메뉴 건너뛰기




Volumn 274, Issue , 2020, Pages

Kinetics of denaturation and aggregation of highly concentrated β-Lactoglobulin under defined thermomechanical treatment

Author keywords

Aggregation; Denaturation; Kinetics; Molecular motion; Thermomechanical treatment; Whey proteins

Indexed keywords

ACTIVATION ENERGY; AGGLOMERATION; COVALENT BONDS; DENATURATION; ENZYME KINETICS; KINETICS; REACTION RATES; SHEAR DEFORMATION; SULFUR COMPOUNDS;

EID: 85075627761     PISSN: 02608774     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jfoodeng.2019.109825     Document Type: Article
Times cited : (22)

References (53)
  • 1
    • 0033805350 scopus 로고    scopus 로고
    • Effect of milk concentration on the irreversible thermal denaturation and disulfide aggregation of β-lactoglobulin
    • Anema, S.G., Effect of milk concentration on the irreversible thermal denaturation and disulfide aggregation of β-lactoglobulin. J. Agric. Food Chem. 48:9 (2000), 4168–4175, 10.1021/jf991173e.
    • (2000) J. Agric. Food Chem. , vol.48 , Issue.9 , pp. 4168-4175
    • Anema, S.G.1
  • 2
    • 0001430290 scopus 로고    scopus 로고
    • Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk
    • Anema, S.G., McKenna, A.B., Reaction kinetics of thermal denaturation of whey proteins in heated reconstituted whole milk. J. Agric. Food Chem. 44:2 (1996), 422–428, 10.1021/jf950217q.
    • (1996) J. Agric. Food Chem. , vol.44 , Issue.2 , pp. 422-428
    • Anema, S.G.1    McKenna, A.B.2
  • 3
    • 0003393082 scopus 로고    scopus 로고
    • Lebensmittelchemie
    • Springer Berlin Heidelberg Berlin, Heidelberg
    • Belitz, H.-D., Grosch, W., Schieberle, P., Lebensmittelchemie. 2008, Springer Berlin Heidelberg, Berlin, Heidelberg.
    • (2008)
    • Belitz, H.-D.1    Grosch, W.2    Schieberle, P.3
  • 4
    • 5544264460 scopus 로고
    • Kinetics of capillary shear degradation in concentrated polymer solutions
    • Bestul, A.B., Kinetics of capillary shear degradation in concentrated polymer solutions. J. Chem. Phys. 24:6 (1956), 1196–1201, 10.1063/1.1742739.
    • (1956) J. Chem. Phys. , vol.24 , Issue.6 , pp. 1196-1201
    • Bestul, A.B.1
  • 5
    • 1542575976 scopus 로고    scopus 로고
    • Heat-induced denaturation/aggregation of β-lactoglobulin A and B: kinetics of the first intermediates formed
    • Croguennec, T., O'Kennedy, B.T., Mehra, R., Heat-induced denaturation/aggregation of β-lactoglobulin A and B: kinetics of the first intermediates formed. Int. Dairy J. 14:5 (2004), 399–409, 10.1016/j.idairyj.2003.09.005.
    • (2004) Int. Dairy J. , vol.14 , Issue.5 , pp. 399-409
    • Croguennec, T.1    O'Kennedy, B.T.2    Mehra, R.3
  • 6
    • 84987367516 scopus 로고
    • Reaction kinetics of the denaturation of whey proteins in milk
    • Dannenberg, F., Kessler, H.-G., Reaction kinetics of the denaturation of whey proteins in milk. J. Food Sci. 53:1 (1988), 258–263, 10.1111/j.1365-2621.1988.tb10223.x.
    • (1988) J. Food Sci. , vol.53 , Issue.1 , pp. 258-263
    • Dannenberg, F.1    Kessler, H.-G.2
  • 7
    • 84858990585 scopus 로고    scopus 로고
    • Functional properties of whey proteins microparticulated at low pH
    • Dissanayake, M., Liyanaarachchi, S., Vasiljevic, T., Functional properties of whey proteins microparticulated at low pH. J. Dairy Sci. 95:4 (2012), 1667–1679, 10.3168/jds.2011-4823.
    • (2012) J. Dairy Sci. , vol.95 , Issue.4 , pp. 1667-1679
    • Dissanayake, M.1    Liyanaarachchi, S.2    Vasiljevic, T.3
  • 8
    • 84876738736 scopus 로고    scopus 로고
    • Denaturation of whey proteins as a function of heat, pH and protein concentration
    • Dissanayake, M., Ramchandran, L., Donkor, O.N., Vasiljevic, T., Denaturation of whey proteins as a function of heat, pH and protein concentration. Int. Dairy J. 31:2 (2013), 93–99, 10.1016/j.idairyj.2013.02.002.
    • (2013) Int. Dairy J. , vol.31 , Issue.2 , pp. 93-99
    • Dissanayake, M.1    Ramchandran, L.2    Donkor, O.N.3    Vasiljevic, T.4
  • 9
    • 85029586853 scopus 로고    scopus 로고
    • Analysis of the reaction behavior of highly concentrated plant proteins in extrusion-like conditions
    • Emin, M.A., Quevedo, M., Wilhelm, M., Karbstein, H.P., Analysis of the reaction behavior of highly concentrated plant proteins in extrusion-like conditions. Innov. Food Sci. Emerg. Technol. 44 (2017), 15–20, 10.1016/j.ifset.2017.09.013.
    • (2017) Innov. Food Sci. Emerg. Technol. , vol.44 , pp. 15-20
    • Emin, M.A.1    Quevedo, M.2    Wilhelm, M.3    Karbstein, H.P.4
  • 10
    • 33846219578 scopus 로고    scopus 로고
    • Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry
    • Fitzsimons, S.M., Mulvihill, D.M., Morris, E.R., Denaturation and aggregation processes in thermal gelation of whey proteins resolved by differential scanning calorimetry. Food Hydrocolloids 21:4 (2007), 638–644, 10.1016/j.foodhyd.2006.07.007.
    • (2007) Food Hydrocolloids , vol.21 , Issue.4 , pp. 638-644
    • Fitzsimons, S.M.1    Mulvihill, D.M.2    Morris, E.R.3
  • 11
    • 0000706426 scopus 로고    scopus 로고
    • Heat-induced denaturation and aggregation of beta-Lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates
    • Galani, D., Apenten, R.K., Heat-induced denaturation and aggregation of beta-Lactoglobulin: kinetics of formation of hydrophobic and disulphide-linked aggregates. J. Appl. Crystallogr. 34:5–6 (1999), 467–476, 10.1046/j.1365-2621.1999.00314.x.
    • (1999) J. Appl. Crystallogr. , vol.34 , Issue.5-6 , pp. 467-476
    • Galani, D.1    Apenten, R.K.2
  • 12
    • 84988099677 scopus 로고
    • β-lactoglobulin denaturation and aggregation reactions and fouling deposit formation: a DSC study
    • Gotham, S.M., Fryer, P.J., Pritchard, A.M., β-lactoglobulin denaturation and aggregation reactions and fouling deposit formation: a DSC study. Int. J. Food Sci. Technol. 27:3 (1992), 313–327, 10.1111/j.1365-2621.1992.tb02033.x.
    • (1992) Int. J. Food Sci. Technol. , vol.27 , Issue.3 , pp. 313-327
    • Gotham, S.M.1    Fryer, P.J.2    Pritchard, A.M.3
  • 13
    • 85010244959 scopus 로고
    • Heat denaturation of β-lactoglobulins A and B
    • Gough, P., Jenness, R., Heat denaturation of β-lactoglobulins A and B. J. Dairy Sci. 45:9 (1962), 1033–1039, 10.3168/jds.S0022-0302(62)89556-3.
    • (1962) J. Dairy Sci. , vol.45 , Issue.9 , pp. 1033-1039
    • Gough, P.1    Jenness, R.2
  • 14
    • 0019039146 scopus 로고
    • Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5
    • Harwalkar, V.R., Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5. J. Dairy Sci. 63:7 (1980), 1052–1057, 10.3168/jds.S0022-0302(80)83046-3.
    • (1980) J. Dairy Sci. , vol.63 , Issue.7 , pp. 1052-1057
    • Harwalkar, V.R.1
  • 15
    • 0031935279 scopus 로고    scopus 로고
    • Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions
    • Havea, P., Singh, H., Creamer, L.K., Campanella, O.H., Electrophoretic characterization of the protein products formed during heat treatment of whey protein concentrate solutions. J. Dairy Res. 65:1 (1998), 79–91, 10.1017/S0022029997002641.
    • (1998) J. Dairy Res. , vol.65 , Issue.1 , pp. 79-91
    • Havea, P.1    Singh, H.2    Creamer, L.K.3    Campanella, O.H.4
  • 16
    • 0001266819 scopus 로고    scopus 로고
    • Molecular mass distributions of heat-induced β-lactoglobulin aggregates
    • Hoffmann, M.A.M., Sala, G., Olieman, C., Kruif, K.G. de, Molecular mass distributions of heat-induced β-lactoglobulin aggregates. J. Agric. Food Chem. 45:8 (1997), 2949–2957, 10.1021/jf9700788.
    • (1997) J. Agric. Food Chem. , vol.45 , Issue.8 , pp. 2949-2957
    • Hoffmann, M.A.M.1    Sala, G.2    Olieman, C.3    Kruif, K.G.D.4
  • 17
    • 0032843334 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin as a function of pH
    • Hoffmann, M.A.M., van Mil, P.J.J.M., Heat-induced aggregation of β-lactoglobulin as a function of pH. J. Agric. Food Chem. 47:5 (1999), 1898–1905, 10.1021/jf980886e.
    • (1999) J. Agric. Food Chem. , vol.47 , Issue.5 , pp. 1898-1905
    • Hoffmann, M.A.M.1    van Mil, P.J.J.M.2
  • 18
    • 0002284922 scopus 로고
    • Modifications of high-order structures upon heating of β-lactoglobulin: dependence on the protein concentration
    • Iametti, S., Cairoli, S., Gregori, B. de, Bonomi, F., Modifications of high-order structures upon heating of β-lactoglobulin: dependence on the protein concentration. J. Agric. Food Chem. 43:1 (1995), 53–58, 10.1021/jf00049a011.
    • (1995) J. Agric. Food Chem. , vol.43 , Issue.1 , pp. 53-58
    • Iametti, S.1    Cairoli, S.2    Gregori, B.D.3    Bonomi, F.4
  • 19
    • 0025851699 scopus 로고
    • Thermal denaturation of whey proteins and its effect in dairy technology
    • Kessler, H.-G., Beyer, H.-J., Thermal denaturation of whey proteins and its effect in dairy technology. Int. J. Biol. Macromol. 13:3 (1991), 165–173, 10.1016/0141-8130(91)90043-T.
    • (1991) Int. J. Biol. Macromol. , vol.13 , Issue.3 , pp. 165-173
    • Kessler, H.-G.1    Beyer, H.-J.2
  • 20
    • 85018490584 scopus 로고    scopus 로고
    • Reaction behaviour of highly concentrated whey protein isolate under defined heat treatments
    • Koch, L., Emin, M.A., Schuchmann, H.P., Reaction behaviour of highly concentrated whey protein isolate under defined heat treatments. Int. Dairy J. 71 (2017), 114–121, 10.1016/j.idairyj.2017.03.013.
    • (2017) Int. Dairy J. , vol.71 , pp. 114-121
    • Koch, L.1    Emin, M.A.2    Schuchmann, H.P.3
  • 21
    • 85019758698 scopus 로고    scopus 로고
    • Influence of defined shear rates on structural changes and functional properties of highly concentrated whey protein isolate-citrus pectin blends at elevated temperatures
    • Koch, L., Hummel, L., Schuchmann, H.P., Emin, M.A., Influence of defined shear rates on structural changes and functional properties of highly concentrated whey protein isolate-citrus pectin blends at elevated temperatures. Food Biophys. 12:3 (2017), 309–322, 10.1007/s11483-017-9487-2.
    • (2017) Food Biophys. , vol.12 , Issue.3 , pp. 309-322
    • Koch, L.1    Hummel, L.2    Schuchmann, H.P.3    Emin, M.A.4
  • 22
    • 85021144446 scopus 로고    scopus 로고
    • Structural changes and functional properties of highly concentrated whey protein isolate-citrus pectin blends after defined, high temperature treatments
    • Koch, L., Hummel, L., Schuchmann, H.P., Emin, M.A., Structural changes and functional properties of highly concentrated whey protein isolate-citrus pectin blends after defined, high temperature treatments. Lebensm. Wiss. Technol. 84 (2017), 634–642, 10.1016/j.lwt.2017.06.026.
    • (2017) Lebensm. Wiss. Technol. , vol.84 , pp. 634-642
    • Koch, L.1    Hummel, L.2    Schuchmann, H.P.3    Emin, M.A.4
  • 23
    • 34248331731 scopus 로고    scopus 로고
    • Collapse of the hydration shell of a protein prior to thermal unfolding
    • Koizumi, M., Hirai, H., Onai, T., Inoue, K., Hirai, M., Collapse of the hydration shell of a protein prior to thermal unfolding. J. Appl. Crystallogr. 40:s1 (2007), s175–s178, 10.1107/S0021889807003354.
    • (2007) J. Appl. Crystallogr. , vol.40 , Issue.s1 , pp. s175-s178
    • Koizumi, M.1    Hirai, H.2    Onai, T.3    Inoue, K.4    Hirai, M.5
  • 24
    • 0342374989 scopus 로고    scopus 로고
    • Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation
    • Le Bon, C., Nicolai, T., Durand, D., Kinetics of aggregation and gelation of globular proteins after heat-induced denaturation. Macromolecules 32:19 (1999), 6120–6127, 10.1021/ma9905775.
    • (1999) Macromolecules , vol.32 , Issue.19 , pp. 6120-6127
    • Le Bon, C.1    Nicolai, T.2    Durand, D.3
  • 25
    • 84944183900 scopus 로고    scopus 로고
    • β-Lactoglobulin heat denaturation: a critical assessment of kinetic modelling
    • Loveday, S.M., β-Lactoglobulin heat denaturation: a critical assessment of kinetic modelling. Int. Dairy J. 52 (2016), 92–100, 10.1016/j.idairyj.2015.08.001.
    • (2016) Int. Dairy J. , vol.52 , pp. 92-100
    • Loveday, S.M.1
  • 26
    • 84976048291 scopus 로고
    • The denaturation of α-lactalbumin and β-lactoglobulin in heated milk
    • Lyster, R.L.J., The denaturation of α-lactalbumin and β-lactoglobulin in heated milk. J. Dairy Res., 37(02), 1970, 233, 10.1017/S0022029900013297.
    • (1970) J. Dairy Res. , vol.37 , Issue.2 , pp. 233
    • Lyster, R.L.J.1
  • 27
    • 0000495653 scopus 로고
    • Whey protein denaturation in concentrated skimmilks
    • McKenna, B.M., O'Sullivan, A.C., Whey protein denaturation in concentrated skimmilks. J. Dairy Sci. 54:7 (1971), 1075–1077, 10.3168/jds.S0022-0302(71)85973-8.
    • (1971) J. Dairy Sci. , vol.54 , Issue.7 , pp. 1075-1077
    • McKenna, B.M.1    O'Sullivan, A.C.2
  • 28
    • 0014198603 scopus 로고
    • Effect of pH on β-Lactoglobulins
    • McKenzie, H.A., Sawyer, W.H., Effect of pH on β-Lactoglobulins. Nature 214:5093 (1967), 1101–1104, 10.1038/2141101a0.
    • (1967) Nature , vol.214 , Issue.5093 , pp. 1101-1104
    • McKenzie, H.A.1    Sawyer, W.H.2
  • 29
    • 0033969150 scopus 로고    scopus 로고
    • Implications of macromolecular crowding for protein assembly
    • Minton, A.P., Implications of macromolecular crowding for protein assembly. Curr. Opin. Struct. Biol. 10:1 (2000), 34–39, 10.1016/S0959-440X(99)00045-7.
    • (2000) Curr. Opin. Struct. Biol. , vol.10 , Issue.1 , pp. 34-39
    • Minton, A.P.1
  • 30
    • 79957700522 scopus 로고    scopus 로고
    • Kinetic study of β-lactoglobulin thermal aggregation at low pH
    • Mudgal, P., Daubert, C.R., Foegeding, E.A., Kinetic study of β-lactoglobulin thermal aggregation at low pH. J. Food Eng. 106:2 (2011), 159–165, 10.1016/j.jfoodeng.2011.04.025.
    • (2011) J. Food Eng. , vol.106 , Issue.2 , pp. 159-165
    • Mudgal, P.1    Daubert, C.R.2    Foegeding, E.A.3
  • 31
    • 84878585040 scopus 로고    scopus 로고
    • Controlled food protein aggregation for new functionality
    • Nicolai, T., Durand, D., Controlled food protein aggregation for new functionality. Curr. Opin. Colloid Interface Sci. 18:4 (2013), 249–256, 10.1016/j.cocis.2013.03.001.
    • (2013) Curr. Opin. Colloid Interface Sci. , vol.18 , Issue.4 , pp. 249-256
    • Nicolai, T.1    Durand, D.2
  • 32
    • 24944458015 scopus 로고    scopus 로고
    • Kinetics of heat-induced whey protein denaturation and aggregation in skim milks with adjusted whey protein concentration
    • Oldfield, D.J., Singh, H., Taylor, M.W., Kinetics of heat-induced whey protein denaturation and aggregation in skim milks with adjusted whey protein concentration. J. Dairy Res. 72:3 (2005), 369–378, 10.1017/S002202990500107X.
    • (2005) J. Dairy Res. , vol.72 , Issue.3 , pp. 369-378
    • Oldfield, D.J.1    Singh, H.2    Taylor, M.W.3
  • 33
    • 0032047305 scopus 로고    scopus 로고
    • Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-high temperature (UHT) pilot plant
    • Oldfield, D.J., Singh, H., Taylor, M.W., Pearce, K.N., Kinetics of denaturation and aggregation of whey proteins in skim milk heated in an ultra-high temperature (UHT) pilot plant. Int. Dairy J. 8:4 (1998), 311–318, 10.1016/S0958-6946(98)00089-2.
    • (1998) Int. Dairy J. , vol.8 , Issue.4 , pp. 311-318
    • Oldfield, D.J.1    Singh, H.2    Taylor, M.W.3    Pearce, K.N.4
  • 34
    • 0000760427 scopus 로고
    • Calorimetric study of thermal denaturation of β-lactoglobulin
    • Park, K.H., Lund, D.B., Calorimetric study of thermal denaturation of β-lactoglobulin. J. Dairy Sci. 67:8 (1984), 1699–1706, 10.3168/jds.S0022-0302(84)81495-2.
    • (1984) J. Dairy Sci. , vol.67 , Issue.8 , pp. 1699-1706
    • Park, K.H.1    Lund, D.B.2
  • 35
    • 82155179316 scopus 로고    scopus 로고
    • Influence of calcium on β-lactoglobulin denaturation kinetics: implications in unfolding and aggregation mechanisms
    • Petit, J., Herbig, A.-L., Moreau, A., Delaplace, G., Influence of calcium on β-lactoglobulin denaturation kinetics: implications in unfolding and aggregation mechanisms. J. Dairy Sci. 94:12 (2011), 5794–5810, 10.3168/jds.2011-4470.
    • (2011) J. Dairy Sci. , vol.94 , Issue.12 , pp. 5794-5810
    • Petit, J.1    Herbig, A.-L.2    Moreau, A.3    Delaplace, G.4
  • 36
    • 85061333078 scopus 로고    scopus 로고
    • High moisture extrusion of soy protein concentrate: influence of thermomechanical treatment on protein-protein interactions and rheological properties
    • Pietsch, V.L., Bühler, J.M., Karbstein, H.P., Emin, M.A., High moisture extrusion of soy protein concentrate: influence of thermomechanical treatment on protein-protein interactions and rheological properties. J. Food Eng. 251 (2019), 11–18, 10.1016/j.jfoodeng.2019.01.001.
    • (2019) J. Food Eng. , vol.251 , pp. 11-18
    • Pietsch, V.L.1    Bühler, J.M.2    Karbstein, H.P.3    Emin, M.A.4
  • 37
    • 85053059070 scopus 로고    scopus 로고
    • Kinetics of wheat gluten polymerization at extrusion-like conditions relevant for the production of meat analog products
    • Pietsch, V.L., Karbstein, H.P., Emin, M.A., Kinetics of wheat gluten polymerization at extrusion-like conditions relevant for the production of meat analog products. Food Hydrocolloids 85 (2018), 102–109, 10.1016/j.foodhyd.2018.07.008.
    • (2018) Food Hydrocolloids , vol.85 , pp. 102-109
    • Pietsch, V.L.1    Karbstein, H.P.2    Emin, M.A.3
  • 38
    • 85068395580 scopus 로고    scopus 로고
    • Investigation on the influence of high protein concentrations on the thermal reaction behaviour of β-lactoglobulin by experimental and numerical analyses
    • Quevedo, M., Jandt, U., Kulozik, U., Karbstein, H.P., Emin, M.A., Investigation on the influence of high protein concentrations on the thermal reaction behaviour of β-lactoglobulin by experimental and numerical analyses. Int. Dairy J. 97 (2019), 99–110, 10.1016/j.idairyj.2019.06.004.
    • (2019) Int. Dairy J. , vol.97 , pp. 99-110
    • Quevedo, M.1    Jandt, U.2    Kulozik, U.3    Karbstein, H.P.4    Emin, M.A.5
  • 40
    • 33749331938 scopus 로고    scopus 로고
    • The effect of temperature and shear rate upon the aggregation of whey protein and its implications for milk fouling
    • Simmons, M.J.H., Jayaraman, P., Fryer, P.J., The effect of temperature and shear rate upon the aggregation of whey protein and its implications for milk fouling. J. Food Eng. 79:2 (2007), 517–528, 10.1016/j.jfoodeng.2006.02.013.
    • (2007) J. Food Eng. , vol.79 , Issue.2 , pp. 517-528
    • Simmons, M.J.H.1    Jayaraman, P.2    Fryer, P.J.3
  • 41
    • 0000267310 scopus 로고
    • Study of a mathematical theory for the coagulation kinetics of colloidal solutions
    • Smoluchowski, M. von, Study of a mathematical theory for the coagulation kinetics of colloidal solutions. Z. Phys. Chem. 92:2 (1918), 129–168.
    • (1918) Z. Phys. Chem. , vol.92 , Issue.2 , pp. 129-168
    • Smoluchowski, M.V.1
  • 42
    • 0036077429 scopus 로고    scopus 로고
    • Whey protein aggregation under shear conditions - effects of pH-value and removal of calcium
    • Spiegel, T., Huss, M., Whey protein aggregation under shear conditions - effects of pH-value and removal of calcium. Int. J. Food Sci. Technol. 37:5 (2002), 559–568, 10.1046/j.1365-2621.2002.00612.x.
    • (2002) Int. J. Food Sci. Technol. , vol.37 , Issue.5 , pp. 559-568
    • Spiegel, T.1    Huss, M.2
  • 43
    • 84937796596 scopus 로고    scopus 로고
    • Effect of pH, transmembrane pressure and whey proteins on the properties of casein micelle deposit layers
    • Steinhauer, T., Lonfat, J., Hager, I., Gebhardt, R., Kulozik, U., Effect of pH, transmembrane pressure and whey proteins on the properties of casein micelle deposit layers. J. Membr. Sci. 493 (2015), 452–459, 10.1016/j.memsci.2015.06.007.
    • (2015) J. Membr. Sci. , vol.493 , pp. 452-459
    • Steinhauer, T.1    Lonfat, J.2    Hager, I.3    Gebhardt, R.4    Kulozik, U.5
  • 44
    • 0012197262 scopus 로고
    • Thermal aggregation of whey protein concentrates under fluid shear conditions
    • Steventon, A.J., Donald, A.M., Gladden, L.F., Thermal aggregation of whey protein concentrates under fluid shear conditions. Biochem. Milk Prod., 1994, 133–142, 10.1533/9780857093066.133.
    • (1994) Biochem. Milk Prod. , pp. 133-142
    • Steventon, A.J.1    Donald, A.M.2    Gladden, L.F.3
  • 45
    • 79951768234 scopus 로고    scopus 로고
    • Effects of shear on proteins in solution
    • Thomas, C.R., Geer, D., Effects of shear on proteins in solution. Biotechnol. Lett. 33:3 (2011), 443–456, 10.1007/s10529-010-0469-4.
    • (2011) Biotechnol. Lett. , vol.33 , Issue.3 , pp. 443-456
    • Thomas, C.R.1    Geer, D.2
  • 46
    • 22244485011 scopus 로고    scopus 로고
    • Effect of pH and T on the reaction kinetic parameters of the thermal denaturation of β-lg
    • Tolkach, A., Kulozik, U., Effect of pH and T on the reaction kinetic parameters of the thermal denaturation of β-lg. Milchwissenschaft, 2005, 249–252.
    • (2005) Milchwissenschaft , pp. 249-252
    • Tolkach, A.1    Kulozik, U.2
  • 47
    • 41949117726 scopus 로고    scopus 로고
    • Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin
    • Tolkach, A., Kulozik, U., Reaction kinetic pathway of reversible and irreversible thermal denaturation of β-lactoglobulin. Lait 87:4–5 (2007), 301–315, 10.1051/lait:2007012.
    • (2007) Lait , vol.87 , Issue.4-5 , pp. 301-315
    • Tolkach, A.1    Kulozik, U.2
  • 48
    • 84874513386 scopus 로고    scopus 로고
    • Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale
    • Toro-Sierra, J., Tolkach, A., Kulozik, U., Fractionation of α-lactalbumin and β-lactoglobulin from whey protein isolate using selective thermal aggregation, an optimized membrane separation procedure and resolubilization techniques at pilot plant scale. Food Bioprocess Technol. 6:4 (2013), 1032–1043, 10.1007/s11947-011-0732-2.
    • (2013) Food Bioprocess Technol. , vol.6 , Issue.4 , pp. 1032-1043
    • Toro-Sierra, J.1    Tolkach, A.2    Kulozik, U.3
  • 49
    • 0000295322 scopus 로고    scopus 로고
    • Kinetics of heat-induced aggregation of β-lactoglobulin
    • Verheul, M., Roefs, S.P.F.M., Kruif, K.G. de, Kinetics of heat-induced aggregation of β-lactoglobulin. J. Agric. Food Chem. 46:3 (1998), 896–903, 10.1021/jf970751t.
    • (1998) J. Agric. Food Chem. , vol.46 , Issue.3 , pp. 896-903
    • Verheul, M.1    Roefs, S.P.F.M.2    Kruif, K.G.D.3
  • 50
    • 0000868933 scopus 로고    scopus 로고
    • Effects of agitation on proteins
    • E. Dickinson R. Miller Royal Society of Chemistry Cambridge
    • Walstra, P., Effects of agitation on proteins. Dickinson, E., Miller, R., (eds.) Food Colloids: Fundamentals of Formulation, 2001, Royal Society of Chemistry, Cambridge, 245–254.
    • (2001) Food Colloids: Fundamentals of Formulation , pp. 245-254
    • Walstra, P.1
  • 51
    • 84930960359 scopus 로고    scopus 로고
    • Thermal denaturation kinetics of whey proteins at high protein concentrations
    • Wolz, M., Kulozik, U., Thermal denaturation kinetics of whey proteins at high protein concentrations. Int. Dairy J. 49 (2015), 95–101, 10.1016/j.idairyj.2015.05.008.
    • (2015) Int. Dairy J. , vol.49 , pp. 95-101
    • Wolz, M.1    Kulozik, U.2
  • 52
    • 84954131061 scopus 로고    scopus 로고
    • Thermal aggregation of whey proteins under shear stress
    • Wolz, M., Mersch, E., Kulozik, U., Thermal aggregation of whey proteins under shear stress. Food Hydrocolloids 56 (2016), 396–404, 10.1016/j.foodhyd.2015.12.036.
    • (2016) Food Hydrocolloids , vol.56 , pp. 396-404
    • Wolz, M.1    Mersch, E.2    Kulozik, U.3
  • 53
    • 80053053352 scopus 로고    scopus 로고
    • Mechanochemistry in thermomechanical processing of foods: kinetic aspects
    • Zhao, X., Wei, Y., Wang, Z., Zhang, B., Chen, F., Zhang, P., Mechanochemistry in thermomechanical processing of foods: kinetic aspects. J. Food Sci. 76:7 (2011), R134–R142, 10.1111/j.1750-3841.2011.02301.x.
    • (2011) J. Food Sci. , vol.76 , Issue.7 , pp. R134-R142
    • Zhao, X.1    Wei, Y.2    Wang, Z.3    Zhang, B.4    Chen, F.5    Zhang, P.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.