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Volumn 44, Issue 7, 1996, Pages 1651-1657

Protein ternary phase diagrams. 1. Effect of ethanol, ammonium sulfate, and temperature on the phase behavior of type B gelatin

Author keywords

Ethanol; Gelatin; Phase diagram; Protein; Salt

Indexed keywords


EID: 8644253643     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf950676r     Document Type: Article
Times cited : (39)

References (44)
  • 1
    • 84988119548 scopus 로고
    • Review: Enzyme inactivation during heat processing of food-stuffs
    • Adams, J. B. Review: Enzyme inactivation during heat processing of food-stuffs. Int. J. Food Sci. Technol. 1991, 26, 1-20.
    • (1991) Int. J. Food Sci. Technol. , vol.26 , pp. 1-20
    • Adams, J.B.1
  • 2
    • 0027847854 scopus 로고
    • Towards a phenomenological definition of the term "gel"
    • Almdal, K.; Dyre, J.; Hvidt, S.; Kramer, O. Towards a phenomenological definition of the term "gel". Polym. Gels Networks 1993, 1, 5-17.
    • (1993) Polym. Gels Networks , vol.1 , pp. 5-17
    • Almdal, K.1    Dyre, J.2    Hvidt, S.3    Kramer, O.4
  • 3
    • 33845471920 scopus 로고
    • Progel and gel formation and reversibility of gelation of whey, soybean and albumin protein gels
    • Beveridge, T.; Jones, L.; Tung, M. A. Progel and gel formation and reversibility of gelation of whey, soybean and albumin protein gels. J. Agric. Food Chem. 1984, 32 (4), 301-313.
    • (1984) J. Agric. Food Chem. , vol.32 , Issue.4 , pp. 301-313
    • Beveridge, T.1    Jones, L.2    Tung, M.A.3
  • 4
    • 0000778476 scopus 로고
    • Crystallization - Coacervation - flocculation
    • Kruyt, H. R., Ed.; Elsevier: New York
    • Bungenberg de Jong, H. G. Crystallization - coacervation - flocculation. In Colloid Science; Kruyt, H. R., Ed.; Elsevier: New York, 1949; pp 250-258.
    • (1949) Colloid Science , pp. 250-258
    • Bungenberg De Jong, H.G.1
  • 5
    • 0010769584 scopus 로고
    • Phase equilibria and structures in the aqueous system of wheat lipids
    • Carlson, T.; Larsson, K.; Miezis, Y. Phase equilibria and structures in the aqueous system of wheat lipids. Cereal Chem. 1976, 55, 168-179.
    • (1976) Cereal Chem. , vol.55 , pp. 168-179
    • Carlson, T.1    Larsson, K.2    Miezis, Y.3
  • 6
    • 0000017857 scopus 로고
    • Structural and mechanical properties of biopolymer gels
    • Dickinson, E., Ed.; RCS Special Publication 82; Royal Society of Chemistry: Cambridge, UK
    • Clark, A. H. Structural and mechanical properties of biopolymer gels. In Food Polymers, Gels and Colloids; Dickinson, E., Ed.; RCS Special Publication 82; Royal Society of Chemistry: Cambridge, UK, 1991; pp 322-338.
    • (1991) Food Polymers, Gels and Colloids , pp. 322-338
    • Clark, A.H.1
  • 7
    • 33947438832 scopus 로고
    • Preparation and properties of serum and plasma proteins. XIII. Crystallization of serum albumin from ethanol-water mixtures
    • Cohn, E. J.; Hughes, W. L.; Weare, J. H. Preparation and properties of serum and plasma proteins. XIII. Crystallization of serum albumin from ethanol-water mixtures. J. Am. Chem. Soc. 1947, 69, 1753-1761.
    • (1947) J. Am. Chem. Soc. , vol.69 , pp. 1753-1761
    • Cohn, E.J.1    Hughes, W.L.2    Weare, J.H.3
  • 8
    • 0343578714 scopus 로고
    • The variation of the viscosity of gelatin sols with temperature
    • Croome, R. J. The variation of the viscosity of gelatin sols with temperature. J. Appl. Chem. 1953, 3, 330-334.
    • (1953) J. Appl. Chem. , vol.3 , pp. 330-334
    • Croome, R.J.1
  • 9
    • 0039090046 scopus 로고
    • A comparative study of the flocculation and coacervation of different systems
    • Dervichian, D. G. A comparative study of the flocculation and coacervation of different systems. Discuss. Faraday Soc. 1954, 18, 231-239.
    • (1954) Discuss. Faraday Soc. , vol.18 , pp. 231-239
    • Dervichian, D.G.1
  • 10
    • 4243896358 scopus 로고
    • Chlorophyll A in bilayer membranes. I. The thermal phase diagram with disterol phosphatidylcholine
    • Eigenberg, K. E.; Croasmun, W. R.; Chan, S. I. Chlorophyll A in bilayer membranes. I. The thermal phase diagram with disterol phosphatidylcholine. Biochim. Biophys. Acta 1982, 679, 353-360.
    • (1982) Biochim. Biophys. Acta , vol.679 , pp. 353-360
    • Eigenberg, K.E.1    Croasmun, W.R.2    Chan, S.I.3
  • 11
    • 8644249131 scopus 로고    scopus 로고
    • Protein ternary phase diagrams. 2. Effect of ethanol, ammonium sulfate, and temperature on the phase behavior of (S)-ovalbumin
    • Elysée-Collen, B.; Lencki, R. W. Protein ternary phase diagrams. 2. Effect of ethanol, ammonium sulfate, and temperature on the phase behavior of (S)-ovalbumin. J. Agric. Food Chem. 1996, 44, 1658-1663.
    • (1996) J. Agric. Food Chem. , vol.44 , pp. 1658-1663
    • Elysée-Collen, B.1    Lencki, R.W.2
  • 12
    • 0039515927 scopus 로고
    • Phase diagrams in kappa-carageenan/locust bean gum systems
    • Fernandes, P. B.; Gonçalves, M. P.; Doublier, J. L. Phase diagrams in kappa-carageenan/locust bean gum systems. Food Hydrocol. 1991, 5 (1/2), 71-73.
    • (1991) Food Hydrocol. , vol.5 , Issue.1-2 , pp. 71-73
    • Fernandes, P.B.1    Gonçalves, M.P.2    Doublier, J.L.3
  • 13
    • 0008734428 scopus 로고
    • The physical properties of gelatin
    • Ward, A. G., Court, A., Eds.; Academic: New York
    • Finch, C. A.; Jobling, A. The physical properties of gelatin. In The Science and Technology of Gelatin; Ward, A. G., Court, A., Eds.; Academic: New York, 1977; pp 250-294.
    • (1977) The Science and Technology of Gelatin , pp. 250-294
    • Finch, C.A.1    Jobling, A.2
  • 14
    • 0001243741 scopus 로고
    • Turbidity and hardness of a heat-induced gel of hen egg ovalbumin
    • Hatta, H.; Kitabatake, N.; Doi, E. Turbidity and hardness of a heat-induced gel of hen egg ovalbumin. Agric. Biol. Chem. 1986, 50, 2083-2089.
    • (1986) Agric. Biol. Chem. , vol.50 , pp. 2083-2089
    • Hatta, H.1    Kitabatake, N.2    Doi, E.3
  • 15
    • 0343578712 scopus 로고
    • Gelation of gelatin solution
    • Hayashi, A.; Oh, S.-C. Gelation of gelatin solution. Agric. Biol. Chem. 1983, 47, 1711-1716.
    • (1983) Agric. Biol. Chem. , vol.47 , pp. 1711-1716
    • Hayashi, A.1    Oh, S.-C.2
  • 16
    • 0014681791 scopus 로고
    • Structural stability and solvent denaturation of myoglobin
    • Herskovits, T. T.; Jaillet, H. Structural stability and solvent denaturation of myoglobin. Science 1969, 763, 282-285.
    • (1969) Science , vol.763 , pp. 282-285
    • Herskovits, T.T.1    Jaillet, H.2
  • 17
    • 51649143786 scopus 로고
    • Lyophilic colloids. XIX. Effect of several neutral salts and nonelectrolytes on isoelectric gelatin sol
    • Holleman, L. W. J.; Bungenberg de Jong, H. G.; Tjaden Modderman, R. S. Lyophilic colloids. XIX. Effect of several neutral salts and nonelectrolytes on isoelectric gelatin sol. Kolloid-Beihefte 1933, 38, 439-460.
    • (1933) Kolloid-Beihefte , vol.38 , pp. 439-460
    • Holleman, L.W.J.1    Bungenberg De Jong, H.G.2    Tjaden Modderman, R.S.3
  • 18
    • 0001479796 scopus 로고
    • Thermodynamics of polymer compatibility in ternary systems
    • Hsu, C. C.; Prausnitz, J. M. Thermodynamics of polymer compatibility in ternary systems. Macromolecules 1974, 7, 320-328.
    • (1974) Macromolecules , vol.7 , pp. 320-328
    • Hsu, C.C.1    Prausnitz, J.M.2
  • 19
    • 0002115791 scopus 로고
    • Relationship between collagen and gelatin
    • Ward, A. G., Court, A., Eds.; Academic: New York
    • Johns, P.; Court, A. Relationship between collagen and gelatin. In The Science and Technology of Gelatin; Ward, A. G., Court, A., Eds.; Academic: New York, 1977; pp 138-178.
    • (1977) The Science and Technology of Gelatin , pp. 138-178
    • Johns, P.1    Court, A.2
  • 20
    • 8644292390 scopus 로고
    • Harris, P. H., Ed.; Elsevier: New York
    • Johnston-Banks, F. A. Gelatine. In Food Gels; Harris, P. H., Ed.; Elsevier: New York, 1990; pp 233-290.
    • (1990) Food Gels , pp. 233-290
    • Gelatine, J.F.A.1
  • 21
    • 0025246663 scopus 로고
    • Hydrophobic chromatography
    • Deutscher, M. P., Ed.; Academic: San Diego, CA
    • Kennedy, R. M. Hydrophobic chromatography. In Methods in Enzymology; Deutscher, M. P., Ed.; Academic: San Diego, CA, 1990; Vol. 182, pp 339-346.
    • (1990) Methods in Enzymology , vol.182 , pp. 339-346
    • Kennedy, R.M.1
  • 22
    • 0344311689 scopus 로고
    • The aqueous system of monogalactosyl diglycerides and digalactosyl diglycerides - Significance to the structure of the thylalkoid membrane
    • Larsson, K.; Puang-Ngern, S. The aqueous system of monogalactosyl diglycerides and digalactosyl diglycerides - significance to the structure of the thylalkoid membrane. Dev. Plant Biol. 1979, 3, 27-33.
    • (1979) Dev. Plant Biol. , vol.3 , pp. 27-33
    • Larsson, K.1    Puang-Ngern, S.2
  • 23
    • 0002297283 scopus 로고
    • Gelation of gelatin
    • Mitchell, J. R., Ledward, D. A., Eds.; Elsevier: New York
    • Ledward, D. A. Gelation of gelatin. In Functional Properties of Food Macromolecules; Mitchell, J. R., Ledward, D. A., Eds.; Elsevier: New York, 1985; pp 171-201.
    • (1985) Functional Properties of Food Macromolecules , pp. 171-201
    • Ledward, D.A.1
  • 24
    • 0026970477 scopus 로고
    • Effect of subunit dissociation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior
    • Lencki, R. W.; Arul, J.; Neufeld, R. J. Effect of subunit dissociation, aggregation, coagulation, and decomposition on enzyme inactivation kinetics: II. Biphasic and grace period behavior. Biotechnol. Bioeng. 1992, 40, 1427-1434.
    • (1992) Biotechnol. Bioeng. , vol.40 , pp. 1427-1434
    • Lencki, R.W.1    Arul, J.2    Neufeld, R.J.3
  • 25
    • 0017623134 scopus 로고
    • Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series
    • Melander, W.; Horvath, C. Salt effects on hydrophobic interactions in precipitation and chromatography of proteins: An interpretation of the lyotropic series. Arch. Biochem. Biophys. 1977, 783, 200-215.
    • (1977) Arch. Biochem. Biophys. , vol.783 , pp. 200-215
    • Melander, W.1    Horvath, C.2
  • 26
    • 85025547740 scopus 로고
    • Effect of monovalent and divalent cations on the rheological properties of gellan gels
    • Moritaka, H.; Fukuba, H.; Kumeno, K.; Nakahama, N.; Nishinari, K. Effect of monovalent and divalent cations on the rheological properties of gellan gels. Food Hydrocolloids 1991, 4, 495-507.
    • (1991) Food Hydrocolloids , vol.4 , pp. 495-507
    • Moritaka, H.1    Fukuba, H.2    Kumeno, K.3    Nakahama, N.4    Nishinari, K.5
  • 27
    • 84982607471 scopus 로고
    • Complex gels of proteins and acidic polysaccharides. Part II. The effect of electrostatic interaction on structure formation in complex gels of gelatin and alginate
    • Muchin, M. A.; Streltsova, Z. A.; Vajnerman, E. S.; Tolstoguzov, V. B. Complex gels of proteins and acidic polysaccharides. Part II. The effect of electrostatic interaction on structure formation in complex gels of gelatin and alginate. Nahrung 1978, 22 (10), 867-871.
    • (1978) Nahrung , vol.22 , Issue.10 , pp. 867-871
    • Muchin, M.A.1    Streltsova, Z.A.2    Vajnerman, E.S.3    Tolstoguzov, V.B.4
  • 28
    • 84982531319 scopus 로고
    • Thermodynamic compatibility of proteins in aqueous media. Part I. Phase diagrams of some water - Protein A - protein B systems
    • Polyakov, V. I.; Kireyeva, O. K.; Grinberg, V. Y.; Tolstoguzov, V. B. Thermodynamic compatibility of proteins in aqueous media. Part I. Phase diagrams of some water - protein A - protein B systems. Nahrung 1985, 29, 153-160.
    • (1985) Nahrung , vol.29 , pp. 153-160
    • Polyakov, V.I.1    Kireyeva, O.K.2    Grinberg, V.Y.3    Tolstoguzov, V.B.4
  • 29
    • 0001001105 scopus 로고
    • Mechanical properties of globular protein gels: 1. Incipient gelation behavior
    • Richardson, R. K.; Ross-Murphy, S. B. Mechanical properties of globular protein gels: 1. Incipient gelation behavior. Int. J. Biol. Macromol. 1981, 3, 315-320.
    • (1981) Int. J. Biol. Macromol. , vol.3 , pp. 315-320
    • Richardson, R.K.1    Ross-Murphy, S.B.2
  • 30
    • 0025208216 scopus 로고
    • Ion-exchange chromatography
    • Deutscher, M. P., Ed.; Academic: San Diego, CA
    • Rossomando, E. F. Ion-exchange chromatography. In Methods in Enzymology; Deutscher, M. P., Ed.; Academic: San Diego, CA, 1990; Vol. 182, pp 309-320.
    • (1990) Methods in Enzymology , vol.182 , pp. 309-320
    • Rossomando, E.F.1
  • 33
    • 0000983898 scopus 로고
    • Polymer-chemical properties of gelatin in foods
    • Slade, L.; Levine, H. Polymer-chemical properties of gelatin in foods. Adv. Meat Res. 1987, 4, 251-266.
    • (1987) Adv. Meat Res. , vol.4 , pp. 251-266
    • Slade, L.1    Levine, H.2
  • 34
    • 85025575777 scopus 로고
    • Viscoelastic behavior of β-lactoglobulin gel structures
    • Stading, M.; Hermannson, A. M. Viscoelastic behavior of β-lactoglobulin gel structures. Food Hydrocolloids 1990, 4, 121-135.
    • (1990) Food Hydrocolloids , vol.4 , pp. 121-135
    • Stading, M.1    Hermannson, A.M.2
  • 35
    • 0001852940 scopus 로고
    • The gelatin gel and the sol-gel transformation
    • Ward, A. G., Court, A., Eds.; Academic: New York
    • Stainsby, G. The gelatin gel and the sol-gel transformation. In The Science and Technology of Gelatin; Ward, A. G., Court, A., Eds.; Academic: New York, 1977; pp 179-208.
    • (1977) The Science and Technology of Gelatin , pp. 179-208
    • Stainsby, G.1
  • 36
    • 84981426958 scopus 로고
    • A percolation analysis of the concentration dependence of the gelation of whey protein concentrates
    • Steventon, A. J.; Gladden, L. F.; Fryer, P. J. A percolation analysis of the concentration dependence of the gelation of whey protein concentrates. J. Text. Stud. 1991, 22, 201-218.
    • (1991) J. Text. Stud. , vol.22 , pp. 201-218
    • Steventon, A.J.1    Gladden, L.F.2    Fryer, P.J.3
  • 37
    • 0018486910 scopus 로고
    • Studies on the rigidity of gelatine gels
    • Tar, I.; Wolfram, E. Studies on the rigidity of gelatine gels. Br. Polym. J. 1979, 11, 97-99.
    • (1979) Br. Polym. J. , vol.11 , pp. 97-99
    • Tar, I.1    Wolfram, E.2
  • 39
    • 8644282602 scopus 로고
    • Effects of amino acid composition and microenvironment on protein structure
    • Whitaker, J. R., Tannenbaum, S. R., Eds.; AVI: Westport, CT
    • van Holde, K E. Effects of amino acid composition and microenvironment on protein structure. In Food Proteins; Whitaker, J. R., Tannenbaum, S. R., Eds.; AVI: Westport, CT, 1977; pp 1-13.
    • (1977) Food Proteins , pp. 1-13
    • Van Holde, K.E.1
  • 40
    • 0009940455 scopus 로고
    • Neutral salts: The generality of their effects on the stability of macromolecular conformations
    • von Hippel, P. H.; Wong, K.-Y. Neutral salts: The generality of their effects on the stability of macromolecular conformations. Science 1964, 14, 577-580.
    • (1964) Science , vol.14 , pp. 577-580
    • Von Hippel, P.H.1    Wong, K.-Y.2
  • 41
    • 0002762987 scopus 로고
    • Physical tests for gelatin and gelatin products
    • Ward, A. G., Court, A., Eds.; Academic: New York
    • Wainewright, F. W. Physical tests for gelatin and gelatin products. In The Science and Technology of Gelatin; Ward, A. G., Court, A., Eds.; Academic: New York, 1977; pp 507-534.
    • (1977) The Science and Technology of Gelatin , pp. 507-534
    • Wainewright, F.W.1
  • 43
    • 0011942727 scopus 로고
    • Technical and pharmaceutical uses of gelatin
    • Ward, A. G., Court, A., Eds.; Academic: New York
    • Wood, P. D. Technical and pharmaceutical uses of gelatin. In The Science and Technology of Gelatin; Ward, A. G., Court, A., Eds.; Academic: New York, 1977; pp 414-438.
    • (1977) The Science and Technology of Gelatin , pp. 414-438
    • Wood, P.D.1


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