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Volumn 25, Issue , 2016, Pages 15-21

Impact of stirring speed on β-lactoglobulin fibril formation

Author keywords

fibril; morphology; stirring; zeta potential; lactoglobulin

Indexed keywords

PARTICLE SIZE; PARTICLE SIZE ANALYSIS; TURBIDITY; ZETA POTENTIAL;

EID: 84964744495     PISSN: 12267708     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10068-016-0093-8     Document Type: Article
Times cited : (24)

References (37)
  • 1
    • 33744457994 scopus 로고    scopus 로고
    • Investigating the permanent electric dipole moment of β-lactoglobulin fibrils, using transient electric birefringence
    • COI: 1:CAS:528:DC%2BD28XlsVKjurY%3D
    • Rogers SS, Venema P, van der Ploeg JPM, van der Linden E, Sagis LM, Donald AM. Investigating the permanent electric dipole moment of β-lactoglobulin fibrils, using transient electric birefringence. Biopolymers 82: 241–252 (2006)
    • (2006) Biopolymers , vol.82 , pp. 241-252
    • Rogers, S.S.1    Venema, P.2    van der Ploeg, J.P.M.3    van der Linden, E.4    Sagis, L.M.5    Donald, A.M.6
  • 3
    • 76849113758 scopus 로고    scopus 로고
    • Amyloid fibrils as a nanoscaffold for enzyme immobilization
    • COI: 1:CAS:528:DC%2BC3cXitlCitrY%3D
    • Pilkington SM, Roberts SJ, Meade SJ, Gerrard JA. Amyloid fibrils as a nanoscaffold for enzyme immobilization. Biotechnol. Progr. 26: 93–100 (2010)
    • (2010) Biotechnol. Progr. , vol.26 , pp. 93-100
    • Pilkington, S.M.1    Roberts, S.J.2    Meade, S.J.3    Gerrard, J.A.4
  • 4
    • 33845431968 scopus 로고    scopus 로고
    • Functional materials in food nanotechnology
    • Weiss J, Takhistov P, McClements DJ. Functional materials in food nanotechnology. J. Food Sci. 71: 107–116 (2006)
    • (2006) J. Food Sci. , vol.71 , pp. 107-116
    • Weiss, J.1    Takhistov, P.2    McClements, D.J.3
  • 6
    • 34347252586 scopus 로고    scopus 로고
    • The effect of heating on β-lactoglobulin-chitosan mixtures as influenced by pH and ionic strength
    • COI: 1:CAS:528:DC%2BD2sXnsVSqsrk%3D
    • Mounsey JS, O’Kennedy BT, Fenelon MA, Brodkorb A. The effect of heating on β-lactoglobulin-chitosan mixtures as influenced by pH and ionic strength. Food Hydrocolloid. 22: 65–73 (2008)
    • (2008) Food Hydrocolloid. , vol.22 , pp. 65-73
    • Mounsey, J.S.1    O’Kennedy, B.T.2    Fenelon, M.A.3    Brodkorb, A.4
  • 7
    • 0030993642 scopus 로고    scopus 로고
    • Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis
    • COI: 1:CAS:528:DyaK2sXjsFCms7c%3D
    • Qi XL, Holt C, McNulty D, Clarke DT, Brownlow S, Jones GR. Effect of temperature on the secondary structure of β-lactoglobulin at pH 6.7, as determined by CD and IR spectroscopy: A test of the molten globule hypothesis. Biochem. J. 324: 341–346 (1997)
    • (1997) Biochem. J. , vol.324 , pp. 341-346
    • Qi, X.L.1    Holt, C.2    McNulty, D.3    Clarke, D.T.4    Brownlow, S.5    Jones, G.R.6
  • 8
    • 0034467427 scopus 로고    scopus 로고
    • A large-scale isolation of native β-lactoglobulin: Characterization of physicochemical properties and comparison with other methods
    • COI: 1:CAS:528:DC%2BD3MXhvVaqtb4%3D
    • Konrad G, Lieske B, Faber W. A large-scale isolation of native β-lactoglobulin: Characterization of physicochemical properties and comparison with other methods. Int. Dairy J. 10: 713–721 (2000)
    • (2000) Int. Dairy J. , vol.10 , pp. 713-721
    • Konrad, G.1    Lieske, B.2    Faber, W.3
  • 9
    • 0037468659 scopus 로고    scopus 로고
    • A new ligand for an old lipocalin: Induced circular dichroism spectra reveal binding of bilirubin to bovine β-lactoglobulin
    • COI: 1:CAS:528:DC%2BD3sXitFams7c%3D
    • Zsila F. A new ligand for an old lipocalin: Induced circular dichroism spectra reveal binding of bilirubin to bovine β-lactoglobulin. FEBS Lett. 539: 85–90 (2003)
    • (2003) FEBS Lett. , vol.539 , pp. 85-90
    • Zsila, F.1
  • 10
    • 0001417865 scopus 로고    scopus 로고
    • Static and dynamic scattering of β-lactoglobulin aggregates formed after heat induced denaturation at pH 2
    • COI: 1:CAS:528:DyaK1MXhvFOlsbw%3D
    • Aymard P, Nicolai T, Durand D, Clark A. Static and dynamic scattering of β-lactoglobulin aggregates formed after heat induced denaturation at pH 2. Macromolecules 32: 2542–2552 (1999)
    • (1999) Macromolecules , vol.32 , pp. 2542-2552
    • Aymard, P.1    Nicolai, T.2    Durand, D.3    Clark, A.4
  • 11
    • 0008452276 scopus 로고    scopus 로고
    • Heat-induced gelation of globular proteins: Part 3. Molecular studies on low pH β-lactoglobulin gels
    • COI: 1:CAS:528:DC%2BD3cXnt1Sjtbc%3D
    • Kavanagh GM, Clark AH, Ross-Murphy SB. Heat-induced gelation of globular proteins: Part 3. Molecular studies on low pH β-lactoglobulin gels. Int. J. Biol. Macromol. 28: 41–50 (2000)
    • (2000) Int. J. Biol. Macromol. , vol.28 , pp. 41-50
    • Kavanagh, G.M.1    Clark, A.H.2    Ross-Murphy, S.B.3
  • 12
    • 14844363573 scopus 로고    scopus 로고
    • Temperature dependence of the nucleation constant rate in β amyloid fibrillogenesis
    • COI: 1:CAS:528:DC%2BD2MXitlOhurk%3D
    • Sabate R, Gallardo M, Estelrich J. Temperature dependence of the nucleation constant rate in β amyloid fibrillogenesis. Int. J. Biol. Macromol. 35: 9–13 (2005)
    • (2005) Int. J. Biol. Macromol. , vol.35 , pp. 9-13
    • Sabate, R.1    Gallardo, M.2    Estelrich, J.3
  • 13
    • 12344272183 scopus 로고    scopus 로고
    • Aggregation across the length scales in β-lactoglobulin
    • COI: 1:CAS:528:DC%2BD2cXpvFWqsL4%3D
    • Bromley EH, Krebs MR, Donald AM. Aggregation across the length scales in β-lactoglobulin. Faraday Discuss. 128: 13–27 (2005)
    • (2005) Faraday Discuss. , vol.128 , pp. 13-27
    • Bromley, E.H.1    Krebs, M.R.2    Donald, A.M.3
  • 14
    • 0036784667 scopus 로고    scopus 로고
    • A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea
    • COI: 1:CAS:528:DC%2BD38XntlCrtrw%3D
    • Hamada D, Dobson CM. A kinetic study of β-lactoglobulin amyloid fibril formation promoted by urea. Protein Sci. 11: 2417–2426 (2002)
    • (2002) Protein Sci. , vol.11 , pp. 2417-2426
    • Hamada, D.1    Dobson, C.M.2
  • 15
    • 84881644282 scopus 로고    scopus 로고
    • β-Lactoglobulin self-assembly: Structural changes in early stages and disulfide bonding in fibrils
    • COI: 1:CAS:528:DC%2BC3sXhtVyrt7fO
    • Dave AC, Loveday SM, Anema SG, Loo TS, Norris GE, Jameson GB, Singh H. β-Lactoglobulin self-assembly: Structural changes in early stages and disulfide bonding in fibrils. J. Agr. Food Chem. 61: 7817–7828 (2013)
    • (2013) J. Agr. Food Chem. , vol.61 , pp. 7817-7828
    • Dave, A.C.1    Loveday, S.M.2    Anema, S.G.3    Loo, T.S.4    Norris, G.E.5    Jameson, G.B.6    Singh, H.7
  • 16
    • 0033977086 scopus 로고    scopus 로고
    • Amyloid fibrillogenesis: Theme and variations
    • COI: 1:CAS:528:DC%2BD3cXhs1Sltrc%3D
    • Rochet JC, Lansbury PT Jr. Amyloid fibrillogenesis: Theme and variations. Curr. Opin. Struc. Biol. 10: 60–68 (2000)
    • (2000) Curr. Opin. Struc. Biol. , vol.10 , pp. 60-68
    • Rochet, J.C.1    Lansbury, P.J.2
  • 17
    • 34047234694 scopus 로고    scopus 로고
    • Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing
    • COI: 1:CAS:528:DC%2BD28XhtlWmu7zK
    • Pearce FG, Mackintosh SH, Gerrard JA. Formation of amyloid-like fibrils by ovalbumin and related proteins under conditions relevant to food processing. J. Agr. Food Chem. 55: 318–322 (2007)
    • (2007) J. Agr. Food Chem. , vol.55 , pp. 318-322
    • Pearce, F.G.1    Mackintosh, S.H.2    Gerrard, J.A.3
  • 19
    • 71749112862 scopus 로고    scopus 로고
    • Shearinduced structure and mechanics of β-lactoglobulin amyloid fibrils
    • COI: 1:CAS:528:DC%2BD1MXhsVyqsrzL
    • Dunstan DE, Hamilton-Brown P, Asimakis P, Ducker W, Bertolini J. Shearinduced structure and mechanics of β-lactoglobulin amyloid fibrils. Soft Matter 5: 5020–5028 (2009)
    • (2009) Soft Matter , vol.5 , pp. 5020-5028
    • Dunstan, D.E.1    Hamilton-Brown, P.2    Asimakis, P.3    Ducker, W.4    Bertolini, J.5
  • 20
    • 84892619828 scopus 로고    scopus 로고
    • Modulating β-lactoglobulin nanofibril self-assembly at pH 2 using glycerol and sorbitol
    • COI: 1:CAS:528:DC%2BC3sXhvFaltLbJ
    • Dave AC, Loveday SM, Anema SG, Jameson GB, Singh H. Modulating β-lactoglobulin nanofibril self-assembly at pH 2 using glycerol and sorbitol. Biomacromolecules 15: 95–103 (2014)
    • (2014) Biomacromolecules , vol.15 , pp. 95-103
    • Dave, A.C.1    Loveday, S.M.2    Anema, S.G.3    Jameson, G.B.4    Singh, H.5
  • 22
    • 80054996044 scopus 로고    scopus 로고
    • β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions
    • COI: 1:CAS:528:DC%2BC3MXhtlGiu7%2FF
    • Loveday SM, Wang XL, Rao MA, Anema SG, Singh H. β-Lactoglobulin nanofibrils: Effect of temperature on fibril formation kinetics, fibril morphology and the rheological properties of fibril dispersions. Food Hydrocolloid. 27: 242–249 (2012)
    • (2012) Food Hydrocolloid. , vol.27 , pp. 242-249
    • Loveday, S.M.1    Wang, X.L.2    Rao, M.A.3    Anema, S.G.4    Singh, H.5
  • 23
    • 84901627062 scopus 로고    scopus 로고
    • Amyloid fibril formation by β-lactoglobulin is inhibited by gold nanoparticles
    • COI: 1:CAS:528:DC%2BC2cXhtFyjsr7O
    • Sardar S, Pal S, Maity S, Chakraborty J, Halder UC. Amyloid fibril formation by β-lactoglobulin is inhibited by gold nanoparticles. Int. J. Biol. Macromol. 69: 137–145 (2014)
    • (2014) Int. J. Biol. Macromol. , vol.69 , pp. 137-145
    • Sardar, S.1    Pal, S.2    Maity, S.3    Chakraborty, J.4    Halder, U.C.5
  • 24
    • 84893736228 scopus 로고    scopus 로고
    • The characteristics of heat-induced aggregates formed by mixtures of β-lactoglobulin and β-casein
    • COI: 1:CAS:528:DC%2BC2cXmsVKksbo%3D
    • Kehoe JJ, Foegeding EA. The characteristics of heat-induced aggregates formed by mixtures of β-lactoglobulin and β-casein. Food Hydrocolloid. 39: 264–271 (2014)
    • (2014) Food Hydrocolloid. , vol.39 , pp. 264-271
    • Kehoe, J.J.1    Foegeding, E.A.2
  • 25
    • 11144222595 scopus 로고    scopus 로고
    • The binding of thioflavin-T to amyloid fibrils: Localization and implications
    • COI: 1:CAS:528:DC%2BD2MXjvFGj
    • Krebs MRH, Bromley EHC, Donald AM. The binding of thioflavin-T to amyloid fibrils: Localization and implications. J. Struct. Biol. 149: 30–37 (2005)
    • (2005) J. Struct. Biol. , vol.149 , pp. 30-37
    • Krebs, M.R.H.1    Bromley, E.H.C.2    Donald, A.M.3
  • 26
    • 67249141423 scopus 로고    scopus 로고
    • The critical aggregation concentration of β-lactoglobulin-based fibril formation
    • Kroes-Nijboer A, Venema P, Bouman J. The critical aggregation concentration of β-lactoglobulin-based fibril formation. Food Biophys. 4: 59–63 (2009)
    • (2009) Food Biophys. , vol.4 , pp. 59-63
    • Kroes-Nijboer, A.1    Venema, P.2    Bouman, J.3
  • 27
    • 34447640541 scopus 로고    scopus 로고
    • Effect of stirring and seeding on whey protein fibril formation
    • COI: 1:CAS:528:DC%2BD2sXmsFWisrY%3D
    • Bolder SG, Sagis LM, Venema P, van der Linden E. Effect of stirring and seeding on whey protein fibril formation. J. Agr. Food Chem. 55: 5661–5669 (2007)
    • (2007) J. Agr. Food Chem. , vol.55 , pp. 5661-5669
    • Bolder, S.G.1    Sagis, L.M.2    Venema, P.3    van der Linden, E.4
  • 28
    • 58849138718 scopus 로고    scopus 로고
    • Thioflavin T fluorescence assay for β-lactoglobulin fibrils hindered by DAPH
    • COI: 1:CAS:528:DC%2BD1MXhtlGlsb0%3D
    • Kroes-Nijboer A, Lubbersen YS, Venema P, van der Linden E. Thioflavin T fluorescence assay for β-lactoglobulin fibrils hindered by DAPH. J. Struct. Biol. 165: 140–145 (2009)
    • (2009) J. Struct. Biol. , vol.165 , pp. 140-145
    • Kroes-Nijboer, A.1    Lubbersen, Y.S.2    Venema, P.3    van der Linden, E.4
  • 29
    • 77949805635 scopus 로고    scopus 로고
    • Characterization of β-lactoglobulin fibrillar assembly using atomic force microscopy, polyacrylamide gel electrophoresis, and in situ fourier transform infrared spectroscopy
    • COI: 1:CAS:528:DC%2BC3cXisVCgsrs%3D
    • Oboroceanu D, Wang L, Brodkorb A, Magner E, Auty MA. Characterization of β-lactoglobulin fibrillar assembly using atomic force microscopy, polyacrylamide gel electrophoresis, and in situ fourier transform infrared spectroscopy. J. Agr. Food Chem. 58: 3667–3673 (2010)
    • (2010) J. Agr. Food Chem. , vol.58 , pp. 3667-3673
    • Oboroceanu, D.1    Wang, L.2    Brodkorb, A.3    Magner, E.4    Auty, M.A.5
  • 30
    • 84923833663 scopus 로고
    • Thermal aggregation of β-lactoglobulin: Effect of pH, ionic environment and thiol reagent
    • COI: 1:CAS:528:DyaK3sXhs1OkurY%3D
    • Xiong YL, Dawson KA, Wan L. Thermal aggregation of β-lactoglobulin: Effect of pH, ionic environment and thiol reagent. J. Dairy Sci. 76: 70–77 (1993)
    • (1993) J. Dairy Sci. , vol.76 , pp. 70-77
    • Xiong, Y.L.1    Dawson, K.A.2    Wan, L.3
  • 31
    • 33751421851 scopus 로고    scopus 로고
    • Electrostatically driven protein aggregation: β-Lactoglobulin at low ionic strength
    • COI: 1:CAS:528:DC%2BD28Xpslejurg%3D
    • Majhi PR, Ganta RR, Vanam RP, Seyrek E, Giger K, Dubin PL. Electrostatically driven protein aggregation: β-Lactoglobulin at low ionic strength. Langmuir 22: 9150–9159 (2006)
    • (2006) Langmuir , vol.22 , pp. 9150-9159
    • Majhi, P.R.1    Ganta, R.R.2    Vanam, R.P.3    Seyrek, E.4    Giger, K.5    Dubin, P.L.6
  • 32
    • 48849103441 scopus 로고    scopus 로고
    • Properties of protein fibrils in whey protein isolate solutions: Microstructure, flow behaviour and gelation
    • COI: 1:CAS:528:DC%2BD1cXhtVSjsrnN
    • Akkermans C, van der Goot AJ, Venema P, van der Linden E, Boom RM. Properties of protein fibrils in whey protein isolate solutions: Microstructure, flow behaviour and gelation. Int. Dairy J. 18: 1034–1042 (2008)
    • (2008) Int. Dairy J. , vol.18 , pp. 1034-1042
    • Akkermans, C.1    van der Goot, A.J.2    Venema, P.3    van der Linden, E.4    Boom, R.M.5
  • 33
    • 77955511339 scopus 로고    scopus 로고
    • Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages
    • COI: 1:CAS:528:DC%2BC3cXpsFKqsL0%3D
    • Ron N, Zimet P, Bargarum J, Livney YD. Beta-lactoglobulin-polysaccharide complexes as nanovehicles for hydrophobic nutraceuticals in non-fat foods and clear beverages. Int. Dairy J. 20: 686–693 (2010)
    • (2010) Int. Dairy J. , vol.20 , pp. 686-693
    • Ron, N.1    Zimet, P.2    Bargarum, J.3    Livney, Y.D.4
  • 34
    • 84884232301 scopus 로고    scopus 로고
    • pH effects on the intermolecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology
    • COI: 1:CAS:528:DC%2BC3sXht12htrbP
    • Engelhardt K, Lexis M, Gochev G, Konnerth C, Miller R, Willenbacher N, Peukert W, Braunschweig B. pH effects on the intermolecular structure of β-lactoglobulin modified air-water interfaces and its impact on foam rheology. Langmuir 29: 11646–11655 (2013)
    • (2013) Langmuir , vol.29 , pp. 11646-11655
    • Engelhardt, K.1    Lexis, M.2    Gochev, G.3    Konnerth, C.4    Miller, R.5    Willenbacher, N.6    Peukert, W.7    Braunschweig, B.8
  • 35
    • 84867525281 scopus 로고    scopus 로고
    • Simultaneous control of pH and ionic strength during interfacial rheology of β-lactoglobulin fibrils adsorbed at liquid/liquid interfaces
    • Rûhs PA, Scheuble N, Windhab EJ, Mezzenga R, Fischer P. Simultaneous control of pH and ionic strength during interfacial rheology of β-lactoglobulin fibrils adsorbed at liquid/liquid interfaces. Langmuir 28: 12536–12543 (2012)
    • (2012) Langmuir , vol.28 , pp. 12536-12543
    • Rûhs, P.A.1    Scheuble, N.2    Windhab, E.J.3    Mezzenga, R.4    Fischer, P.5
  • 36
    • 0006313731 scopus 로고
    • The rheology of pseudoplastic fluids in porous media using network modeling
    • COI: 1:CAS:528:DyaL1MXksl2jsLk%3D
    • Sorbie KS, Clifford PJ, Jones ERW. The rheology of pseudoplastic fluids in porous media using network modeling. J. Colloid Interf. Sci. 130: 508–534 (1989)
    • (1989) J. Colloid Interf. Sci. , vol.130 , pp. 508-534
    • Sorbie, K.S.1    Clifford, P.J.2    Jones, E.R.W.3
  • 37
    • 0036746821 scopus 로고    scopus 로고
    • Linear and nonlinear viscoelastic behavior of oil-in-water emulsions stabilized with polysaccharides
    • Quintana JM, Califano AN, Zaritzky NE, Partal, P, Franco JM. Linear and nonlinear viscoelastic behavior of oil-in-water emulsions stabilized with polysaccharides. J. Texture Stud. 33: 215–236 (2002)
    • (2002) J. Texture Stud. , vol.33 , pp. 215-236
    • Quintana, J.M.1    Califano, A.N.2    Zaritzky, N.E.3    Partal, P.4    Franco, J.M.5


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