations. Journal of Physical Chemistry B 2006, 110:8832-8839.
    • (2006) Journal of Physical Chemistry B , vol.110 , pp. 8832-8839
    • de Carvalho, S.J.1    Ghiotto, R.T.2    da Silva, F.L.B.3
  • 9
    • 0038397268 scopus 로고    scopus 로고
    • Biodefense properties of milk: the role of antimicrobial proteins and peptides
    • Clare D.A., Catignani G.L., Swaisgood H.E. Biodefense properties of milk: the role of antimicrobial proteins and peptides. Current Pharmaceutical Design 2003, 9:1239-1255.
    • (2003) Current Pharmaceutical Design , vol.9 , pp. 1239-1255
    • Clare, D.A.1    Catignani, G.L.2    Swaisgood, H.E.3
  • 10
    • 79955612452 scopus 로고    scopus 로고
    • Expanded functionality of modified whey protein dispersions after transglutaminase catalysis peptides
    • Clare D.A., Daubert C.R. Expanded functionality of modified whey protein dispersions after transglutaminase catalysis peptides. Journal of Food Science 2011, 76(4):C576-C584.
    • (2011) Journal of Food Science , vol.76 , Issue.4 , pp. C576-C584
    • Clare, D.A.1    Daubert, C.R.2
  • 11
    • 69249089296 scopus 로고    scopus 로고
    • Polyelectrolyte-protein complexation driven by charge regulation
    • Da Silva F.L.B., Jönsson B. Polyelectrolyte-protein complexation driven by charge regulation. Soft Matter 2009, 5(15):2862-2868.
    • (2009) Soft Matter , vol.5 , Issue.15 , pp. 2862-2868
    • Da Silva, F.L.B.1    Jönsson, B.2
  • 12
    • 0003176491 scopus 로고
    • Bovine milk protein properties and the manufacturing quality of milk
    • Dalgleish D.G. Bovine milk protein properties and the manufacturing quality of milk. Livestock Production Science 1992, 35:75-93.
    • (1992) Livestock Production Science , vol.35 , pp. 75-93
    • Dalgleish, D.G.1
  • 13
    • 42149164796 scopus 로고    scopus 로고
    • Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions
    • Dickinson E. Interfacial structure and stability of food emulsions as affected by protein-polysaccharide interactions. Soft Matter 2008, 4:932-942.
    • (2008) Soft Matter , vol.4 , pp. 932-942
    • Dickinson, E.1
  • 14
    • 84874022478 scopus 로고    scopus 로고
    • Stabilising emulsion-based colloidal structures with mixed food ingredients
    • Dickinson E. Stabilising emulsion-based colloidal structures with mixed food ingredients. Journal of the Science of Food and Agriculture 2013, 93:710-721.
    • (2013) Journal of the Science of Food and Agriculture , vol.93 , pp. 710-721
    • Dickinson, E.1
  • 15
    • 43749113594 scopus 로고    scopus 로고
    • Aggregation in β-lactoglobulin
    • Donald A.M. Aggregation in β-lactoglobulin. Soft Matter 2000, 4:1147-1150.
    • (2000) Soft Matter , vol.4 , pp. 1147-1150
    • Donald, A.M.1
  • 16
    • 84870815649 scopus 로고    scopus 로고
    • Cold-set whey protein microgels for the stable immobilization of lipids
    • Egan T., Jacquier J.-C., Rosenberg Y., Rosenberg M. Cold-set whey protein microgels for the stable immobilization of lipids. Food Hydrocolloids 2013, 31:317-324.
    • (2013) Food Hydrocolloids , vol.31 , pp. 317-324
    • Egan, T.1    Jacquier, J.-C.2    Rosenberg, Y.3    Rosenberg, M.4
  • 17
    • 84896737169 scopus 로고    scopus 로고
    • Cold-set whey protein microgels as ph modulated immobilisation matrices for charged bioactives
    • Egan T., O'Riordan D., O'Sullivan M., Jacquier J.-C. Cold-set whey protein microgels as ph modulated immobilisation matrices for charged bioactives. Food Chemistry 2014, 156:197-203.
    • (2014) Food Chemistry , vol.156 , pp. 197-203
    • Egan, T.1    O'Riordan, D.2    O'Sullivan, M.3    Jacquier, J.-C.4
  • 18
    • 79958699963 scopus 로고    scopus 로고
    • Lactoferrin in relation to biological functions and applications: a review
    • El-Loly M.M., Mahfouz M.B. Lactoferrin in relation to biological functions and applications: a review. International Journal of Dairy Science 2011, 6(2):79-111.
    • (2011) International Journal of Dairy Science , vol.6 , Issue.2 , pp. 79-111
    • El-Loly, M.M.1    Mahfouz, M.B.2
  • 19
    • 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 C.J., Adhikari B.P. Complex coacervation with whey protein isolate and gum arabic for the microencapsulation of omega-3 rich tuna oil. Food & Function 2014, 5:2743-2750.
    • (2014) Food & Function , vol.5 , pp. 2743-2750
    • Eratte, D.1    Wang, B.2    Dowling, K.3    Barrow, C.J.4    Adhikari, B.P.5
  • 20
    • 52949152374 scopus 로고    scopus 로고
    • Earliest date for milk use in the near east and southeastern europe linked to cattle herding
    • Evershed R.P., Payne S., Sherratt A.G., Copley M.S., Coolidge J., Urem-Kotsu D., et al. Earliest date for milk use in the near east and southeastern europe linked to cattle herding. Nature 2008, 455:528-531.
    • (2008) Nature , vol.455 , pp. 528-531
    • Evershed, R.P.1    Payne, S.2    Sherratt, A.G.3    Copley, M.S.4    Coolidge, J.5    Urem-Kotsu, D.6
  • 24
    • 44649154950 scopus 로고    scopus 로고
    • Attractive interactions between selected anionic exopolysaccharides and milk proteins
    • Girard M., Schaffer-Lequart C. Attractive interactions between selected anionic exopolysaccharides and milk proteins. Food Hydrocolloids 2007, 22:1425-1434.
    • (2007) Food Hydrocolloids , vol.22 , pp. 1425-1434
    • Girard, M.1    Schaffer-Lequart, C.2
  • 25
    • 0042532737 scopus 로고    scopus 로고
    • Protein self-association in solution: the bovine β-lactoglobulin dimer and octamer
    • Gottschalk M., Nilsson H., Roos H., Halle B. Protein self-association in solution: the bovine β-lactoglobulin dimer and octamer. Protein Science 2003, 12:2404-2411.
    • (2003) Protein Science , vol.12 , pp. 2404-2411
    • Gottschalk, M.1    Nilsson, H.2    Roos, H.3    Halle, B.4
  • 26
    • 21244497694 scopus 로고    scopus 로고
    • Characterization of polyanionprotein complexes by frontal analysis continuous capillary electrophoresis and small angle neutron scattering: effect of polyanion flexibility
    • Hattori T., Bataldar S., Kato R., Bohidar H., Dubin P. Characterization of polyanionprotein complexes by frontal analysis continuous capillary electrophoresis and small angle neutron scattering: effect of polyanion flexibility. Analytical Biochemistry 2005, 342(2):229-236.
    • (2005) Analytical Biochemistry , vol.342 , Issue.2 , pp. 229-236
    • Hattori, T.1    Bataldar, S.2    Kato, R.3    Bohidar, H.4    Dubin, P.5
  • 27
    • 0034768130 scopus 로고    scopus 로고
    • Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment
    • Havea P., Singh H., Creamer L.K. Characterization of heat-induced aggregates of beta-lactoglobulin, alpha-lactalbumin and bovine serum albumin in a whey protein concentrate environment. Journal of Dairy Research 2001, 68(3):483-497.
    • (2001) Journal of Dairy Research , vol.68 , Issue.3 , pp. 483-497
    • Havea, P.1    Singh, H.2    Creamer, L.K.3
  • 28
    • 0015243893 scopus 로고
    • Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility
    • Hekman A. Association of lactoferrin with other proteins, as demonstrated by changes in electrophoretic mobility. Biochimica et Biophysica Acta (BBA) - Protein Structure 1971, 251(3):380-387.
    • (1971) Biochimica et Biophysica Acta (BBA) - Protein Structure , vol.251 , Issue.3 , pp. 380-387
    • Hekman, A.1
  • 30
    • 0031310473 scopus 로고    scopus 로고
    • Characterization and partial purification of bovine α-lactalbumin and β-casein produced in milk of transgenic mice
    • Jeng S.-Y., Bleck G.T., Wheeler M.B., Jime R. Characterization and partial purification of bovine α-lactalbumin and β-casein produced in milk of transgenic mice. Journal of Dairy Science 1997, 80:3167-3175.
    • (1997) Journal of Dairy Science , vol.80 , pp. 3167-3175
    • Jeng, S.-Y.1    Bleck, G.T.2    Wheeler, M.B.3    Jime, R.4
  • 32
    • 58149155020 scopus 로고    scopus 로고
    • Electrostatics in macromolecular solution
    • Royal Society of Chemistry, Londres, E. Dickinson, M.E. Leser (Eds.)
    • Jönsson B., Lund M., da Silva F.L.B. Electrostatics in macromolecular solution. Food colloids: Self-assembly and material science 2007, 129-154. Royal Society of Chemistry, Londres. E. Dickinson, M.E. Leser (Eds.).
    • (2007) Food colloids: Self-assembly and material science , pp. 129-154
    • Jönsson, B.1    Lund, M.2    da Silva, F.L.B.3
  • 36
  • 37
    • 0032422201 scopus 로고    scopus 로고
    • Impact of processing on bioactive proteins and peptides
    • Korhonen H. Impact of processing on bioactive proteins and peptides. Trends in Food Science & Technology 1998, 9(8-9):307-319.
    • (1998) Trends in Food Science & Technology , vol.9 , Issue.8-9 , pp. 307-319
    • Korhonen, H.1
  • 39
    • 84969188108 scopus 로고    scopus 로고
    • Dimerization of terminal domains in spiders silk proteins is controlled by electrostatic anisotropy and modulated by hydrophobic patches
    • Kurut A., Dicko C., Lund M. Dimerization of terminal domains in spiders silk proteins is controlled by electrostatic anisotropy and modulated by hydrophobic patches. ACS Biomaterials Science & Engineering 2015, 1(6):363-371.
    • (2015) ACS Biomaterials Science & Engineering , vol.1 , Issue.6 , pp. 363-371
    • Kurut, A.1    Dicko, C.2    Lund, M.3
  • 40
    • 84858665589 scopus 로고    scopus 로고
    • Anisotropic interactions in protein mixtures: self assembly and phase behavior in aqueous solution
    • Kurut A., Persson B.A., Åkesson T., Forsman J., Lund M. Anisotropic interactions in protein mixtures: self assembly and phase behavior in aqueous solution. Journal of Physical Chemistry Letters 2012, 3(6):731-734.
    • (2012) Journal of Physical Chemistry Letters , vol.3 , Issue.6 , pp. 731-734
    • Kurut, A.1    Persson, B.A.2    Åkesson, T.3    Forsman, J.4    Lund, M.5
  • 42
    • 33750943428 scopus 로고    scopus 로고
    • Interactions between furcellaran and the globular proteins bovine serum albumin and β-lactoglobulin
    • Laos K., Brownsey G., Ring S. Interactions between furcellaran and the globular proteins bovine serum albumin and β-lactoglobulin. Carbohydrate Polymers 2007, 67(1):116-123.
    • (2007) Carbohydrate Polymers , vol.67 , Issue.1 , pp. 116-123
    • Laos, K.1    Brownsey, G.2    Ring, S.3
  • 43
    • 0029666602 scopus 로고    scopus 로고
    • Light scattering studies of the binding of bovine serum albumin to a cationic polyelectrolyte
    • Li Y., Mattison K.W., Dubin P.L., Havel H.A., Edwards S.L. Light scattering studies of the binding of bovine serum albumin to a cationic polyelectrolyte. Biopolymers 1996, 38(4):527-533.
    • (1996) Biopolymers , vol.38 , Issue.4 , pp. 527-533
    • Li, Y.1    Mattison, K.W.2    Dubin, P.L.3    Havel, H.A.4    Edwards, S.L.5
  • 44
    • 0029130333 scopus 로고
    • Lactoferrin: molecular structure and biological function
    • Lönnerdal B., Iyer S. Lactoferrin: molecular structure and biological function. Annual Review of Nutrition 1995, 15:93-110.
    • (1995) Annual Review of Nutrition , vol.15 , pp. 93-110
    • Lönnerdal, B.1    Iyer, S.2
  • 45
    • 47649095644 scopus 로고    scopus 로고
    • Albumin adsorption to contact lens materials: a review
    • Luensmann D., Jones L. Albumin adsorption to contact lens materials: a review. Cont Lens Anterior Eye 2008, 31(4):179-187.
    • (2008) Cont Lens Anterior Eye , vol.31 , Issue.4 , pp. 179-187
    • Luensmann, D.1    Jones, L.2
  • 46
    • 0242290876 scopus 로고    scopus 로고
    • A mesoscopic model for protein-protein interactions in solution
    • Lund M., Jönsson B. A mesoscopic model for protein-protein interactions in solution. Biophysical Journal 2003, 85:2940-2947.
    • (2003) Biophysical Journal , vol.85 , pp. 2940-2947
    • Lund, M.1    Jönsson, B.2
  • 48
    • 51149205529 scopus 로고
    • Calculation of thermodynamic properties of polyelectrolytes
    • Marcus R.A. Calculation of thermodynamic properties of polyelectrolytes. Journal of Chemical Physics 1955, 23:1057.
    • (1955) Journal of Chemical Physics , vol.23 , pp. 1057
    • Marcus, R.A.1
  • 49
    • 84887380806 scopus 로고    scopus 로고
    • Springer Science Business Media, New York, P.L. McSweeney, P.F. Fox (Eds.)
    • Advanced dairy chemistry - Proteins: Basic aspects 2013, Springer Science Business Media, New York. 4th ed. P.L. McSweeney, P.F. Fox (Eds.).
    • (2013) Advanced dairy chemistry - Proteins: Basic aspects
  • 50
    • 84870170136 scopus 로고    scopus 로고
    • Hofmeister challenges: Ion binding and charge of the bsa protein as explicit examples
    • Medda L., Barse B., Cugia F., Boström M., Parsons D.F., Ninham B.W., et al. Hofmeister challenges: Ion binding and charge of the bsa protein as explicit examples. Langmuir 2012, 28:16355-16363.
    • (2012) Langmuir , vol.28 , pp. 16355-16363
    • Medda, L.1    Barse, B.2    Cugia, F.3    Boström, M.4    Parsons, D.F.5    Ninham, B.W.6
  • 52
    • 33947467623 scopus 로고
    • The interaction of proteins with synthetic polyelectrolytes. I. Complexing of bovine serum albumin
    • Morawetz H., Hughes W.L. The interaction of proteins with synthetic polyelectrolytes. I. Complexing of bovine serum albumin. The Journal of Physical Chemistry 1952, 56(1):64-69.
    • (1952) The Journal of Physical Chemistry , vol.56 , Issue.1 , pp. 64-69
    • Morawetz, H.1    Hughes, W.L.2
  • 54
    • 51049101653 scopus 로고    scopus 로고
    • Formation and stability of α-lactalbumin-lysozyme spherical particles: Involvement of electrostatic forces
    • Nigen M., Croguennec T., Bouhallab S. Formation and stability of α-lactalbumin-lysozyme spherical particles: Involvement of electrostatic forces. Food Hydrocolloids 2009, 23(2):510-518.
    • (2009) Food Hydrocolloids , vol.23 , Issue.2 , pp. 510-518
    • Nigen, M.1    Croguennec, T.2    Bouhallab, S.3
  • 55
    • 61649105725 scopus 로고    scopus 로고
    • Molecular interaction between apo or holo α-lactalbumin and lysozyme: formation of heterodimers as assessed by fluorescence measurements
    • Nigen M., Tilly V., Croguennec T., Drouinkucma D., Bouhallab S. Molecular interaction between apo or holo α-lactalbumin and lysozyme: formation of heterodimers as assessed by fluorescence measurements. Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics 2009, 1794(4):709-715.
    • (2009) Biochimica et Biophysica Acta (BBA) - Proteins & Proteomics , vol.1794 , Issue.4 , pp. 709-715
    • Nigen, M.1    Tilly, V.2    Croguennec, T.3    Drouinkucma, D.4    Bouhallab, S.5
  • 56
    • 0001461682 scopus 로고
    • Examination of titration behavior
    • Nozaki Y., Tanford C. Examination of titration behavior. Methods Enzymol 1967, 11:715-734.
    • (1967) Methods Enzymol , vol.11 , pp. 715-734
    • Nozaki, Y.1    Tanford, C.2
  • 57
    • 33745908901 scopus 로고    scopus 로고
    • Towards control of aggregational behaviour of α-lactalbumin at acidic pH
    • Pedersen J.B., Fojan P., Sorensen J., Petersen S.B. Towards control of aggregational behaviour of α-lactalbumin at acidic pH. Journal of Fluorescence 2006, 16(2):611-621.
    • (2006) Journal of Fluorescence , vol.16 , Issue.2 , pp. 611-621
    • Pedersen, J.B.1    Fojan, P.2    Sorensen, J.3    Petersen, S.B.4
  • 58
    • 2442575245 scopus 로고    scopus 로고
    • No need to be HAMLET or BAMLET to interact with histones: binding of monomeric α-lactalbumin to histones and basic poly-amino acids
    • Permyakov S.E., Pershikova I.V., Khokhlova T.I., Uversky V.N., Permyakov E.A. No need to be HAMLET or BAMLET to interact with histones: binding of monomeric α-lactalbumin to histones and basic poly-amino acids. Biochemistry 2004, 43(19):5575-5582.
    • (2004) Biochemistry , vol.43 , Issue.19 , pp. 5575-5582
    • Permyakov, S.E.1    Pershikova, I.V.2    Khokhlova, T.I.3    Uversky, V.N.4    Permyakov, E.A.5
  • 60
    • 84887346615 scopus 로고
    • Interaction of bovine beta-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids
    • Puyol P., Perez D.M., Ena J.M., Calvo M. Interaction of bovine beta-lactoglobulin and other bovine and human whey proteins with retinol and fatty acids. Agricultural and Biological Chemistry 1991, 55(10):2515-2520.
    • (1991) Agricultural and Biological Chemistry , vol.55 , Issue.10 , pp. 2515-2520
    • Puyol, P.1    Perez, D.M.2    Ena, J.M.3    Calvo, M.4
  • 63
    • 84908463104 scopus 로고    scopus 로고
    • Formation of soluble whey protein aggregates and their stability in beverages
    • Ryan K.N., Foegeding E.A. Formation of soluble whey protein aggregates and their stability in beverages. Food Hydrocolloids 2015, 43:265-274.
    • (2015) Food Hydrocolloids , vol.43 , pp. 265-274
    • Ryan, K.N.1    Foegeding, E.A.2
  • 65
    • 48449103710 scopus 로고    scopus 로고
    • Role of protein in cosmetics
    • Secchi G. Role of protein in cosmetics. Clinics in Dermatology 2008, 26(4):321-325.
    • (2008) Clinics in Dermatology , vol.26 , Issue.4 , pp. 321-325
    • Secchi, G.1
  • 66
    • 4344568255 scopus 로고    scopus 로고
    • Frontal analysis continuous capillary electrophoresis for protein-polyelectrolyte binding studies
    • Humana Press Inc., Ch. 11, M.A. Strege, A.L. Lagu (Eds.)
    • Seyrek E., Hattori T., Dubin P.L. Frontal analysis continuous capillary electrophoresis for protein-polyelectrolyte binding studies. Methods in molecular Biology: Capillary electrophoresis of proteins and peptides 2004, 217-228. Humana Press Inc., Ch. 11. M.A. Strege, A.L. Lagu (Eds.).
    • (2004) Methods in molecular Biology: Capillary electrophoresis of proteins and peptides , pp. 217-228
    • Seyrek, E.1    Hattori, T.2    Dubin, P.L.3
  • 67
    • 84898888317 scopus 로고    scopus 로고
    • Effect of charge regulation and iondipole interactions on the selectivity of proteinnanoparticle binding
    • da Silva F.L.B., Boström M., Persson C. Effect of charge regulation and iondipole interactions on the selectivity of proteinnanoparticle binding. Langmuir 2014, 30(14):4078-4083.
    • (2014) Langmuir , vol.30 , Issue.14 , pp. 4078-4083
    • da Silva, F.L.B.1    Boström, M.2    Persson, C.3
  • 68
    • 0034974669 scopus 로고    scopus 로고
    • A critical investigation of the Tanford-Kirkwood scheme by means of Monte Carlo simulations
    • da Silva F.L.B., Jönsson B., Penfold R. A critical investigation of the Tanford-Kirkwood scheme by means of Monte Carlo simulations. Protein Science 2001, 10:1415-1425.
    • (2001) Protein Science , vol.10 , pp. 1415-1425
    • da Silva, F.L.B.1    Jönsson, B.2    Penfold, R.3
  • 70
    • 44549084148 scopus 로고    scopus 로고
    • Whey and whey proteins: from gutter-to-gold
    • Smithers G. Whey and whey proteins: from gutter-to-gold. International Dairy Journal 2008, 18(7):695-704.
    • (2008) International Dairy Journal , vol.18 , Issue.7 , pp. 695-704
    • Smithers, G.1
  • 72
    • 0035892451 scopus 로고    scopus 로고
    • The relationship between contact lens surface charge and in-vitro protein deposition levels
    • Soltys-Robitaille C., Ammon D.M., Valint P.L., Grobe G.L. The relationship between contact lens surface charge and in-vitro protein deposition levels. Biomaterials 2001, 22(24):3257-3260.
    • (2001) Biomaterials , vol.22 , Issue.24 , pp. 3257-3260
    • Soltys-Robitaille, C.1    Ammon, D.M.2    Valint, P.L.3    Grobe, G.L.4
  • 73
    • 0034492988 scopus 로고    scopus 로고
    • Occurrence, structure, biochemical properties and technological characteristics of lactoferrin
    • Steijns J.M., van Hooijdonk A.C.M. Occurrence, structure, biochemical properties and technological characteristics of lactoferrin. British Journal of Nutrition 2000, 84(Supplement, S1):11-17.
    • (2000) British Journal of Nutrition , vol.84 , pp. 11-17
    • Steijns, J.M.1    van Hooijdonk, A.C.M.2
  • 74
    • 84888355956 scopus 로고    scopus 로고
    • Faunus - a flexible framework for Monte Carlo simulation
    • Stenqvist B., Thuresson A., Kurut A., Vácha R., Lund M. Faunus - a flexible framework for Monte Carlo simulation. Mol Sim 2013, 39(14-15):1233-1239.
    • (2013) Mol Sim , vol.39 , Issue.14-15 , pp. 1233-1239
    • Stenqvist, B.1    Thuresson, A.2    Kurut, A.3    Vácha, R.4    Lund, M.5
  • 76
    • 0032029214 scopus 로고    scopus 로고
    • Polymer science concepts in dairy systems-an overview of milk protein and food hydrocolloid interaction
    • Syrbe A., Bauer W., Klostermeyer H. Polymer science concepts in dairy systems-an overview of milk protein and food hydrocolloid interaction. International Dairy Journal 1998, 8(3):179-193.
    • (1998) International Dairy Journal , vol.8 , Issue.3 , pp. 179-193
    • Syrbe, A.1    Bauer, W.2    Klostermeyer, H.3
  • 77
    • 0030915773 scopus 로고    scopus 로고
    • Significant role of electrostatic interactions for stabilization of protein assemblies
    • Takahashi T. Significant role of electrostatic interactions for stabilization of protein assemblies. Advances in Biophysics 1997, 34:41-54.
    • (1997) Advances in Biophysics , vol.34 , pp. 41-54
    • Takahashi, T.1
  • 81
    • 0036120646 scopus 로고    scopus 로고
    • Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety
    • Tenovuo J. Clinical applications of antimicrobial host proteins lactoperoxidase, lysozyme and lactoferrin in xerostomia: efficacy and safety. Oral Diseases 2002, 8(1):23-29.
    • (2002) Oral Diseases , vol.8 , Issue.1 , pp. 23-29
    • Tenovuo, J.1
  • 84
    • 34347394734 scopus 로고    scopus 로고
    • Molecular-weight distribution and structural transformation in water-soluble complexes of poly(acrylic acid) and bovine serum albumin
    • Topuzogullari M., Cimen N., Mustafaeva Z., Mustafaev M. Molecular-weight distribution and structural transformation in water-soluble complexes of poly(acrylic acid) and bovine serum albumin. European Polymer Journal 2007, 43(7):2935-2946.
    • (2007) European Polymer Journal , vol.43 , Issue.7 , pp. 2935-2946
    • Topuzogullari, M.1    Cimen, N.2    Mustafaeva, Z.3    Mustafaev, M.4
  • 85
    • 57849114390 scopus 로고    scopus 로고
    • PH-induced changes in adsorbed β-lactoglobulin molecules measured using atomic force microscopy
    • Touhami A., Dutcher J.R. pH-induced changes in adsorbed β-lactoglobulin molecules measured using atomic force microscopy. Soft Matter 2009, 5(1):220-227.
    • (2009) Soft Matter , vol.5 , Issue.1 , pp. 220-227
    • Touhami, A.1    Dutcher, J.R.2
  • 86
    • 0033198231 scopus 로고    scopus 로고
    • Adsorption of low molecular weight proteins to hemodialysis membranes: experimental results and simulations
    • Valette P., Thomas M., Déjardin P. Adsorption of low molecular weight proteins to hemodialysis membranes: experimental results and simulations. Biomaterials 1999, 20:1621-1634.
    • (1999) Biomaterials , vol.20 , pp. 1621-1634
    • Valette, P.1    Thomas, M.2    Déjardin, P.3
  • 87
    • 61649119636 scopus 로고    scopus 로고
    • Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability
    • Vardhanabhuti B., Yucel U., Coupland J.N., Foegedinga E.A. Interactions between β-lactoglobulin and dextran sulfate at near neutral pH and their effect on thermal stability. Food Hydrocolloids 2009, 23(6):1511-1520.
    • (2009) Food Hydrocolloids , vol.23 , Issue.6 , pp. 1511-1520
    • Vardhanabhuti, B.1    Yucel, U.2    Coupland, J.N.3    Foegedinga, E.A.4
  • 89
    • 0030149441 scopus 로고    scopus 로고
    • Protein separation via polyelectrolyte coacervation: selectivity and efficiency
    • Wang Y.-F., Gao J.Y., Dubin P.L. Protein separation via polyelectrolyte coacervation: selectivity and efficiency. Biotechnology Progress 1996, 12(3):356-362.
    • (1996) Biotechnology Progress , vol.12 , Issue.3 , pp. 356-362
    • Wang, Y.-F.1    Gao, J.Y.2    Dubin, P.L.3
  • 90
    • 84896539125 scopus 로고    scopus 로고
    • Springer Science Business Media, New York, R.R. Watson, S. Zibadi, V.R. Preedy (Eds.)
    • Dietary components and immune function 2010, Springer Science Business Media, New York. 1st ed. R.R. Watson, S. Zibadi, V.R. Preedy (Eds.).
    • (2010) Dietary components and immune function
  • 93
    • 84890654066 scopus 로고    scopus 로고
    • Heteroprotein complex coacervation: bovine β-Lactoglobulin and lactoferrin
    • Yan Y., Kizilay E., Seeman D., Flanagan S., Dubin P.L., Bovetto L., et al. Heteroprotein complex coacervation: bovine β-Lactoglobulin and lactoferrin. Langmuir 2013, 29:15614-15623.
    • (2013) Langmuir , vol.29 , pp. 15614-15623
    • Yan, Y.1    Kizilay, E.2    Seeman, D.3    Flanagan, S.4    Dubin, P.L.5    Bovetto, L.6
  • 94
    • 84931003985 scopus 로고    scopus 로고
    • Exposure of thiol groups in the heat-induced denaturation of β-lactoglobulin
    • Zeiler R.N.W., Bolhuis P.G. Exposure of thiol groups in the heat-induced denaturation of β-lactoglobulin. Mol Sim 2015, 41(10-12):1006-1014.
    • (2015) Mol Sim , vol.41 , Issue.10-12 , pp. 1006-1014
    • Zeiler, R.N.W.1    Bolhuis, P.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.