메뉴 건너뛰기




Volumn 120, Issue 1, 2014, Pages 57-68

Formation of β-lactoglobulin aggregates during thermomechanical treatments under controlled shear and temperature conditions

Author keywords

FBRM; Shear; Targeted structure; Whey protein aggregate

Indexed keywords

FBRM; FOCUSED BEAM REFLECTANCE MEASUREMENT; LABORATORY-SCALE DEVICES; PROTEIN CONCENTRATIONS; QUANTITATIVE CHARACTERIZATION; STATIC HEAT TREATMENT; TEMPERATURE CONDITIONS; WHEY PROTEINS;

EID: 84882304539     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2013.07.003     Document Type: Article
Times cited : (25)

References (37)
  • 2
    • 0001430290 scopus 로고    scopus 로고
    • Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk
    • S.G. Anema, and A.B. McKenna Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk Journal of Agricultural and Food Chemistry 44 1996 422 428 (Pubitemid 126469444)
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , Issue.2 , pp. 422-428
    • Anema, S.G.1    McKenna, A.B.2
  • 3
    • 0030272655 scopus 로고    scopus 로고
    • The effect of temperature and ionic strength on the dimerisation of β-lactoglobulin
    • DOI 10.1016/0141-8130(96)01130-0
    • P. Aymard, D. Durand, and T. Nicolai The effect of temperature and ionic strength on the dimerisation of beta-lactoglobulin International Journal of Biological Macromolecules 19 1996 213 221 (Pubitemid 26354240)
    • (1996) International Journal of Biological Macromolecules , vol.19 , Issue.3 , pp. 213-221
    • Aymard, P.1    Durand, D.2    Nicolai, T.3
  • 4
    • 0032697836 scopus 로고    scopus 로고
    • Thermal aggregation of whey proteins in model solutions as affected by casein/whey protein ratios
    • M. Beaulieu, Y. Pouliot, and M. Pouliot Thermal aggregation of whey proteins in model solutions as affected by casein/whey protein ratios Journal of Food Science 64 5 1999 776 780 (Pubitemid 29536839)
    • (1999) Journal of Food Science , vol.64 , Issue.5 , pp. 776-780
    • Beaulieu, M.1    Pouliot, Y.2    Pouliot, M.3
  • 6
    • 84987367516 scopus 로고
    • Reaction kinetics of the denaturation of whey proteins in milk
    • F. Dannenberg, and H. Kessler Reaction kinetics of the denaturation of whey proteins in milk Journal of Food Science 53 1988 258 263
    • (1988) Journal of Food Science , vol.53 , pp. 258-263
    • Dannenberg, F.1    Kessler, H.2
  • 7
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • M. Dissanayake, and T. Vasiljevic Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing Journal of Dairy Science 92 2009 1387 1397
    • (2009) Journal of Dairy Science , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 8
    • 60349109570 scopus 로고    scopus 로고
    • Mechanism of formation of stable heat induced beta-lactoglobulin microgels
    • L. Donato, C. Schmitt, L. Bovetto, and M. Rouvet Mechanism of formation of stable heat induced beta-lactoglobulin microgels International Dairy Journal 19 2009 295 306
    • (2009) International Dairy Journal , vol.19 , pp. 295-306
    • Donato, L.1    Schmitt, C.2    Bovetto, L.3    Rouvet, M.4
  • 10
    • 59549099513 scopus 로고    scopus 로고
    • The effect of shear rate on the molecular mass distributionof heat-induced aggregates of mixtures containing whey proteins and κ-carrageenan
    • S. Gaaloul, M. Corredig, and S.L. Turgeon The effect of shear rate on the molecular mass distributionof heat-induced aggregates of mixtures containing whey proteins and κ-carrageenan Food Biophysics 4 2009 13 22
    • (2009) Food Biophysics , vol.4 , pp. 13-22
    • Gaaloul, S.1    Corredig, M.2    Turgeon, S.L.3
  • 11
    • 75149130837 scopus 로고    scopus 로고
    • Preparation of nanoparticles from denatured whey protein by pH-cycling treatment
    • H.J. Giroux, J. Houde, and M. Britten Preparation of nanoparticles from denatured whey protein by pH-cycling treatment Food Hydrocolloids 24 2010 341 346
    • (2010) Food Hydrocolloids , vol.24 , pp. 341-346
    • Giroux, H.J.1    Houde, J.2    Britten, M.3
  • 12
    • 0034871473 scopus 로고    scopus 로고
    • Incorporation of whey proteins in cheese
    • DOI 10.1016/S0958-6946(01)00071-1, PII S0958694601000711
    • J. Hinrichs Incorporation of whey proteins in cheese International Dairy Journal 11 2001 495 503 (Pubitemid 32752189)
    • (2001) International Dairy Journal , vol.11 , Issue.4-7 , pp. 495-503
    • Hinrichs, J.1
  • 13
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • J.M. Jung, G. Savin, M. Pouzot, C. Schmitt, and R. Mezzenga Structure of heat-induced beta-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate Biomacromolecules 9 9 2008 2477 2486
    • (2008) Biomacromolecules , vol.9 , Issue.9 , pp. 2477-2486
    • Jung, J.M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 14
    • 10644282943 scopus 로고    scopus 로고
    • Use of focused beam reflectance measurement (FBRM) and process video imaging (PVI) in a modified mixed suspension mixed product removal (MSMPR) cooling crystallizer
    • E. Kougoulos, A.G. Jones, K.H. Jennings, and M.W. Wood-Kaczmar Use of focused beam reflectance measurement (FBRM) and process video imaging (PVI) in a modified mixed suspension mixed product removal (MSMPR) cooling crystallizer Journal of Crystal Growth 273 2005 529 534
    • (2005) Journal of Crystal Growth , vol.273 , pp. 529-534
    • Kougoulos, E.1    Jones, A.G.2    Jennings, K.H.3    Wood-Kaczmar, M.W.4
  • 15
    • 0033447189 scopus 로고    scopus 로고
    • Whey protein aggregates and their interaction with exo-polysaccharides
    • K.G. Kruif de, and R. Tuinier Whey protein aggregates and their interaction with exo-polysaccharides International Journal of Food Science and Technology 34 5-6 1999 487 492 (Pubitemid 129513182)
    • (1999) International Journal of Food Science and Technology , vol.34 , Issue.5-6 , pp. 487-492
    • De Kruif, K.G.1    Tuinier, R.2
  • 16
    • 33846853968 scopus 로고    scopus 로고
    • Rheological characterisation of starch based food products under unsteady temperature conditions and high heating rate
    • DOI 10.1016/j.jfoodeng.2006.01.072, PII S0260877406001592
    • S. Lagarrigue, L.G. Alvarez, and D. Flick Rheological characterisation of starch based food products under unsteady temperature conditions and high heating rate Journal of Food Engineering 81 2 2007 273 281 (Pubitemid 46227637)
    • (2007) Journal of Food Engineering , vol.81 , Issue.2 , pp. 273-281
    • Lagarrigue, S.1    Alvarez, G.2    Flick, D.3
  • 17
    • 34247639374 scopus 로고    scopus 로고
    • Light-scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and β-lactoglobulin at neutral pH
    • DOI 10.1021/jf063029g
    • N. Mahmoudi, S. Mehalebi, T. Nicolai, D. Durand, and A. Riaublanc Light scattering study of the structure of aggregates and gels formed by heat-denatured whey protein isolate and b-lactoglobulin at neutral pH Journal of Agricultural and Food Chemistry 55 2007 3104 3111 (Pubitemid 46668324)
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.8 , pp. 3104-3111
    • Mahmoudi, N.1    Mehalebi, S.2    Nicolai, T.3    Durand, D.4    Riaublanc, A.5
  • 19
    • 70350138530 scopus 로고    scopus 로고
    • Stability of β-lactoglobulin/micellar casein mixtures on heating in simulated milk ultrafiltrate at pH 6.0
    • J.S. Mounsey, and B.T. O'kennedy Stability of β-lactoglobulin/ micellar casein mixtures on heating in simulated milk ultrafiltrate at pH 6.0 International Journal of Dairy Technology 62 2009 493 499
    • (2009) International Journal of Dairy Technology , vol.62 , pp. 493-499
    • Mounsey, J.S.1    O'Kennedy, B.T.2
  • 20
    • 67349185830 scopus 로고    scopus 로고
    • Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of β-lactoglobulin
    • G. Muhammad, T. Croguennec, J. Jardin, M. Piot, and S. Bouhallab Copper modulates the heat-induced sulfhydryl/disulfide interchange reactions of β-lactoglobulin Food Chemistry 116 4 2009 884 891
    • (2009) Food Chemistry , vol.116 , Issue.4 , pp. 884-891
    • Muhammad, G.1    Croguennec, T.2    Jardin, J.3    Piot, M.4    Bouhallab, S.5
  • 21
    • 79961023076 scopus 로고    scopus 로고
    • β-Lactoglobulin and WPI aggregates: Formation, structure and applications
    • T. Nicolai, M. Britten, and C. Schmitt β-Lactoglobulin and WPI aggregates: formation, structure and applications Food Hydrocolloids 25 2011 1945 1962
    • (2011) Food Hydrocolloids , vol.25 , pp. 1945-1962
    • Nicolai, T.1    Britten, M.2    Schmitt, C.3
  • 22
  • 24
    • 57449085310 scopus 로고    scopus 로고
    • The dominating effect of ionic strength on the heat induced denaturation and aggregation of β-lactoglobulin in simulated milk ultrafiltrate
    • B.T. O'Kennedy, and J.S. Mounsey The dominating effect of ionic strength on the heat induced denaturation and aggregation of β-lactoglobulin in simulated milk ultrafiltrate International Dairy Journal 19 2009 123 128
    • (2009) International Dairy Journal , vol.19 , pp. 123-128
    • O'Kennedy, B.T.1    Mounsey, J.S.2
  • 25
    • 0742288323 scopus 로고    scopus 로고
    • Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
    • DOI 10.1016/j.foodres.2003.09.008
    • O.E. Perez, and A.M.R. Pilosof Pulsed electric effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white Food Research International 37 2004 102 110 (Pubitemid 38157678)
    • (2004) Food Research International , vol.37 , Issue.1 , pp. 102-110
    • Perez, O.E.1    Pilosof, A.M.R.2
  • 26
    • 82155179316 scopus 로고    scopus 로고
    • Influence of calcium on β-lactoglobulin denaturation kinetics: Implications in unfolding and aggregation mechanisms
    • J. Petit, A.-L. Herbig, A. Moreau, and G. Delaplace Influence of calcium on β-lactoglobulin denaturation kinetics: implications in unfolding and aggregation mechanisms Journal of Dairy Science 94 12 2011 5794 5810
    • (2011) Journal of Dairy Science , vol.94 , Issue.12 , pp. 5794-5810
    • Petit, J.1    Herbig, A.-L.2    Moreau, A.3    Delaplace, G.4
  • 28
    • 67651115509 scopus 로고    scopus 로고
    • Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions
    • C. Schmitt, C. Bovay, A.M. Vuilliomenet, M. Rouvet, L. Bovetto, R. Barbar, and C. Sanchez Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions Langmuir 2009
    • (2009) Langmuir
    • Schmitt, C.1    Bovay, C.2    Vuilliomenet, A.M.3    Rouvet, M.4    Bovetto, L.5    Barbar, R.6    Sanchez, C.7
  • 29
    • 33749331938 scopus 로고    scopus 로고
    • The effect of temperature and shear rate upon the aggregation of whey protein and its implications for milk fouling
    • DOI 10.1016/j.jfoodeng.2006.02.013, PII S0260877406001798
    • M.J.H. Simmons, P. Jayaraman, and P.J. Fryer The effect of temperature and shear rate upon the aggregation of whey protein and its implications for milk fouling Journal of Food Engineering 79 2007 517 528 (Pubitemid 44498921)
    • (2007) Journal of Food Engineering , vol.79 , Issue.2 , pp. 517-528
    • Simmons, M.J.H.1    Jayaraman, P.2    Fryer, P.J.3
  • 31
    • 44549084148 scopus 로고    scopus 로고
    • Whey and whey proteins-from "gutter-to-gold"
    • G.W. Smithers Whey and whey proteins-from "gutter-to-gold" International Dairy Journal 18 2008 695 704
    • (2008) International Dairy Journal , vol.18 , pp. 695-704
    • Smithers, G.W.1
  • 32
    • 0033410063 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions -effects of lactose and heating temperature on aggregate size and structure
    • T. Spiegel Whey protein aggregation under shear conditions - effects of lactose and heating temperature on aggregate size and structure International Journal of Food Science and Technology 34 1999 523 531 (Pubitemid 129513187)
    • (1999) International Journal of Food Science and Technology , vol.34 , Issue.5-6 , pp. 523-531
    • Spiegel, T.1
  • 33
    • 0036077429 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions - Effects of pH-value and removal of calcium
    • T. Spiegel, and M. Huss Whey protein aggregation under shear conditions - effects of pH-value and removal of calcium International Journal of Food Science and Technology 37 2002 559 568
    • (2002) International Journal of Food Science and Technology , vol.37 , pp. 559-568
    • Spiegel, T.1    Huss, M.2
  • 34
    • 84870648685 scopus 로고    scopus 로고
    • Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin
    • A. Tolkach, and U. Kulozik Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin Le Lait 87 2007 4 5
    • (2007) Le Lait , vol.87 , pp. 4-5
    • Tolkach, A.1    Kulozik, U.2
  • 35
    • 33746219698 scopus 로고    scopus 로고
    • Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0
    • DOI 10.1016/j.foodhyd.2005.10.017, PII S0268005X05002298
    • G. Unterhaslberger, C. Schmitt, C. Sanchez, C. Appolonia-Nouzille, and A. Raemya Heat denaturation and aggregation of β-lactoglobulin enriched WPI in the presence of arginine HCl, NaCl and guanidinium HCl at pH 4.0 and 7.0 Food Hydrocolloids 20 7 2006 1006 1019 (Pubitemid 44093777)
    • (2006) Food Hydrocolloids , vol.20 , Issue.7 , pp. 1006-1019
    • Unterhaslberger, G.1    Schmitt, C.2    Sanchez, C.3    Appolonia-Nouzille, C.4    Raemy, A.5
  • 36
    • 84923833663 scopus 로고
    • Thermal aggregation of β-lactoglobulin: Effect of pH, ionic environment, and thiol reagent
    • Y.L. Xiong, K.A. Dawson, and L. Wan Thermal aggregation of β-lactoglobulin: effect of pH, ionic environment, and thiol reagent Journal of Dairy Science 76 1 1993 70 77
    • (1993) Journal of Dairy Science , vol.76 , Issue.1 , pp. 70-77
    • Xiong, Y.L.1    Dawson, K.A.2    Wan, L.3
  • 37
    • 77956131588 scopus 로고    scopus 로고
    • Kinetics of formation and physicochemical characterization of thermally-induced β-lactoglobulin aggregates
    • R.N. Zúñiga, A. Tolkach, U. Kulozik, and J.M. Aguilera Kinetics of formation and physicochemical characterization of thermally-induced β-lactoglobulin aggregates Journal of Food Science 2010 75
    • (2010) Journal of Food Science , pp. 75
    • Zúñiga, R.N.1    Tolkach, A.2    Kulozik, U.3    Aguilera, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.