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Original Articles

Thermal unfolding of β‐lactoglobulin, α‐lactalbumin, and bovine serum albumin. A thermodynamic approach

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Pages 565-601 | Published online: 29 Sep 2009

References

  • McKenzie , H. A. 1967 . Milk proteins . Adv. Protein Chem. , 22 : 147
  • McKenzie , H. A. 1971 . “ β‐lactoglobulin ” . In Milk proteins: Chemistry and Molecular Biology , Edited by: Mckenzie , H. A. 257 New York : Academic Press .
  • Foster , J. F. 1977 . Albumin Structure Function and Uses , Edited by: Rosenoer , V. M. , Oratz , M. and Rothchild , M. A. 53 Oxford : Pergamon .
  • Gordon , W. G. 1971 . “ Alpha‐lactalbumin ” . In Milk Proteins , Edited by: McKenzie , H. A. Vol. II , 331 New York : Academic Press .
  • Lyster , R. L. J. 1972 . Reviews of the progress of dairy science, Section C, Chemistry of milk proteins . J. Dairy Res. , 39 : 279
  • Jenness , R. 1974 . “ The composition of milk ” . In Lactation: a comprehensive treatise , Edited by: Larson , B. L. and Smith , V. R. Vol. III , 3 New York : Academic Press .
  • Thomson , M. P. and Farrell , H. M. 1974 . “ Genetic variants of milk proteins ” . In Lactation: a Comprehensive Treatise , Edited by: Larson , B. L. and Smith , V. R. Vol. III , 109 New York : Academic Press .
  • Whitney , R. McL , Brunner , J. R. , Ebner , K. E. , Farell , H. M. , Josephson , R. V. , Morr , C. V. and Swaisgood , H. E. 1976 . Nomenclature of the proteins of cows milk . J. Dairy Sci. , 59 : 798
  • Swaisgood , H. E. 1982 . “ Chemistry of milk protein ” . In Developments in Dairy Chemistry Vol. 1, Proteins , Edited by: Fox , P. F. Vol. 1 , 1 New York : Applied Science .
  • Peters , T. Jr. 1985 . Serum albumin . Adv. Protein Chem. , 37 : 161
  • Morr , C. V. 1979 . Review: functionality of whey protein products . N. Z. J. Dairy Sci. Technol. , 14 : 185
  • de Wit , J. N. and Klarenbeek , G. 1984 . Effects of various treatments on structure and solubility of whey proteins . J. Dairy Sci. , 67 : 2701
  • Kinsella , J. E. 1984 . Milk proteins: physicochemical and functional properties . CRC Crit. Rev. Food Sci. Nutr. , 21 : 197
  • Mulvihill , D. M. and Donovan , M. 1987 . Whey proteins and their thermal denaturation‐ a review . Ir. J. Food Sci. Technol. , 11 : 43
  • Kinsella , J. E. and Whitehead , D. M. 1989 . Proteins in whey: chemical, physical, and functional properties . Adv. Food Nutr. Res. , 33 : 343
  • Mulvihill , D. M. and Fox , P. F. 1989 . “ Physico‐chemical and functional properties of milk proteins ” . In Developments in Dairy Chemistry , Edited by: Fox , P. F. Vol. 4 , 132 New York : Elsevier Applied Science .
  • Brew , K. and Gobler , J. A. 1992 . “ α‐lactalbumin ” . In Adv. Dairy Chem. Vol. 1, Proteins , Edited by: Fox , P. F. Vol. 1 , 191 New York : Elsevier Applied Science .
  • Walstra , P. and Jeness , R. , eds. 1984 . Dairy chemistry and physics , New York : J. Wiley & Sons .
  • de Wit , J. N. , Klarenbeek , G. and Hontelez‐Backx , E. 1977 . Evaluation of functional properties of whey protein concentrates and whey protein isolates. I. Isolation and characterization . Neth. Milk Dairy , 44 : 509
  • Maubois , J. L. , Pierre , A. , Fauquant , J. and Piot , M. 1987 . Industrial fractionation of main whey proteins . Int. Dairy Fed. , 212 : 145
  • Morr , C. V. 1987 . “ Fractionation and modification of whey protein in the U.S ” . In Trends in Whey Utilization , 145 Brussels, , Belgium : International Dairy Federation .
  • Pearce , R. J. 1987 . “ Fractionation of whey proteins ” . In Trends in Whey Utilization , 150 Brussels, , Belgium : International Dairy Federation .
  • de Wit , J. N. , Klarenbeek , G. and Adams , M. 1986 . Evaluation of functional properties of whey proteins isolates. II. Effects of processing history and composition . Neth. Milk Dairy , 7 : 40 41
  • Tissier , J. P. , Lalande , M. and Corrieu , G. 1984 . “ A study of milk deposit on heat exchange surfaces during UHT treatment ” . In Engineering and Food , Edited by: McKenna , B. M. 49 London : Applied Science Publishers .
  • Meireles , M. , Aimar , P. and Sanchez , V. 1991 . Albumin denaturation during ultrafiltration: effects of operating conditions and consequences on membrane fouling . Biotechnol. Bioeng. , 38 : 528
  • Kronman , M. J. 1989 . Metal‐ion binding and the molecular conformational properties of alpha‐lactalbumin . CRC Crit Rev. Biochem. Mol. Biol. , 24 : 565
  • Godozac‐Zimmerman , J. , Conti , A. and Napolitano , L. 1988 . The primary structure of donkey (Equus asinus) Iysozyme contains the Ca(II) binding site of alpha‐lactalbumin . Biol. Chem. Hoppe‐Seyler , 269 : 1109
  • Hambling , S. G. , McAlpine , A. S. and Sawyer , L. 1992 . “ β‐lactoglobulin ” . In Advances in Milk Chemistry Vol. I, Proteins Edited by: Fox , P. F. Vol. 1 , 141
  • Gumpen , S. , Hegg , P. O. and Martens , H. 1979 . Thermal stability of fatty acid‐serum albumin complexes studied by differential scanning calorimetry . Biochem. Biophys. Acta , 574 : 189
  • Min He , X. and Carter , C. 1992 . Atomic structure and chemistry of human serum albumin . Nature , 358 : 209
  • Kilara , A. and Sharkasi , T. 1986 . Effects of temperature on food proteins and its implications on functional properties . CRC Crit. Rev. Food Sci. Nutr. , 23 : 323
  • Kinsella , J. E. 1976 . Functional properties of food proteins: a survey . Crit. Rev. Food Sci. Nutr. , 4 : 219
  • Ferry , J. D. 1949 . Protein gels . Adv. Protein Chem. , 4 : 1
  • Hermansson , A. M. 1979 . “ Aggregation and denaturation involved in gel formation ” . In Functionality and Protein Structure , Edited by: Pour‐El , A. 81 Washington D. C. : American Chemical Society .
  • Graham , D. E. and Philips , M. C. 1976 . “ The conformation of proteins at air interface and their role in stabilizing foams ” . In Foams , Edited by: Aker , R. J. 237 New York : Academic Press .
  • Damodaran , K. B. and Damodaran , S. 1987 . Structure‐function relationship of proteins: adsorption of structural intermediates of bovine albumin at the air‐water interface . J. Agric. Food Chem. , 35 : 236
  • Kauzmann , W. 1959 . Some factors in the interpretation of protein denaturation . Adv. Protein Chem. , 14 : 1
  • Chotia , C. 1975 . Structural invariants in protein folding . Nature (London) , 254 : 304
  • Saito , N. 1989 . Principles of protein architecture . Adv. Biophys. , 25 : 95
  • Dill , K. A. 1990 . Dominant forces in protein folding . Biochemistry , 29 : 7133
  • Privalov , P. L. and Gill , S. J. 1988 . Stability of protein structure and hydrophobic interaction . Adv. Protein Chem. , 39 : 193
  • Creighton , T. E. 1984 . Pathway and mechanisms of protein folding . Adv. Biophys. , 18 : 1
  • Creighton , T. E. 1980 . Role of the environment in the refolding of reduced pancreatic trypsin inhibitor . J. Mol. Biol. , 144 : 521
  • Finkelstein , A. V. and Ptitsyn , O. B. 1987 . Why do globular proteins fit the limited set of folding patterns? . Prog. Biophys. Molec., Biol. , 50 : 171
  • Jaenicke , R. 1987 . Folding and association of proteins . Prog. Biophys. Mol. Biol. , 49 : 117
  • Von Hippel , P. M. and Schleich , T. 1969 . “ Structure and stability of biological macromolecules ” . Edited by: Timasheff , S. N. and Fasman , G. D. 417 New York : Marcel Dekker .
  • Damodaran , S. and Kinsella , J. E. 1982 . “ Effects of ions on protein conformation and functionality ” . In Food Protein Deterioration. Mechanisms and Functionality , ACS Symposium Series Edited by: Cherry , J. P. 327 Washington, DC : American Chemical Society .
  • Privalov , P. L. and Khechinashvili , N. N. 1974 . A thermodynamic approach to the problem of stabilization of globular proteins structure: a calorimetric study . J. Mol. Biol. , 86 : 665
  • Colvi , J. R. . Denaturation: a requiem . Symposium on Foods: Proteins and Their Reactions . Edited by: Schultz , H. W. and Anglemer , A. F. pp. 69 Westport, CT : AVI Publishing Co., Inc. .
  • Papiz , M. Z. , Sawyer , L. , Eliopoulos , E. E. , North , A. C. T. , Findlay , J. B. C. , Sivaprasadarao , R. , Jones , T. A. , Newcomer , M. E. and Kraulis , P. J. 1986 . The structure of β‐lactoglobulin and its similarity to plasma retinol‐binding protein . Nature (London) , 324 : 383
  • Tanford , C. , Bunville , L. G. and Nozaki , Y. 1952 . The reversible transformation of β‐lactoglobulin at pH 7.5 . J. Am. Chem. Soc. , 81 : 4032
  • Tanford , C. , De , P. K. and Taggart , V. G. 1960 . The role of α‐helix in the structure of proteins. Optical rotatory dispersion of β‐lactoglobulin . J. Am. Chem. Soc. , 82 : 6028
  • Timasheff , S. N. , Mescanti , L. , Bash , J. J. and Townend , R. 1966 . Conformational transitions of bovine β‐lactoglobulins A, B, and C . J. Biol. Chem. , 241 : 2496
  • Timasheff , S. N. , Townend , R. and Mescanti , L. 1966 . The optical rotatory dispersion of β‐lactoglobulin . J. Biol. Chem. , 241 : 1863
  • McKenzie , H. A. , Sawyer , W. H. and Smit , M. B. 1967 . Optical rotatory dispersion and sedimentation of association‐dissociation: bovine β‐lactoglobulin near pH 5 . Biochem. Biophys. Acta , 147 : 73
  • Sawyer , W. H. , Norton , R. S. , Nichol , L. W. and McKenzie , G. H. 1971 . Thermodenaturation of bovine β‐lactoglobulin. Kinetics and the introduction of β‐structure . Biochim. Biophys. Acta , 243 : 19
  • Townend , R. , Kumosinski , T. F. and Timasheff , S. N. 1967 . The circular dichroism of β‐lactoglobulin . J. Biol. Chem. , 242 : 4538
  • Lakkis , J. and Villota , R. 1992 . Effects of acylation on substructural properties of proteins: a study using fluorescence and circular dichroism . J. Agric. Food Chem. , 40 : 553
  • Timasheff , S. N. and Susi , H. 1966 . Infrared investigation of the secondary structure of β‐lactoglobulin . J. Biol. Chem. , 241 : 249
  • Byler , D. M. and Susi , H. 1986 . Examination of the secondary structure of proteins by deconvolution FTIR spectra . Biopolymers , 25 : 469
  • Casal , H. L. , Kohler , U. and Mantsch , H. H. 1988 . Structural and conformational changes of β‐lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature . Biochim. Biophys. Acta , 957 : 11
  • Monaco , H. L. , Zanotti , G. , Spadon , P. , Bolognesi , M. , Sawyer , L. and Eliopoulos , E. E. 1987 . Crystal structure of the trigonal form of bovine beta‐lactoglobulin and of its complex with retinol at 2.5 Å, resolution . J. Mol. Biol. , 197 : 695
  • Larson , B. L. and Jenness , R. 1952 . Characterization of the sulphydryl groups and the kinetics of the heat denaturation of crystalline β‐lactoglobulin . J. Amer. Chem. Soc. , 74 : 3090
  • Lyster , R. L. J. 1964 . The free and masked sulphydryl groups of heated milk and milk powder and a new method for their determination . J. Dairy Res. , 31 : 41
  • Sawyer , W. H. 1968 . Heat denaturation of bovine β‐lactoglobulin and relevance of disulphide aggregation . J. Dairy Sci. , 51 : 323
  • Watanabe , K. and Klostermeyer , H. 1976 . Heat‐induced changes in sulfhydryl and disulphyde levels of β‐lactoglobulin A and the formation of polymers . J. Dairy Res. , 43 : 411
  • Shimada , K. and Cheftel , J. C. 1989 . Sulfhydryl group/ disulfide bond interchange reactions during heat‐induced gelation of whey protein isolate . J. Agric. Food Chem. , 37 : 161
  • Creamer , L. K. , Parry , D. A. D. and Malcom , G. N. 1983 . Secondary structure of bovine β‐lactoglobulin B . Arch. Biochem. Biophys. , 227 : 98
  • Pessen , H. , Purcell , J. M. and Farrell , H. M. Jr. 1985 . Proton relaxation rates of water in dilute solutions of β‐lactoglobulin. Determination of cross relaxation and correlation with structural changes by the use of two genetic variants of a self‐associating globular protein . Biochim. Biophy. Acta , 828 : 1
  • Dufour , E. and Haertle , T. 1990 . Alcohol‐induced changes of‐β‐Iactoglobulin‐retinol‐binding stoichiometry . Protein Eng. , 4 : 185
  • Arakawa , T. and Timasheff , S. N. 1982 . Stabilization of protein structure by sugars . Biochemistry , 21 : 6536
  • Baumy , J. J. and Brule , G. 1988 . Binding of bivalent cations to α‐lactalbumin and β‐lactoglobulin: effect of pH and ionic strength . Le Lait , 68 : 33
  • Hiraoka , Y. , Segawa , T. , Kuwajima , K. , Sugai , S. and Murai , N. 1980 . Alpha‐lactalbumin: a calcium metallo‐protein . Biochem. Biophys. Res. Commun. , 95 : 1098
  • Kuroki , R. , Taniyama , Y. , Seko , C. , Nakamura , H. , Kikuchi , M. and Ikahara , M. 1989 . Design and creation of a Ca2+ binding site in human lysozyme to enhance structural stability . Proc. Natl. Sci., U.S.A. , 86 : 6903
  • Nitta , K. , Tsuge , H. , Shimazaki and Sugai , S. 1989 . Calcium‐binding lysozymes . Biol. Chem. Hoppe‐Seyler , 369 : 1109
  • Acharya , K. R. , Stuart , D. I. , Walker , N. P. C. , Lewis , H. and Philips , D. C. 1989 . Refined structure of baboon a‐lactalbumin at 1.7 Å resolution. Comparison with C‐type lysozyme . J. Mol. Biol. , 208 : 90
  • Kronman , M. J. , Andreotti , R. E. and Vitols , R. 1964 . Inter‐ intramolecular interactions of α‐lactalbumin. II. Aggregation reactions at acid pH . Biochimie , 3 : 1152
  • Dolgikh , D. A. , Gilmanshin , R. I. , Brazhnikov , E. V. , Bychkova , V. E. , Semisotnov , G. V. , Venyaminov , S. Yu and Ptitsyn , O. B. 1981 . α‐lactalbumin: compact state with fluctuating tertiary structure? . FEBS Lett. , 136 : 311
  • Dolgikh , D. L. A. , Abaturov , L. V. , Bolotina , I. A. , Brazhnikov , E. V. , Bychkova , V. E. , Gil , M. R. I. , Lebedev , Yu O. , Semisotnov , G. V. , Tiktopulo , E. I. and Ptitsyn , O. B. 1985 . Compact state of a protein molecule with pronounced small‐scale mobility: bovine alpha‐lactalbumin . Eur. Biophys. J. , 13 : 109
  • Izumi , Y. , Miyake , Y. , Kuwajimai , K. and Sugai , S. 1983 . Folding‐unfolding of α‐lactalbumin . Physica , 120B : 444
  • Gast , K. , Zirwer , D. , Welfe , H. , Bychkova , V. E. and Ptitsyn , O. B. 1986 . Quasielastic light scattering from human comparison of molecular dimensions in native and ‘molten globule’ states . Int. J. Biol. Macromol. , 8 : 231
  • Polis , B. D. , Schmuckler , H. W. and Custer , J. 1950 . Isolation of a crystalline albumin from milk . J. Biol. Chem. , 187 : 349
  • Georges , C. and Guinand , S. 1960 . Sur la dissociation reversible de la β‐lactoglobulin, a des pH supérieurs à 5.5. 1. Etude par la diffusion, de la lumiére . J. Chem. Phys. Physico‐Chim. Biol. , 57 : 606
  • Dupont , M. 1965 . Comparison de la thermodenaturation des β‐lactoglobulines A et B à pH 6.85 . Biochim. Biophys. Acta , 94 : 573
  • Dupont , M. and Yon , J. 1961 . Influence du chlorure de sodium sur la vitesse de thermodénaturation de la β‐lactoglobuline bovine a pH 6.9 . Chem. Phys. , 58 : 682
  • Pantaloni , D. 1964 . Etude du mécanisme d'agrégation thermique de la β‐lactoglobuline . C. R. Acad. Sci. , 259 : 1775
  • Sheraga , H. A. , Nemethy , G. and Steinberg , I. Z. 1962 . The contribution of hydrophobic bonds to the thermal stability of protein conformations . J. Biol. Chem. , 237 : 2506
  • Mills , O. E. 1976 . Effect of temperature on tryptophan fluorescence of β‐lactoglobulin B . Biochim. Biophys. Acta , 434 : 324
  • Mills , O. E. and Creamer , L. K. 1975 . A conformational change in bovine β‐lactoglobulin at low pH . Biochem. Biophys. Acta , 379 : 618
  • Permyakov , E. A. and Burstein , E. A. 1984 . Some aspects of studies of thermal transitions in proteins by means of their intrinsic fluorescence . Biophys. Chem. , 19 : 265
  • Bonomi , F. , Iametti , S. , Pagliari , E. and Peri , C. 1988 . A spectrofluorimetric approach to the estimation of the surface hydrophobicity modifications in milk proteins upon thermal treatment . Milchwissenschaft , 43 : 281
  • Semisotnov , G. V. , Rodionova , N. A. , Razgulyael , O. I. , Uverski , V. N. , Gripas , A. F. and Gilmanshin , R. I. 1991 . Study of the “molten globule”; intermediate state in protein folding by a hydrophobic fluorescence probe . Biopolymers , 31 : 119
  • Lapanje , S. and Poklar , N. 1989 . Calorimetric and circular dichroism studies of the thermal denaturation of β‐lactoglobulin . Biophys. Chem. , 34 : 155
  • Brandts , J. F. 1969 . “ Conformational transitions of proteins in water and in aqueous mixtures ” . In Structure and Stability of Biological Macromolecules , Edited by: Timasheff , S. N. and Fasman , G. D. 213 New York : Marcel Dekker Inc. .
  • Tanford , C. 1968 . Protein denaturation . Adv. Protein Chem. , 23 : 121
  • Privalov , P. L. 1980 . Scanning microcalorimetry for studying macromolecules . Pure Appl. Chem. , 52 : 479
  • Kuwajima , K. 1989 . The molten globule state as a clue for understanding the folding and cooperativity of globular‐protein structure . Proteins, Structure, Function and Genetics , 6 : 87
  • Privalov , P. L. and Potekhin , D. R. 1986 . Scanning calo‐rimetry in studying temperature induced changes in proteins . Methods Enzymol. , 131 : 4
  • Castronuovo , G. 1990 . Proteins in aqueous solution. Calorimetric studies and thermodynamic characterization . Thermochim. Acta , 193 : 363
  • Baldwin , R. L. 1986 . Temperature dependence of the hydrophobic interaction in protein folding . Proc. Natl. Acad. Sci. U.S.A. , 83 : 8069
  • Harwalkar , V. R. and Kalab , M. 1985 . Thermal denaturation and aggregation in solution. Electron microscopic study . Milchwisserschafft , 40 : 65
  • Relkin , P. and Launay , B. 1990 . Concentration effects on the kinetics of β‐lactoglobulin heat denaturation: a differential scanning calorimetric study . Food Hydro‐colloids , 4 : 19
  • Borchardt , H. J. and Daniels , S. F. 1957 . Application of differential thermal analysis to study of reaction kinetic . J. Am. Chem. Soc. , 79 : 41
  • Kissinger , H. E. 1957 . Reaction kinetics in differential thermal analysis . Anal. Chem. , 29 : 1702
  • Mraw , S. C. 1982 . Mathematic treatment of heat flow in differential scanning calorimetry and differential thermal analysis instruments . Rev. Sci. Instrum. , 53 : 228
  • Dumas , J. P. 1978 . The analysis of theoretical melting curves in differential scanning calorimetry . J. Phys. D: Appl. Phys. , 11 : 1
  • Relkin , P. 1994 . Differential scanning calorimetry: a useful tool for studying protein denaturation . Thermochim. Acta , 246 : 371
  • Heuvel , H. M. and Lind , K. C. J. B. 1970 . Computerized analysis and correction of differential scanning calorimetric data for effects due to thermal lag and heat capacity changes . Anal. Chem. , 42 : 1044
  • Sochava , I. V. , Belopolskaya , T. V. and Smirnova , O. I. 1985 . DSC study of reversible and irreversible thermal denaturation of concentrated globular protein solutions . Biophys. Chem. , 22 : 323
  • Hemminger , W. F. and Sarge , S. M. 1991 . The baseline construction and its influence on the measurements of heat with differential scanning calorimeters . J. Thermal Anal. , 37 : 1455
  • Relkin , P. and Launay , B. 1991 . On the partial reversibility of β‐lactoglobulin heat denaturation . J. Thermal Anal. , 37 : 1887
  • Harwalkar , V. R. 1980 . Measurement of thermal denaturation of β‐lactoglobulin at pH 2.5 . J. Dairy Sci. , 63 : 1043
  • Kella , N. K. D. and Kinsella , J. E. 1988 . Enhanced thermodynamic stability of β‐lactoglobulin at low pH . Biochem. J. , 255 : 113
  • Parris , N. , Purcell , J. M. and Ptashkin , S. M. 1991 . Thermal denaturation of whey proteins in skim milk . J. Agric. Food Chem. , 39 : 2167
  • Lambelet , P. , Berrocal , R. and Ducret , F. 1989 . Low‐resolution NMR spectroscopy: a tool to study protein denaturation. I. Application to diamagnetic whey proteins . J. Dairy Res. , 56 : 211
  • Dalgleish , D. G. 1990 . The effect of denaturation of β‐lactoglobulin on renneting — a quantitative study . Milchwiss. , 45 : 492
  • Ruegg , M. , Moor , M. and Blanc , B. 1977 . A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate . J. Dairy Res. , 44 : 509
  • Hegg , P.‐O. 1980 . Thermal stability of β‐lactoglobulin as function of pH and the relative concentration of sodium dodecyl sulfate . Acta Agric. Scand , 30 : 401
  • de Wit , J. N. and Swinkel , G. A. M. 1980 . A differential scanning calorimetric study of the thermal denaturation of bovine β‐lactoglobulin, thermal behavior at temperature up to 100°C . Biochim. Biophys. Acta , 624 : 40
  • de Wit , J. N. and Klarenbeek , G. 1981 . A differential scanning calorimetric study of the thermal behavior of bovine β‐lactoglobulin at temperature up to 160°C . J. Dairy Res. , 48 : 293
  • Pfeil , W. 1981 . Thermodynamic of α‐lactalbumin unfolding . Biophys. Chem. , 13 : 181
  • Bernal , V. and Jelen , P. 1985 . Thermal stability of whey proteins — a calorimetric study . J. Dairy Sci. , 68 : 2847
  • Paulsson , M. , Hegg , P.‐O. and Castberg , H. B. 1985 . Thermal stability of whey proteins studied by differential scanning calorimetry . Thermochim. Acta , 95 : 435
  • Schwarz , F. P. 1990 . Biological thermodynamic data for the calibration of differential scanning calorimeters: heat capacity data on the unfolding transition of β‐Iactoglobulin in solution . Thermochim. Acta , 159 : 305
  • Relkin , P. , Eynard , L. and Launay , B. 1992 . Thermodynamic parameters of β‐lactoglobulin and α‐lactalbumin. A DSC study of denaturation by heating . Thermochim. Acta , 204 : 111
  • Kaminogawa , S. , Shimizu , M. , Ametan , A. , Hattori , M. , Ando , O. , Hachimura , Y. , Totsuka , M. and Yamauchi , K. 1989 . Monoclonal antibodies as probes for monitoring the denaturation process of bovine β‐lactoglobulin . Biochem. Biophys. Acta , 998 : 50
  • Relkin , P. , Liu and Launay , B. 1993 . denaturation, gelification and emulsification properties of β‐lactoglobulin . J Dispersion Sci. Technol. , 14 : 335
  • Patocka , J. , Drathen , M. and Jelen , P. 1987 . Heat stability of isolated whey protein fractions in highly acidic conditions . Milchwissenschaft , 42 : 700
  • Griko , Y. V. and Privalov , P. L. 1992 . Calorimetric study of the heat and cold denaturation of β‐lactoglobulin . Biochemistry , 31 : 8810
  • Gough , P. and Jeness , R. 1962 . Heat denaturation of bovine β‐lactoglobulin A and B . J. Dairy Sci. , 45 : 1033
  • Imafidon , G. I. , Ng‐Kwai‐Hang , K. F. , Harwalkar , V. R. and Ma , C.‐Y. 1991 . Differential scanning calorimetric study of different genetic variants of β‐lactoglobulin . J. Dairy Sci. , 74 : 2416
  • Liu , T. 1993 . Etude des proprétés de dénaturation et de gélification thermiques de concentrés de la β‐lacto‐globuline. Influence des procédés de purification , ENSIA, University Paris‐Sud and University Paris VII . Doctoral thesis
  • Liu , T. , Relkin , P. and Launay , B. 1994 . Thermal denaturation and heat‐induced gelation of β‐lactoglobulin. Effects of some chemical parameters . Thermochim. Acta , 246 : 387
  • Xiao , L. Q. , Brownlow , S. , Holt , C. and Sellers , P. 1995 . Effect of concentration on the thermal denaturation of β‐lactoglobuline at pH 6.75 and pH 8.05 . Arch. Biochem. Biophys. ,
  • Paulsson , M. and Djemek , P. 1990 . Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry . J. Dairy Sci. , 73 : 590
  • Foegeding , E. A. , Kuhn , P. R. and Hardin , C. C. 1992 . Specific divalent cation‐induced changes during gelation of b‐lactoglobulin . J. Agric. Food Chem. , 40 : 2092
  • Varunsatian , S. , Watanabe , K. , Hayakawa , S. and Nakamura , R. 1983 . Effects of Ca++ Mg++ and Na++ on heat aggregation of whey protein concentrates . J. Food Sci. , 48 : 42
  • Mulvihill , D. M. , Rector , D. and Kinsella , J. E. 1990 . Effects of structuring and destructuring anionic ions on the rheological properties of thermally induced β‐lactoglobulin gels . Food Hydrocolloids , 4 : 267
  • Park , K. H. and Lund , D. B. 1984 . Calorimetric study of thermal denaturation of β‐lactoglobulin . J. Dairy Sci. , 67 : 1699
  • Watanabe , K. , Kyogoku , N. , Matsuda , T. and Nakamura , R. 1985 . Effects of FeCl3 on heat denaturation of β—lactoglobulin A in acid media . J. Agric. Food Chem. , 33 : 403
  • Morr , C. V. and Josephson , R. V. 1968 . Effects of calcium, N‐ethyl maleimide and casein upon whey protein aggregation . J. Dairy Sci. , 51 : 1349
  • Donovan , M. and Mulvihill , D. M. 1987 . Effects of chemical modification and sodium dodecyl sulphate binding on the thermostability of whey protein . Ir. J. Food Sci. Technol. , 11 : 77
  • Gotham , S. M. , Fryer , P. J. and Pritchard , A. M. 1992 . β‐lactoglobulin denaturation and aggregation reactions and fouling deposit formation: a DSC study . Int. J. Food Sci. Technol. , 27 : 313
  • O'Neil , T. E. and Kinsella , J. E. 1987 . Binding of alkanone flavors to β‐lactoglobulin: effects of conformational and chemical modification . J. Agric. Food Chem. , 35 : 770
  • Fugate , R. D. and Song , P. S. 1980 . Spectroscopy characterization of β‐lactoglobulin‐retinol complex . Biochim. Biophys. Acta , 625 : 28
  • Sawyer , W.H. 1969 . Complex between β‐lactoglobulin and κ‐casein . J. Dairy Sci. , 52 : 1347
  • Jang , D. H. and Swaisgood , H. E. 1990 . Disulfide bond formation between thermally denatured β‐lactoglobulin and κ‐casein in casein micelles . J. Dairy Sci. , 73 : 900
  • Haque , Z. , Kristjansson , M. M. and Kinsella , J. E. 1987 . Interaction between casein and β‐lacto‐globulin: possible mechanism . J. Agric. Food Chem. , 35 : 644
  • Haque , Z. and Kinsella , J. E. 1988 . Interaction between heated κ‐casein and β‐lactoglobulin: predominance of hydrophobic interactions in the initial stages of complex formation . J. Dairy Res. , 55 : 67
  • Lyster , R. L. J. 1970 . The denaturation of α‐lactalbumin and β‐lactoglobulin in heated milk . J. Dairy Res. , 37 : 233
  • Manji , B. and Kakuda , Y. 1986 . Thermal denaturation of whey proteins in skim milk . Can. Inst. Food Sci. Technol. , 19 : 163
  • Dannenberg , F. and Kessler , H. G. 1988 . Reaction kinetics of the denaturation of whey protein in milk . J. Food Sci. , 53 : 258
  • Kessler , H. G. and Beyer , H. J. 1991 . Thermal denaturation of whey proteins and its effect in dairy technology . Int. J. Biol Macromol. , 13 : 165
  • Larson , B. L. and Rolleri , C. D. 1955 . Heat denaturation of the specific serum proteins in milk . J. Dairy Sci. , 38 : 351
  • Hiraoka , Y. and Sugai , S. 1984 . Thermodynamics of thermal unfolding of bovine apo‐α‐lactalbumin . Int. J. Peptide Protein Res. , 23 : 535
  • Segawa , T. and Sugai , S. 1983 . Interactions of divalent metal ions with bovine, human and goat alpha‐lactal‐bumins . J. Biochem. (Tokyo) , 93 : 1321
  • Kuwajima , K. , Harushima , Y. and Sugai , S. 1986 . Influence of calcium‐binding on the structure and stability of bovine alpha‐lactalbumin studied by circular dichroism and nuclear magnetic resonance spectra . Int. J. Peptide Protein Res. , 27 : 18
  • Permyakov , E. A. , Morozova , L. A. and Burstein , A. 1985 . Cation binding effects on the pH, thermal and urea denaturation transitions in α‐lactalbumin . Biophys. Chem. , 21 : 21
  • Desmet , J. , Van Dael , H. , Van Cauwelaert , F. , Nitta , K. and Shintaro , S. 1989 . Comparison of the binding of a Ca++ and Mn++ to bovine α‐lactalbumin and equine lysozyme . J. Inorgan. Biochem. , 37 : 185
  • Eynard , L. , Iametti , S. , Relkin , P. and Bonomi , F. 1992 . Surface hydrophobicity changes and heat‐induced modifications of α‐lactalbumin) . J. Agric. Food Chem. , 40 : 1732
  • Desmet , J. , Hanssens , I. and Van Cauwelaert , F. 1987 . Comparison of the binding of Na++ and Ca++ to bovine α‐lactalbumin . Biochim. Biophys. Acta , 912 : 211
  • Pfeil , W. and Sadowski , M. L. 1985 . A scanning calorimetric study of bovine and human apo‐α‐lactalbumin . Stud. Biophys. , 109 : 163
  • Relkin , P. , Launay , B. and Eynard , L. 1993 . Effects of sodium and calcium addition on thermal denaturation of apo‐α‐lactalbumin: a differential scanning calorimetric study . J. Dairy Sci. , 76 : 36
  • Hillier , R. M. 1976 . The quantitative measurement of whey proteins using polyacrylamide‐gel electro‐phoresis . J. Dairy Res. , 43 : 259
  • Harwalkar , V. R. 1986 . Kinetic study of thermal denaturation of proteins in whey . Milchwissenschaft , 41 : 206
  • Hillier , R. M. and Lyster , R. L. J. 1979 . Whey protein denaturation in heated milk and cheese whey . J. Dairy Res. , 46 : 95
  • Elfgam , A. A. and Wheelock , J. V. 1977 . Effect of heat on α‐lactalbumin and β—lactoglobulin in bovine milk . J. Dairy Res. , 44 : 367
  • Pfeil , W. 1987 . Is thermally denatured protein unfolded? the example of α‐lactalbumin . Biochim. Biophys. Acta , 911 : 114
  • Muramaki , K. , Andree , P. J. and Berliner , L. J. 1982 . Cation ion binding to alpha‐lactalbumin species . Biochemistry , 21 : 5488
  • Bratcher , S. C. and Kronman , M. J. 1984 . Inter‐ and intramolecular interactions of alpha‐lactalbumin. XTV. Metal ion binding to the N and A conformers of bovine alpha‐lactalbumin . J. Biol. Chem. , 259 : 10875
  • Tieghem , E. , Van Dael , H. and Van Cauwelaert , F. 1991 . A circular dichroic study of Cu (II) binding to bovine α‐lactalbumin . J. Inorgan. Biochem. , 42 : 119
  • Chaplin , L. C. and Lyster , R. L. 1986 . Irreversible heat denaturation of bovine α‐lactalbumin . J. Dairy Res. , 53 : 249
  • Privalov , P. L. and Monaselidze , D. R. 1963 . Thermal denaturation of bovine albumin . Biofyzica , 8 : 420
  • Itoh , T. , Wada , Y. and Nakanishi , T. 1976 . Differential thermal analysis of milk proteins . Agric. Biol. Chem. , 40 : 1083
  • Yamasaki , M. , Yano , H. and Aoki , K. 1991 . Differential scanning calorimetric studies on bovine serum albumin II. Effects of neutral salts and urea . Int. J. Biol. Macromol. , 13 : 322
  • Yamasaki , M. , Yano , H. and Aoki , K. 1990 . Differential scanning calorimetric studies on bovine serum albumin I. effects of pH and ionic strength . Int. J. Biol. Macromol. , 12 : 263
  • Hayakawa , I. , Kajihara , J. , Morikawa , K. , Oda , M. and Fujio , Y. 1992 . Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals . J. Food Sci. , 57 : 288
  • Shrake , A. , Finlayson , J. S. and Ross , P. D. 1984 . Thermal stability of human albumin measured by differential scanning calorimetry. I. Effects of caprylate and N‐acetyltryptophanate . Vox Sang , 47 : 7
  • Ross , P. D. and Shrake , A. 1988 . Decrease in stability of human albumin with increase in protein concentration . J. Biol. Chem. , 263 : 11196
  • Relkin , P. , Muller , A. and Launay , B. 1195 . “ Conforma‐tional stability of globular proteins: a DSC study of globular whey proteins ” . In Food Macromolecules and Colloids , Edited by: Dickinson , E. and Walstra , P. 167 Cambridge : Royal Society of Chemistry .

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