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Volumn 44, Issue 12, 1996, Pages 3939-3945

Thermal Stabilization of β-Lactoglobulin by Whey Peptide Fractions

Author keywords

Differential scanning calorimetry; Thermal denaturation; Whey peptides; Lactoglobulin

Indexed keywords


EID: 0000480144     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf960081b     Document Type: Article
Times cited : (25)

References (62)
  • 1
    • 0001919523 scopus 로고
    • Enzymatic hydrolysis of food proteins
    • Adler-Nissen, J. Enzymatic hydrolysis of food proteins. Process Biochem. 1977, 12, 18-19, 22-23, 32.
    • (1977) Process Biochem. , vol.12 , pp. 18-19
    • Adler-Nissen, J.1
  • 2
    • 0014117822 scopus 로고
    • On the average hydrophobicity of proteins and the relation between it and protein structure
    • Bigelow, C. C. On the average hydrophobicity of proteins and the relation between it and protein structure. J. Theor. Biol. 1967, 16, 187-211.
    • (1967) J. Theor. Biol. , vol.16 , pp. 187-211
    • Bigelow, C.C.1
  • 3
    • 0023693897 scopus 로고
    • Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature
    • Casal, H. L.; Kohler, U.; Mantsch, H. N. Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature. Biochim. Biophys. Acta 1988, 957, 11-20.
    • (1988) Biochim. Biophys. Acta , vol.957 , pp. 11-20
    • Casal, H.L.1    Kohler, U.2    Mantsch, H.N.3
  • 4
    • 84971943452 scopus 로고
    • A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperature up to 160 °C
    • de Wit, J. N.; Klarenbeek, G. A differential scanning calorimetric study of the thermal behaviour of bovine β-lactoglobulin at temperature up to 160 °C. J. Dairy Res. 1981, 48, 293-302.
    • (1981) J. Dairy Res. , vol.48 , pp. 293-302
    • De Wit, J.N.1    Klarenbeek, G.2
  • 5
    • 85007844131 scopus 로고
    • Effects of various heat treatments on structure and solubility of whey proteins
    • de Wit, J. N.; Klarenbeek, G. Effects of various heat treatments on structure and solubility of whey proteins. J. Dairy Sci. 1984, 67, 2701-2710.
    • (1984) J. Dairy Sci. , vol.67 , pp. 2701-2710
    • De Wit, J.N.1    Klarenbeek, G.2
  • 6
    • 0002864325 scopus 로고
    • Structure and functional behaviour of whey proteins
    • de Wit, J. N. Structure and functional behaviour of whey proteins. Neth. Milk Dairy J. 1981, 35, 47-64.
    • (1981) Neth. Milk Dairy J. , vol.35 , pp. 47-64
    • De Wit, J.N.1
  • 8
    • 0001510699 scopus 로고
    • Binding affinities of β-ionone and related flavor compounds to β-lactoglobulin: Effects of chemical modifications
    • Dufour, E.; Tomasz, H. Binding affinities of β-ionone and related flavor compounds to β-lactoglobulin: Effects of chemical modifications. J. Agric. Food Chem. 1990, 38, 1691-1695.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1691-1695
    • Dufour, E.1    Tomasz, H.2
  • 9
    • 0013852547 scopus 로고
    • Etude d'une étape réversible dans la thermodénaturation de la β-lactoglobuline bovine A
    • Dupont, M. A. Etude d'une étape réversible dans la thermodénaturation de la β-lactoglobuline bovine A. Biochim. Biophys. Acta 1965, 102, 500-513.
    • (1965) Biochim. Biophys. Acta , vol.102 , pp. 500-513
    • Dupont, M.A.1
  • 10
    • 0001675319 scopus 로고
    • Modern aspects of the primary structure and function of β-lactoglobulins
    • Godovac-Zimmermann, J.; Braunitzer, G. Modern aspects of the primary structure and function of β-lactoglobulins. Milchwissenschaft 1987, 42, 294-297.
    • (1987) Milchwissenschaft , vol.42 , pp. 294-297
    • Godovac-Zimmermann, J.1    Braunitzer, G.2
  • 11
    • 0026575310 scopus 로고
    • Molecular dynamics simulations of the whey protein β-lactoglobulin
    • Gu, W.; Brady, J. W. Molecular dynamics simulations of the whey protein β-lactoglobulin. Protein Eng. 1992, 5, 17-27.
    • (1992) Protein Eng. , vol.5 , pp. 17-27
    • Gu, W.1    Brady, J.W.2
  • 12
    • 0018286348 scopus 로고
    • Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry
    • Gumpen, S.; Hegg, P. O.; Martens, H. Thermal stability of fatty acid-serum albumin complexes studied by differential scanning calorimetry. Biochim. Biophys. Acta 1979, 574, 189-196.
    • (1979) Biochim. Biophys. Acta , vol.574 , pp. 189-196
    • Gumpen, S.1    Hegg, P.O.2    Martens, H.3
  • 13
    • 0001341678 scopus 로고
    • Milk Proteins: Molecular, Physical, Chemical, and Biological Aspects
    • Fox, P. F., Ed.; Applied Science. London
    • Hambling, S. G.; McAlpine, A. S.; Sawyer, L. Milk Proteins: Molecular, Physical, Chemical, and Biological Aspects. In Advanced Dairy Chemistry-1.; Fox, P. F., Ed.; Applied Science. London, 1992; pp 141-189.
    • (1992) Advanced Dairy Chemistry-1 , pp. 141-189
    • Hambling, S.G.1    McAlpine, A.S.2    Sawyer, L.3
  • 14
    • 0000611236 scopus 로고
    • Interaction between κ-casein and β-lactoglobulin: Possible mechanism
    • Haque, Z.; Kristjansson, M. M.; Kinsella, J. E. Interaction between κ-casein and β-lactoglobulin: possible mechanism. J. Agric. Food Chem. 1987, 35, 644-649.
    • (1987) J. Agric. Food Chem. , vol.35 , pp. 644-649
    • Haque, Z.1    Kristjansson, M.M.2    Kinsella, J.E.3
  • 15
    • 84976156372 scopus 로고
    • Interaction between κ-casein and β-lactoglobulin predominance of hydrophobic interactions in the initial stages of complex formation
    • Haque, Z.; Kinsella, J. E. Interaction between κ-casein and β-lactoglobulin predominance of hydrophobic interactions in the initial stages of complex formation. J. Dairy Res. 1988, 55, 67-80.
    • (1988) J. Dairy Res. , vol.55 , pp. 67-80
    • Haque, Z.1    Kinsella, J.E.2
  • 17
    • 0001838003 scopus 로고
    • Study of thermodynamics and kinetics of protein stability by thermal analysis
    • Elsevier Science: New York
    • Harwalkar, V. R.; Ma, C. Y. Study of thermodynamics and kinetics of protein stability by thermal analysis. In Thermal Analysis of Foods; Elsevier Science: New York, 1990; pp 16-50.
    • (1990) Thermal Analysis of Foods , pp. 16-50
    • Harwalkar, V.R.1    Ma, C.Y.2
  • 18
    • 85032068892 scopus 로고
    • Whey protein denaturation in heated milk and cheese whey
    • Hillier, R. M.; Lyster, R. L. J. Whey protein denaturation in heated milk and cheese whey. J. Dairy Res. 1979, 46, 95-102.
    • (1979) J. Dairy Res. , vol.46 , pp. 95-102
    • Hillier, R.M.1    Lyster, R.L.J.2
  • 20
    • 0025679061 scopus 로고
    • Characteristics of the interaction of calcium with casein submicelles as determined by analytical affinity chromatography
    • Jang, H. D.; Swaisgood, H. E. Characteristics of the interaction of calcium with casein submicelles as determined by analytical affinity chromatography. Arch. Biochem. Biophys. 1990, 283, 318-328.
    • (1990) Arch. Biochem. Biophys. , vol.283 , pp. 318-328
    • Jang, H.D.1    Swaisgood, H.E.2
  • 21
    • 0023765564 scopus 로고
    • Enhanced thermodynamic stability of β-lactoglobulin at low pH
    • Kella, N. K. D.; Kinsella, J. E. Enhanced thermodynamic stability of β-lactoglobulin at low pH. Biochem. J. 1988, 255, 113-118.
    • (1988) Biochem. J. , vol.255 , pp. 113-118
    • Kella, N.K.D.1    Kinsella, J.E.2
  • 22
    • 0001453945 scopus 로고
    • Effects of medium composition, preheating, and chemical modification upon thermal behavior of oat globulin and β-lactoglobulin
    • Fox, P. F., Condon, J. J. Eds.; Applied Science. London
    • Kinsella, J. E. Effects of medium composition, preheating, and chemical modification upon thermal behavior of oat globulin and β-lactoglobulin. In Food Proteins; Fox, P. F., Condon, J. J. Eds.; Applied Science. London, 1982; pp 210-251.
    • (1982) Food Proteins , pp. 210-251
    • Kinsella, J.E.1
  • 23
    • 0001353395 scopus 로고
    • A heat denaturation study of the 11S globulin in soyabean seeds
    • Koshiyama, I.; Hamano, M.; Fukushima, D. A heat denaturation study of the 11S globulin in soyabean seeds. Food Chem. 1981, 6, 309-322.
    • (1981) Food Chem. , vol.6 , pp. 309-322
    • Koshiyama, I.1    Hamano, M.2    Fukushima, D.3
  • 24
    • 0001759849 scopus 로고
    • Surface hydrophobicity and aggregation of β-lactoglobulin heated near neutral pH
    • Laligant, A.; Dumay, E.; Casas Valencia, C.; Cuq, J. L.; Cheftel, J. C. Surface hydrophobicity and aggregation of β-lactoglobulin heated near neutral pH. J. Agric. Food Chem. 1991, 39, 2147-2155.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 2147-2155
    • Laligant, A.1    Dumay, E.2    Casas Valencia, C.3    Cuq, J.L.4    Cheftel, J.C.5
  • 25
    • 0024460440 scopus 로고
    • Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin
    • Lapanje, S.; Poklar, N. Calorimetric and circular dichroic studies of the thermal denaturation of β-lactoglobulin. Biophys. Chem. 1989, 34, 155-161.
    • (1989) Biophys. Chem. , vol.34 , pp. 155-161
    • Lapanje, S.1    Poklar, N.2
  • 26
    • 0013943915 scopus 로고
    • Validity of the "Two-State" hypothesis for conformational transitions of proteins
    • Lumry, R.; Biltonen, R.; Brandts, J. F. Validity of the "Two-State" hypothesis for conformational transitions of proteins. Biopolymers 1966, 4, 917-944.
    • (1966) Biopolymers , vol.4 , pp. 917-944
    • Lumry, R.1    Biltonen, R.2    Brandts, J.F.3
  • 27
    • 84976048291 scopus 로고
    • The denaturation of alpha-lactalbumine and bêta-lactoglobulin in heated milk
    • Lyster, L. J. The denaturation of alpha-lactalbumine and bêta-lactoglobulin in heated milk. J. Dairy Res. 1970, 37, 233-243.
    • (1970) J. Dairy Res. , vol.37 , pp. 233-243
    • Lyster, L.J.1
  • 28
    • 84987277514 scopus 로고
    • Studies of thermal denaturation of oat globulin by differential scanning calorimetry
    • Ma, C. Y.; Harwalkar, V. R. Studies of thermal denaturation of oat globulin by differential scanning calorimetry. J. Food Sci. 1988, 53, 531-534.
    • (1988) J. Food Sci. , vol.53 , pp. 531-534
    • Ma, C.Y.1    Harwalkar, V.R.2
  • 29
    • 0000125782 scopus 로고
    • β-lactoglobulin
    • McKenzie, H. A., Ed.; Academic: New York
    • McKenzie, H. A. β-lactoglobulin. In Milk Proteins-II; McKenzie, H. A., Ed.; Academic: New York, 1971; pp 257-330.
    • (1971) Milk Proteins-II , pp. 257-330
    • McKenzie, H.A.1
  • 30
    • 0015075957 scopus 로고
    • The denaturation of proteins: Two state? Reversible or irreversible?
    • McKenzie, H. A.; Ralston, G. B. The denaturation of proteins: two state? Reversible or irreversible?. Experientia 1971, 27, 617-744.
    • (1971) Experientia , vol.27 , pp. 617-744
    • McKenzie, H.A.1    Ralston, G.B.2
  • 31
    • 85025345712 scopus 로고
    • Thermal aggregation and gelation of bovine β-lactoglobulin
    • McSwiney, M.; Singh, H.; Campanella, O. Thermal aggregation and gelation of bovine β-lactoglobulin. Food Hydrocolloids 1994, 8(5), 441-453.
    • (1994) Food Hydrocolloids , vol.8 , Issue.5 , pp. 441-453
    • McSwiney, M.1    Singh, H.2    Campanella, O.3
  • 32
    • 0023661017 scopus 로고
    • Crystal structure of the trigonal β-lactoglobulin and of its complex with retinol at 2.5 Å resolution
    • Monaco, H. L.; Zanotti, G.; Spadon, P.; Bolognesi, P.; Sawyer, L.; Eliopoulos, E. E. Crystal structure of the trigonal β-lactoglobulin and of its complex with retinol at 2.5 Å resolution. J. Mol. Biol. 1987, 197, 695-706.
    • (1987) J. Mol. Biol. , vol.197 , pp. 695-706
    • Monaco, H.L.1    Zanotti, G.2    Spadon, P.3    Bolognesi, P.4    Sawyer, L.5    Eliopoulos, E.E.6
  • 35
    • 0000760427 scopus 로고
    • Calorimetric study of the thermal denaturation of β-lactoglobulin
    • Park, K. H.; Lund, D. B. Calorimetric study of the thermal denaturation of β-lactoglobulin. J. Dairy Sci. 1984, 67, 1699-1706.
    • (1984) J. Dairy Sci. , vol.67 , pp. 1699-1706
    • Park, K.H.1    Lund, D.B.2
  • 36
    • 0001253172 scopus 로고
    • Thermal stability of whey proteins studied by differential scanning calorimetry
    • Paulsson, M.; Negg, P.-O.; Castberg, H. H. Thermal stability of whey proteins studied by differential scanning calorimetry. Thermochim. Acta 1985, 95, 435-440.
    • (1985) Thermochim. Acta , vol.95 , pp. 435-440
    • Paulsson, M.1    Negg, P.-O.2    Castberg, H.H.3
  • 37
    • 0345436424 scopus 로고
    • Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry
    • Paulsson, M.; Dejmek, P. Thermal denaturation of whey proteins in mixtures with caseins studied by differential scanning calorimetry. J. Dairy Sci. 1990, 73, 590-600.
    • (1990) J. Dairy Sci. , vol.73 , pp. 590-600
    • Paulsson, M.1    Dejmek, P.2
  • 38
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of turbidimetric technique
    • Pearce, K. N.; Kinsella, J. E. Emulsifying properties of proteins: evaluation of turbidimetric technique. J. Agric. Food Chem. 1978, 26, 716-723.
    • (1978) J. Agric. Food Chem. , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 39
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of ribotrypsinogen, ribonuclease and myoglobin
    • Privalov, P. L.; Khechinashvili, N. N.; Atanasov, B. P. Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of ribotrypsinogen, ribonuclease and myoglobin. Biopolymers 1971, 10, 1865-1890.
    • (1971) Biopolymers , vol.10 , pp. 1865-1890
    • Privalov, P.L.1    Khechinashvili, N.N.2    Atanasov, B.P.3
  • 40
    • 0016224361 scopus 로고
    • A thermodynamic approach to the problem of stabilization of globular protein structure: A Calorimetric study
    • Privalov, P. L.; Khechinashvili, N. N. A thermodynamic approach to the problem of stabilization of globular protein structure: A Calorimetric study. J. Mol. Biol. 1974, 86, 665-684.
    • (1974) J. Mol. Biol. , vol.86 , pp. 665-684
    • Privalov, P.L.1    Khechinashvili, N.N.2
  • 41
    • 84916555996 scopus 로고
    • Effect of binding of retinol and palmitic acid bovine β-lactoglobulin on its resistance to thermal denaturation
    • Puyol, P.; Perez, M. D.; Peiro, J. M.; Calvo, M. Effect of binding of retinol and palmitic acid bovine β-lactoglobulin on its resistance to thermal denaturation. J. Dairy Sci. 1994, 77, 1494-1502.
    • (1994) J. Dairy Sci. , vol.77 , pp. 1494-1502
    • Puyol, P.1    Perez, M.D.2    Peiro, J.M.3    Calvo, M.4
  • 42
    • 0000443256 scopus 로고
    • Structural and conformational basis of the resistance of bêta-lactoglobulin to peptic and chymotryptic digestion
    • Reddy, I. M.; Kella, N. K. D.; Kinsella, J. E. Structural and conformational basis of the resistance of bêta-lactoglobulin to peptic and chymotryptic digestion. J. Agric. Food Chem. 1988, 36 (4), 737-741.
    • (1988) J. Agric. Food Chem. , vol.36 , Issue.4 , pp. 737-741
    • Reddy, I.M.1    Kella, N.K.D.2    Kinsella, J.E.3
  • 43
    • 0001230130 scopus 로고
    • Differential scanning calorimetry: A useful tool for studying protein denaturation
    • Relkin, P. Differential scanning calorimetry: a useful tool for studying protein denaturation. Thermochim. Acta 1994, 246 (2), 371-386.
    • (1994) Thermochim. Acta , vol.246 , Issue.2 , pp. 371-386
    • Relkin, P.1
  • 44
    • 85025552328 scopus 로고
    • Concentration effects on the kinetics of β-lactoglobulin heat denaturation: A differential scanning calorimetric study
    • Relkin, P.; Launay, B. Concentration effects on the kinetics of β-lactoglobulin heat denaturation: a differential scanning calorimetric study. Food Hydrocolloids 1990, 4, 19-26.
    • (1990) Food Hydrocolloids , vol.4 , pp. 19-26
    • Relkin, P.1    Launay, B.2
  • 45
    • 0342421704 scopus 로고
    • Effect of sodium and calcium addition on thermal denaturation of apo-α-lactalbumin: A differential scanning calorimetric study
    • Relkin, P.; Launay, B.; Eynard, L. Effect of sodium and calcium addition on thermal denaturation of apo-α-lactalbumin: a differential scanning calorimetric study. J. Dairy Sci. 1993, 76, 36-47.
    • (1993) J. Dairy Sci. , vol.76 , pp. 36-47
    • Relkin, P.1    Launay, B.2    Eynard, L.3
  • 46
    • 0016691950 scopus 로고
    • Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study
    • Rüegg, M.; Moor, U.; Blanc, B. Hydration and thermal denaturation of β-lactoglobulin. A calorimetric study. Biochim. Biophys. Acta 1975, 400, 534-542.
    • (1975) Biochim. Biophys. Acta , vol.400 , pp. 534-542
    • Rüegg, M.1    Moor, U.2    Blanc, B.3
  • 47
    • 84976113450 scopus 로고
    • A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate
    • Rüegg, M.; Moor, U.; Blanc, B. A calorimetric study of the thermal denaturation of whey proteins in simulated milk ultrafiltrate. J. Dairy Res. 1977, 44, 509-520.
    • (1977) J. Dairy Res. , vol.44 , pp. 509-520
    • Rüegg, M.1    Moor, U.2    Blanc, B.3
  • 48
    • 0000437462 scopus 로고
    • Heat denaturation of bovine β-lactoglobulin and relevance of disulfide aggregation
    • Sawyer, W. H. Heat denaturation of bovine β-lactoglobulin and relevance of disulfide aggregation. J. Dairy Sci. 1968, 51, 323-329.
    • (1968) J. Dairy Sci. , vol.51 , pp. 323-329
    • Sawyer, W.H.1
  • 49
    • 0014565143 scopus 로고
    • Complex between β-lactoglobulin and κ-casein. A review
    • Sawyer, W. H. Complex between β-lactoglobulin and κ-casein. A review. J. Dairy Sci. 1969, 52, 1347-1355.
    • (1969) J. Dairy Sci. , vol.52 , pp. 1347-1355
    • Sawyer, W.H.1
  • 50
    • 0015239798 scopus 로고
    • Thermodenaturation of bovine β-lactoglobulin. Kinetics and the introduction of β structure
    • Sawyer, W. H.; Norton, R. S.; Nichol, L. W.; McKenzie, G. H. Thermodenaturation of bovine β-lactoglobulin. Kinetics and the introduction of β structure. Biochim. Biophys. Acta 1971, 243, 19-26.
    • (1971) Biochim. Biophys. Acta , vol.243 , pp. 19-26
    • Sawyer, W.H.1    Norton, R.S.2    Nichol, L.W.3    McKenzie, G.H.4
  • 51
    • 1542652441 scopus 로고
    • A spectrometric determination of trypsin and chymotrypsin
    • Schwert, G. W.; Takenaka, Y. A spectrometric determination of trypsin and chymotrypsin. Biochim. Biophys. Acta 1955, 15, 570-579.
    • (1955) Biochim. Biophys. Acta , vol.15 , pp. 570-579
    • Schwert, G.W.1    Takenaka, Y.2
  • 52
    • 0001006684 scopus 로고
    • In vitro digestibility of whey protein/ κ-casein complexes isolated from heated concentrated milk
    • Singh, H.; Creamer, L. K. In vitro digestibility of whey protein/ κ-casein complexes isolated from heated concentrated milk. J. Food Sci. 1993, 58, 299-306.
    • (1993) J. Food Sci. , vol.58 , pp. 299-306
    • Singh, H.1    Creamer, L.K.2
  • 53
    • 0001662870 scopus 로고
    • Chemistry of milk proteins
    • Fox, P. F., Condon, J. J., Eds.; Applied Science: London
    • Swaisgood, H. E. Chemistry of milk proteins. In Developments in Dairy Chemistry; Fox, P. F., Condon, J. J., Eds.; Applied Science: London, 1982; pp 1-61.
    • (1982) Developments in Dairy Chemistry , pp. 1-61
    • Swaisgood, H.E.1
  • 54
    • 0001497241 scopus 로고
    • The reversible transformation of β-lactoglobulin at pH 7.5
    • Tanford, C.; Bunville, L. G.; Nozaki, Y. The reversible transformation of β-lactoglobulin at pH 7.5. J. Am. Chem. Soc. 1959, 81, 4032-4036.
    • (1959) J. Am. Chem. Soc. , vol.81 , pp. 4032-4036
    • Tanford, C.1    Bunville, L.G.2    Nozaki, Y.3
  • 55
    • 0001257185 scopus 로고
    • Molecular interactions in β-lactoglobulin. V. The association of genetic species of β-lactoglobulin below the isoelectric point
    • Timasheff, S. N.; Townend, R. Molecular interactions in β-lactoglobulin. V. The association of genetic species of β-lactoglobulin below the isoelectric point. J. Am. Chem. Soc. 1961, 83, 464-469.
    • (1961) J. Am. Chem. Soc. , vol.83 , pp. 464-469
    • Timasheff, S.N.1    Townend, R.2
  • 56
    • 0014027395 scopus 로고
    • The optical rotatory dispersion of β-lactoglobulins
    • Timasheff, S. N.; Townend, R.; Mescanti, L. The optical rotatory dispersion of β-lactoglobulins. J. Biol. Chem. 1966, 241, 1863-1870.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1863-1870
    • Timasheff, S.N.1    Townend, R.2    Mescanti, L.3
  • 57
    • 0000819132 scopus 로고
    • Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5
    • Townend, R.; Weinberger, L.; Timasheff, S. N. Molecular interactions in β-lactoglobulin. IV. The dissociation of β-lactoglobulin below pH 3.5. J. Am. Chem. Soc. 1960, 82, 3175-3179.
    • (1960) J. Am. Chem. Soc. , vol.82 , pp. 3175-3179
    • Townend, R.1    Weinberger, L.2    Timasheff, S.N.3
  • 58
    • 0014199124 scopus 로고
    • The circular dichroism of variants of β-lactoglobulin
    • Townend, R.; Kumosinski, T. F.; Timashef,. S. N. The circular dichroism of variants of β-lactoglobulin. J. Biol. Chem. 1967, 242, 4538-4545.
    • (1967) J. Biol. Chem. , vol.242 , pp. 4538-4545
    • Townend, R.1    Kumosinski, T.F.2    Timashef, S.N.3
  • 60
    • 84987371315 scopus 로고
    • Whey peptide fractions obtained with a two-step ultrafiltration process: Production and characterization
    • Turgeon, S. L.; Gauthier, S. F. Whey peptide fractions obtained with a two-step ultrafiltration process: Production and characterization. J. Food Sci. 1990, 55, 106-110, 157.
    • (1990) J. Food Sci. , vol.55 , pp. 106-110
    • Turgeon, S.L.1    Gauthier, S.F.2
  • 61
    • 0022900156 scopus 로고
    • HPLC analytical separation of peptides according to their molecular weight
    • Vijayalakshmi, M. A.; Lemieux, L.; Amiot, J. HPLC analytical separation of peptides according to their molecular weight. J. Liq. Chromatogr. 1986, 9, 3559-3576.
    • (1986) J. Liq. Chromatogr. , vol.9 , pp. 3559-3576
    • Vijayalakshmi, M.A.1    Lemieux, L.2    Amiot, J.3
  • 62
    • 0000550638 scopus 로고
    • Influence of pH and ionic environment on thermal aggregation pf whey proteins
    • Xiong, Y. L. Influence of pH and ionic environment on thermal aggregation pf whey proteins. J. Agric. Food Chem. 1992, 40, 380-384.
    • (1992) J. Agric. Food Chem. , vol.40 , pp. 380-384
    • Xiong, Y.L.1


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