메뉴 건너뛰기




Volumn , Issue , 2017, Pages 25-56

Thermal denaturation and coagulation of proteins

Author keywords

[No Author keywords available]

Indexed keywords

FOOD PROCESSING; PROCESSING; PROTEINS;

EID: 85052700473     PISSN: None     EISSN: None     Source Type: Book    
DOI: 10.1201/9780203755617     Document Type: Chapter
Times cited : (87)

References (125)
  • 1
    • 0002301704 scopus 로고
    • Protein functionality: Classification, definition and methodology
    • (A. Pour-El, ed.), ACS Symp. Series, No. 147. American Chemical Society, Washington, DC
    • A. Pour-El. Protein functionality: classification, definition and methodology, Protein Functionality in Foods (A. Pour-El, ed.), ACS Symp. Series, No. 147. American Chemical Society, Washington, DC, 1981, p. 5.
    • (1981) Protein Functionality in Foods , pp. 5
    • Pour-El, A.1
  • 2
    • 84963187703 scopus 로고
    • Functional properties of proteins in foods: A survey
    • J. E. Kinsella, Functional properties of proteins in foods: A survey, CRC Crit. Rev. Food Sci. Nutr. 7:219 (1976).
    • (1976) CRC Crit. Rev. Food Sci. Nutr. , vol.7 , pp. 219
    • Kinsella, J.E.1
  • 3
    • 0002712182 scopus 로고
    • Interrelationship of molecular and functional properties of food proteins
    • (J. E. Kinsella and W. G. Soucie, eds.), American Oil Chemists Society, Champaign, IL
    • S. Damodaran, Interrelationship of molecular and functional properties of food proteins. Food Proteins (J. E. Kinsella and W. G. Soucie, eds.), American Oil Chemists Society, Champaign, IL, 1989, p. 43.
    • (1989) Food Proteins , pp. 43
    • Damodaran, S.1
  • 4
    • 0003019884 scopus 로고
    • Whey proteins and their thermal denaturation—a review
    • D. M. Mulvihill and M. Donovan. Whey proteins and their thermal denaturation—a reviewIrish J. Food Sci. Technol. 11:43 (1987).
    • (1987) Irish J. Food Sci. Technol , vol.11 , pp. 43
    • Mulvihill, D.M.1    Donovan, M.2
  • 5
    • 0014364651 scopus 로고
    • Protein denaturation
    • C. Tanford, Protein denaturation, Adv. Protein Chem. 23:121 (1968).
    • (1968) Adv. Protein Chem. , vol.23 , pp. 121
    • Tanford, C.1
  • 6
    • 0000745165 scopus 로고
    • Physical consequences of thermal reactions in food protein systems
    • (H. G. Schwartzberg and R. W. Hartel, eds.), Marcel Dekker, New York
    • D. W. Stanley and R. Y. Yada, Physical consequences of thermal reactions in food protein systems, Physical Chemistry of Foods (H. G. Schwartzberg and R. W. Hartel, eds.), Marcel Dekker, New York, 1992, p. 669.
    • (1992) Physical Chemistry of Foods , pp. 669
    • Stanley, D.W.1    Yada, R.Y.2
  • 7
    • 0008863560 scopus 로고
    • Some factors in the interpretation of protein denaturation
    • W. Kauzmann, Some factors in the interpretation of protein denaturation. Adv. Protein Chem. 14:1 (1959).
    • (1959) Adv. Protein Chem , vol.14 , pp. 1
    • Kauzmann, W.1
  • 8
    • 0002432336 scopus 로고
    • Amino acids, peptides and proteins
    • (O. R. Fennema, ed.), Marcel Dekker, New York
    • J. C. Cheftel, J.-L. Cuq, and D. Lorient, Amino acids, peptides and proteins, Food Chemistry (O. R. Fennema, ed.), Marcel Dekker, New York, 1985, p. 45.
    • (1985) Food Chemistry , pp. 45
    • Cheftel, J.C.1    Cuq, J.-L.2    Lorient, D.3
  • 9
    • 0001823293 scopus 로고
    • Aggregation and denaturation involved in gel formation
    • (A. Pour-El, ed.), ACS Symp. Ser. 92, American Chemical Society, Washington, DC
    • A.-M. Hermansson. Aggregation and denaturation involved in gel formation. Functionality and Protein Structure (A. Pour-El, ed.), ACS Symp. Ser. 92, American Chemical Society, Washington, DC, 1979, p. 82.
    • (1979) Functionality and Protein Structure , pp. 82
    • Hermansson, A.-M.1
  • 10
    • 13044296146 scopus 로고
    • Thermal dissociation and association behaviour of soy proteins
    • B. German, S. Damodaran, and J. E. Kinsella, Thermal dissociation and association behaviour of soy proteins, J. Agric. Food Chem. 30:807 (1982).
    • (1982) J. Agric. Food Chem. , vol.30 , pp. 807
    • German, B.1    Damodaran, S.2    Kinsella, J.E.3
  • 15
    • 0000823423 scopus 로고
    • (A. Pour-El, ed.), ACS Symp. Ser. No. 147, American Chemical Society, Washington, DC
    • R. H. Schmidt, Gelation and coagulation, Protein Functionality in Foods (A. Pour-El, ed.), ACS Symp. Ser. No. 147, American Chemical Society, Washington, DC, 1981, p. 131.
    • (1981) Gelation and Coagulation, Protein Functionality in Foods , pp. 131
    • Schmidt, R.H.1
  • 16
    • 84971897303 scopus 로고
    • The potential application of the theory of branching processes to the association of milk protein
    • T. G. Parker and D. G. Dalgleish, The potential application of the theory of branching processes to the association of milk protein, J. Dairy Res. 44:79 (1977).
    • (1977) J. Dairy Res. , vol.44 , pp. 79
    • Parker, T.G.1    Dalgleish, D.G.2
  • 17
    • 0001561686 scopus 로고
    • Gelation phenomena of soybean globulins: Proteinprotein interactions
    • N. Catsimpoolas and E. W. Meyer, Gelation phenomena of soybean globulins: Proteinprotein interactions, Cereal Chem. 47:559 (1970).
    • (1970) Cereal Chem , vol.47 , pp. 559
    • Catsimpoolas, N.1    Meyer, E.W.2
  • 19
    • 84987318401 scopus 로고
    • Forces involved in soy protein gelation: Effects of various reagents on the formation, hardness and solubility of heat induced gels made from 7S, 1 IS and soy isolate
    • S. Utsumi and J. E. Kinsella, Forces involved in soy protein gelation: Effects of various reagents on the formation, hardness and solubility of heat induced gels made from 7S, 1 IS and soy isolate, J. Food Sci., 50:1278 (1985).
    • (1985) J. Food Sci. , vol.50 , pp. 1278
    • Utsumi, S.1    Kinsella, J.E.2
  • 20
    • 0000141024 scopus 로고
    • Thermal gelation of globular proteins: Weight-average molecular weight dependence of gel strength
    • C. H. Wang and S. Damodaran, Thermal gelation of globular proteins: Weight-average molecular weight dependence of gel strength, J. Agric. Food Chem. 38:1164 (1990).
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1164
    • Wang, C.H.1    Damodaran, S.2
  • 21
    • 0001852940 scopus 로고
    • The gelatin gel and the sol-gel transformation
    • (A. G. Ward and A. Courts, eds.). Academic Press, New York
    • G. Stainsby, The gelatin gel and the sol-gel transformation. The Science and Technology of Gelatin (A. G. Ward and A. Courts, eds.). Academic Press, New York, 1977, p. 179.
    • (1977) The Science and Technology of Gelatin , pp. 179
    • Stainsby, G.1
  • 22
    • 8644282602 scopus 로고
    • Effects of amino acid composition and microenvironment on protein structure
    • (J. R. Whitaker and S. R. Tannenbaum, eds.), AVI Publ. Inc., Westport, CT
    • K. E. Van Holde, Effects of amino acid composition and microenvironment on protein structure. Food Proteins (J. R. Whitaker and S. R. Tannenbaum, eds.), AVI Publ. Inc., Westport, CT, 1977, p. 1.
    • (1977) Food Proteins , pp. 1
    • Van Holde, K.E.1
  • 23
    • 0016411482 scopus 로고
    • Experimental and theoretical aspects of protein folding
    • C. B. Anfinsen and H. A. Scherga, Experimental and theoretical aspects of protein folding, Adv. Prot. Chem. 29:205 (1975).
    • (1975) Adv. Prot. Chem. , vol.29 , pp. 205
    • Anfinsen, C.B.1    Scherga, H.A.2
  • 24
    • 0021749888 scopus 로고
    • Thermodynamic stability and point mutations of bacteriophase t4 lysozyme
    • R. Hawkes, M. G. Grutter, and J. Schellman, Thermodynamic stability and point mutations of bacteriophase t4 lysozyme, J. Mol. Biol. 775:195 (1984).
    • (1984) J. Mol. Biol. , vol.775 , pp. 195
    • Hawkes, R.1    Grutter, M.G.2    Schellman, J.3
  • 25
    • 0018588511 scopus 로고
    • Stability of proteins. Small globular proteins
    • P. L. Privalov, Stability of proteins. Small globular proteins, Adv. Prot. Chem. 33:167 (1979).
    • (1979) Adv. Prot. Chem. , vol.33 , pp. 167
    • Privalov, P.L.1
  • 26
    • 0016812958 scopus 로고
    • Theory of reversible denaturation of globular proteins
    • N. Go, Theory of reversible denaturation of globular proteins, Int. Pept. Prot. J. 7:313(1975).
    • (1975) Int. Pept. Prot. J. , vol.7 , pp. 313
    • Go, N.1
  • 27
    • 0022566930 scopus 로고
    • Effect of temperature on food proteins and its implications on functional properties
    • A. Kilara and T. Y. Sharkasi, Effect of temperature on food proteins and its implications on functional properties, CRC Crit. Rev. Food Sci. Nulr. 23:323 (1986).
    • (1986) CRC Crit. Rev. Food Sci. Nulr. , vol.23 , pp. 323
    • Kilara, A.1    Sharkasi, T.Y.2
  • 28
    • 0026774938 scopus 로고
    • Increased exposure of hydrophobic surface in molten globule state of a-lactalbumin
    • A. K. Lala and P. Kaul, Increased exposure of hydrophobic surface in molten globule state of a-lactalbumin, J. Biol Chem. 267:19914 (1992).
    • (1992) J. Biol Chem. , vol.267 , pp. 19914
    • Lala, A.K.1    Kaul, P.2
  • 29
    • 0021114569 scopus 로고
    • Molten-globule state: A compact form of globular proteins with mobile side chains
    • M. Ohgushi and A. Wada, ‘Molten-globule state’: a compact form of globular proteins with mobile side chains, FEBS Lett. 764:21 (1983).
    • (1983) FEBS Lett , vol.764 , pp. 21
    • Ohgushi, M.1    Wada, A.2
  • 30
    • 0028873168 scopus 로고
    • Recent advances in the understanding of egg white protein functionality
    • Y. Mine, Recent advances in the understanding of egg white protein functionality, Trends Food Sci. Technol. 6:225 (1995).
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 225
    • Mine, Y.1
  • 31
    • 0010781998 scopus 로고
    • Chemistry and biological function of a-lactalbumin
    • T. P. Shukla, Chemistry and biological function of a-lactalbumin, CRC Crit. Rev. Food Technol. 3:41 (1973).
    • (1973) CRC Crit. Rev. Food Technol. , vol.3 , pp. 41
    • Shukla, T.P.1
  • 32
    • 0001501417 scopus 로고
    • Inter- and intramolecular interactions of α-lactalbumin. II. Aggregation reactions at acid pH
    • M. J. Kronman, R. Andreotti, and R. Vitols, Inter- and intramolecular interactions of α-lactalbumin. II. Aggregation reactions at acid pH, Biochemistry 3:1152 (1964).
    • (1964) Biochemistry , vol.3 , pp. 1152
    • Kronman, M.J.1    Andreotti, R.2    Vitols, R.3
  • 33
    • 0014209816 scopus 로고
    • Inter- and intramolecular interactions of α-lactalbumin. VIII. The alkaline conformational change
    • M. J. Kronman, L. G. Holmes, and F. M. Robbins, Inter- and intramolecular interactions of α-lactalbumin. VIII. The alkaline conformational change, Biochim. Biophys. Acta 733:46(1967).
    • (1967) Biochim. Biophys. Acta , vol.733 , pp. 46
    • Kronman, M.J.1    Holmes, L.G.2    Robbins, F.M.3
  • 34
    • 0023626273 scopus 로고
    • Protein folding: Hypothesis and experiments
    • O. B. Ptitsyn, Protein folding: hypothesis and experiments, J. Prot. Chem. 6:273 (1987).
    • (1987) J. Prot. Chem. , vol.6 , pp. 273
    • Ptitsyn, O.B.1
  • 35
    • 0001731813 scopus 로고
    • Irreversible thermal denaturation and formation of linear aggregates of ovalbumin
    • T. Koseki. N. Kitabatake, and E. Doi, Irreversible thermal denaturation and formation of linear aggregates of ovalbumin, Food Hydrocolloids 3:123 (1989).
    • (1989) Food Hydrocolloids , vol.3 , pp. 123
    • Koseki, T.1    Kitabatake, N.2    Doi, E.3
  • 36
    • 0001674196 scopus 로고
    • New approach to improve the gelling and surface functional properties of dried egg white by heating in dry state
    • A. Kato, H. R. Ibrahim, H. Watanabe, K. Honma, and K. Kobayashi, New approach to improve the gelling and surface functional properties of dried egg white by heating in dry state, J. Agric. Food Chem. 37:433 (1989).
    • (1989) J. Agric. Food Chem. , vol.37 , pp. 433
    • Kato, A.1    Ibrahim, H.R.2    Watanabe, H.3    Honma, K.4    Kobayashi, K.5
  • 39
    • 85023412941 scopus 로고
    • Effect of calcium binding on thermal denaturation of bovine α-lactalbumin
    • V. Bernal and P. Jelen, Effect of calcium binding on thermal denaturation of bovine α-lactalbumin, J. Dairy Sci. 67:2452 (1984).
    • (1984) J. Dairy Sci. , vol.67 , pp. 2452
    • Bernal, V.1    Jelen, P.2
  • 40
    • 0001447396 scopus 로고
    • α-Lactalbumin, Advanced Dairy Chemistry
    • (P. F. Fox, ed.), Elsevier Appl. Sci., London
    • K. Brew and J. A. Grobler, α-Lactalbumin, Advanced Dairy Chemistry, Vol. 1, Proteins (P. F. Fox, ed.), Elsevier Appl. Sci., London, 1992, p. 191.
    • (1992) Proteins , vol.1 , pp. 191
    • Brew, K.1    Grobler, J.A.2
  • 41
    • 0024343068 scopus 로고
    • Calcium regulates folding and disulfide-bond formation in α-lactalbumin
    • K. R. Rao and K. Brew, Calcium regulates folding and disulfide-bond formation in α-lactalbumin, Biochem. Biophys. Res. Commun. 163:1390 (1989).
    • (1989) Biochem. Biophys. Res. Commun. , vol.163 , pp. 1390
    • Rao, K.R.1    Brew, K.2
  • 42
    • 0019039146 scopus 로고
    • Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5
    • V. R. Harwalkar, Kinetics of thermal denaturation of β-lactoglobulin at pH 2.5, J. Dairy Sci. 63:1052 (1980).
    • (1980) J. Dairy Sci. , vol.63 , pp. 1052
    • Harwalkar, V.R.1
  • 43
    • 0001498924 scopus 로고
    • FTIR examination of thermal denaturation and gel formation in whey proteins
    • D. M. Byler and J. M. Purcell, FTIR examination of thermal denaturation and gel formation in whey proteins, SP1E 1145:415 (1989).
    • (1989) SP1E , vol.1145 , pp. 415
    • Byler, D.M.1    Purcell, J.M.2
  • 44
    • 0000071641 scopus 로고
    • Protein interactions in gels: Protein-protein interactions
    • (N. S. Hettiarachchy and G. R. Ziegler, eds.), Marcel Dekker, New York
    • D. M. Smith. Protein interactions in gels: Protein-protein interactions, Protein Functionality in Food Systems (N. S. Hettiarachchy and G. R. Ziegler, eds.), Marcel Dekker, New York, 1994, p. 209.
    • (1994) Protein Functionality in Food Systems , pp. 209
    • Smith, D.M.1
  • 45
    • 0000453877 scopus 로고
    • Factors affecting molecular characteristics of whey protein gelation
    • J. I. Boye, I. Alii, A. I. Ismail, B. F. Gibbs, and Y. Konishi, Factors affecting molecular characteristics of whey protein gelation, Int. Dairy J. 5:337 (1995).
    • (1995) Int. Dairy J. , vol.5 , pp. 337
    • Boye, J.I.1    Alii, I.2    Ismail, A.I.3    Gibbs, B.F.4    Konishi, Y.5
  • 46
    • 0000874977 scopus 로고
    • Gelation parameters of enzymatically modified soy protein isolates
    • A. Pour-El and T. A. Swenson, Gelation parameters of enzymatically modified soy protein isolates. Cereal Chem. 53:438 (1976).
    • (1976) Cereal Chem , vol.53 , pp. 438
    • Pour-El, A.1    Swenson, T.A.2
  • 47
    • 0009980613 scopus 로고
    • Gelation properties of whey protein and blended protein systems
    • R. H. Schmidt and B. L. Illingworth, Gelation properties of whey protein and blended protein systems, Food Prod. Dev. 12:60 (1978).
    • (1978) Food Prod. Dev. , vol.12 , pp. 60
    • Schmidt, R.H.1    Illingworth, B.L.2
  • 48
    • 0003635465 scopus 로고
    • The effect of neutral salts on the structure and conformational stability of macromolecules in solution
    • (S. N. Timasheff and G. D. Fasman, eds.), Marcel Dekker, New York
    • P. H. von Hippel and T. Schleich, The effect of neutral salts on the structure and conformational stability of macromolecules in solution. Structure and Stability of Biological Macromolecules (S. N. Timasheff and G. D. Fasman, eds.), Marcel Dekker, New York, 1969, p. 417.
    • (1969) Structure and Stability of Biological Macromolecules , pp. 417
    • Von Hippel, P.H.1    Schleich, T.2
  • 49
    • 0020477047 scopus 로고
    • Preferential interactions of proteins with salt in concentrated solutions
    • J. Arakawa and S. N. Timasheff, Preferential interactions of proteins with salt in concentrated solutions, Biochemistry 24:6545 (1982).
    • (1982) Biochemistry , vol.24 , pp. 6545
    • Arakawa, J.1    Timasheff, S.N.2
  • 50
    • 0013807126 scopus 로고
    • On the conformational stability of globular proteins
    • P. H. von Hippel and K. Y. Wong, On the conformational stability of globular proteins, J. Biol. Chem. 240:3909 (1965).
    • (1965) J. Biol. Chem. , vol.240 , pp. 3909
    • Von Hippel, P.H.1    Wong, K.Y.2
  • 51
    • 0001217039 scopus 로고
    • Effect of salt on the thermal stability of storage proteins from faba bean (Vicia faba)
    • S. D. Amtfield, E. D. Murray, and M. A. H. Ismond. Effect of salt on the thermal stability of storage proteins from faba bean (Vicia faba), J. Food Sci. 57:371 (1986).
    • (1986) J. Food Sci , vol.57 , pp. 371
    • Amtfield, S.D.1    Murray, E.D.2    Ismond, M.A.H.3
  • 52
    • 38249041842 scopus 로고
    • The role of non-covalent forces in micelle formation by vicilin from Vicia faba. II. The effect of stabilizing and destabilizing anions on protein interactions
    • M. A. H. Ismond, E. D. Murray, and S. D. Amtfield. The role of non-covalent forces in micelle formation by vicilin from Vicia faba. II. The effect of stabilizing and destabilizing anions on protein interactions, Food Chem. 21:21 (1986).
    • (1986) Food Chem , vol.21 , pp. 21
    • Ismond, M.A.H.1    Murray, E.D.2    Amtfield, S.D.3
  • 53
    • 84985232976 scopus 로고
    • Study of thermal properties of oat globulin by differential scanning calorimetry
    • V. R. Harwalkar and C.-Y. Ma, Study of thermal properties of oat globulin by differential scanning calorimetry, J. Food Sci. 52:396 (1987).
    • (1987) J. Food Sci. , vol.52 , pp. 396
    • Harwalkar, V.R.1    Ma, C.-Y.2
  • 54
    • 84951399968 scopus 로고
    • Differential thermal analysis of milk proteins
    • T. Itoh, Y. Wada, and T. I. Nakanishi, Differential thermal analysis of milk proteins, Agric. Biol. Chem. 40:1083 (1976).
    • (1976) Agric. Biol. Chem. , vol.40 , pp. 1083
    • Itoh, T.1    Wada, Y.2    Nakanishi, T.I.3
  • 55
    • 0015935138 scopus 로고
    • Differential scanning calorimetric study of collagen fibres swollen in aqueous neutral salt solutions
    • A. Finch and D. A. Ledward, Differential scanning calorimetric study of collagen fibres swollen in aqueous neutral salt solutions, Biochim. Biophys. Acta 295:296 (1973).
    • (1973) Biochim. Biophys. Acta , vol.295 , pp. 296
    • Finch, A.1    Ledward, D.A.2
  • 56
    • 0019037397 scopus 로고
    • Carpenter. A comparison of heat induced gel strengths of bovine plasma and egg albumin protein
    • D. W. Hickson, C. W. Dill. R. G. Morgan, D. A. Suter, and Z. L. Carpenter. A comparison of heat induced gel strengths of bovine plasma and egg albumin protein, J. Anim. Sci. 51: 69(1980).
    • (1980) J. Anim. Sci , vol.51 , pp. 69
    • Hickson, D.W.1    Dill, C.W.2    Morgan, R.G.3    Suter, D.A.4
  • 58
    • 0003918425 scopus 로고
    • Protein interactions. An overview
    • (H. Visser, ed.), VCH Publishers, New York
    • M. M. G. Koning and H. Visser, Protein interactions. An overview. Protein Interactions (H. Visser, ed.), VCH Publishers, New York, 1992, p. 1.
    • (1992) Protein Interactions , pp. 1
    • Koning, M.M.G.1    Visser, H.2
  • 60
    • 0016419640 scopus 로고
    • A differential scanning calorimetric study of the stability of egg white to heat denaturation
    • J. W. Donovan, C. J. Mapes, J. G. Davis, and J. A. Garibaldi, A differential scanning calorimetric study of the stability of egg white to heat denaturation, J. Sci. Food Agric. 26: 73(1975).
    • (1975) J. Sci. Food Agric , vol.26 , pp. 73
    • Donovan, J.W.1    Mapes, C.J.2    Davis, J.G.3    Garibaldi, J.A.4
  • 61
    • 0018789680 scopus 로고
    • Increased thermal stability of proteins in the presence of sugars and polyols
    • J. F. Back, D. Oakenfull, and M. B. Smith, Increased thermal stability of proteins in the presence of sugars and polyols. Biochemistry 78:5191 (1979).
    • (1979) Biochemistry , vol.78 , pp. 5191
    • Back, J.F.1    Oakenfull, D.2    Smith, M.B.3
  • 62
    • 0030088058 scopus 로고    scopus 로고
    • Effect of physico-chemical factors on the secondary structure of /3-lactoglobulin
    • J. I. Boye, A. I. Ismail, and I. Alii, Effect of physico-chemical factors on the secondary structure of /3-lactoglobulin. J. Dairy Res. 63:91 (1996).
    • (1996) J. Dairy Res , vol.63 , pp. 91
    • Boye, J.I.1    Ismail, A.I.2    Alii, I.3
  • 63
    • 0000027238 scopus 로고    scopus 로고
    • Interactions involved in the gelation of bovine serum albumin
    • J. I. Boye, I. Alii, and A. I. Ismail, Interactions involved in the gelation of bovine serum albumin. J. Agric. Food Chem. 44:996 (1996).
    • (1996) J. Agric. Food Chem , vol.44 , pp. 996
    • Boye, J.I.1    Alii, I.2    Ismail, A.I.3
  • 64
    • 0001559873 scopus 로고
    • The influence of sugars on the formation of sulfhydryl groups in heat denaturtion and coagulation of egg albumin
    • C. D. Ball, C. R. Hardt, and W. J. Duddles, The influence of sugars on the formation of sulfhydryl groups in heat denaturtion and coagulation of egg albumin, J. Biol. Chem. 151: 163 (1943).
    • (1943) J. Biol. Chem. , vol.151 , pp. 163
    • Ball, C.D.1    Hardt, C.R.2    Duddles, W.J.3
  • 65
    • 0000000643 scopus 로고
    • Nucleic acids, peptides and proteins
    • (F. Franks, ed.), Plenum Press, New York
    • D. Eagland, Nucleic acids, peptides and proteins. Water: A Comprehensive Treatise (F. Franks, ed.), Plenum Press, New York, 1975, p. 305.
    • (1975) Water: A Comprehensive Treatise , pp. 305
    • Eagland, D.1
  • 66
    • 0003092619 scopus 로고
    • Thermal analysis of food proteins in relation to processing effects
    • (V. R. Harwalkar and C.-Y. Ma, eds.), Elsevier Appl. Sci., London
    • S. D. Arntfield, M. A. H. Ismond, and E. D. Murray, Thermal analysis of food proteins in relation to processing effects, Thermal Analysis of Foods (V. R. Harwalkar and C.-Y. Ma, eds.), Elsevier Appl. Sci., London, 1990, p. 51.
    • (1990) Thermal Analysis of Foods , pp. 51
    • Arntfield, S.D.1    Ismond, M.A.H.2    Murray, E.D.3
  • 67
    • 0012976086 scopus 로고
    • The role of noncovalent forces in micelle formation by vicilin from Vicia faba. III. The effect of urea, guanidine hydrochloride and sucrose on protein interactions
    • M. A. H. Ismond, E. D. Murray, and S. D. Arntfield, The role of noncovalent forces in micelle formation by vicilin from Vicia faba. III. The effect of urea, guanidine hydrochloride and sucrose on protein interactions, Food Chem. 29:189 (1988).
    • (1988) Food Chem , vol.29 , pp. 189
    • Ismond, M.A.H.1    Murray, E.D.2    Arntfield, S.D.3
  • 68
    • 0001453945 scopus 로고
    • Effects of medium composition, preheating and chemical modification upon thermal behavior of oat globulin and β-lactglobulin
    • (J. E. Kinsella and W. G. Soucie, eds.), American Oil Chemists Society, Champaign, IL
    • V. R. Harwalkar and C.-Y. Ma, Effects of medium composition, preheating and chemical modification upon thermal behavior of oat globulin and β-lactglobulin, Food Proteins (J. E. Kinsella and W. G. Soucie, eds.), American Oil Chemists Society, Champaign, IL, 1989, p. 219.
    • (1989) Food Proteins , pp. 219
    • Harwalkar, V.R.1    Ma, C.-Y.2
  • 69
    • 0015457797 scopus 로고
    • The effect of polyhydric and monohydric alcohols on the heat-induced reversible dénaturation of lysozyme and ribonucléase
    • S. Y. Gerlsma and E. J. Stuur, The effect of polyhydric and monohydric alcohols on the heat-induced reversible dénaturation of lysozyme and ribonucléase, Int. J. Peptide Protein Res. 4:311 (1972).
    • (1972) Int. J. Peptide Protein Res , vol.4 , pp. 311
    • Gerlsma, S.Y.1    Stuur, E.J.2
  • 70
    • 0019888281 scopus 로고
    • The stabilization of proteins by sucrose
    • J. C. Lee and S. N. Timasheff, The stabilization of proteins by sucrose, J. Biol. Chem. 256: 7193 (1981).
    • (1981) J. Biol. Chem. , vol.256 , pp. 7193
    • Lee, J.C.1    Timasheff, S.N.2
  • 71
    • 0001002352 scopus 로고
    • Conformation changes of proteins
    • R. Lumry and H. Eyring, Conformation changes of proteins, J. Phys. Chem. 58:110 (1954).
    • (1954) J. Phys. Chem. , vol.58 , pp. 110
    • Lumry, R.1    Eyring, H.2
  • 72
    • 84986786289 scopus 로고
    • The protective effect of sodium dodecyl sulfate on the thermal precipitation of conalbumin. A study on thermal aggregation and dénaturation
    • P. O. Hegg, H. Martens, and B. Lôfqvist, The protective effect of sodium dodecyl sulfate on the thermal precipitation of conalbumin. A study on thermal aggregation and dénaturation, J. Sci. Food Agric. 29:245 (1978).
    • (1978) J. Sci. Food Agric. , vol.29 , pp. 245
    • Hegg, P.O.1    Martens, H.2    Lôfqvist, B.3
  • 73
    • 0002677279 scopus 로고
    • Thermostability of β-lactoglobulin as a function of pH and concentration of sodium dodecyl sulfate
    • P. O. Hegg, Thermostability of β-lactoglobulin as a function of pH and concentration of sodium dodecyl sulfate, Acta Agric. Scand. 30:401 (1980).
    • (1980) Acta Agric. Scand. , vol.30 , pp. 401
    • Hegg, P.O.1
  • 74
    • 84987345032 scopus 로고
    • The protective effect of small amounts of anionic detergents on the thermal aggregation of crude ovalbumin
    • P. O. Hegg and B. Lôfqvist, The protective effect of small amounts of anionic detergents on the thermal aggregation of crude ovalbumin, J. Food Sci. 39:1231 (1974).
    • (1974) J. Food Sci. , vol.39 , pp. 1231
    • Hegg, P.O.1    Lôfqvist, B.2
  • 76
    • 0016022523 scopus 로고
    • Hydration of proteins and polypeptides
    • I. D. Kuntz and W. Kauzmann, Hydration of proteins and polypeptides, Adv. Protein Chem. 28:239 (1974).
    • (1974) Adv. Protein Chem , vol.28 , pp. 239
    • Kuntz, I.D.1    Kauzmann, W.2
  • 77
    • 85052714795 scopus 로고
    • Nitrogen solubility of alfafa protein concentrate as influenced by various factors
    • A. A. Betschart, Nitrogen solubility of alfafa protein concentrate as influenced by various factors, J. Food Sci. 38:324 (1973).
    • (1973) J. Food Sci. , vol.38 , pp. 324
    • Betschart, A.A.1
  • 79
    • 0015890980 scopus 로고
    • Solvent perturbation studies and analysis of protein and model compound data in denaturing organic solvents
    • J. N. Solli and T. T. Herskovits, Solvent perturbation studies and analysis of protein and model compound data in denaturing organic solvents. Anal. Biochem. 54:310 (1973).
    • (1973) Anal. Biochem , vol.54 , pp. 310
    • Solli, J.N.1    Herskovits, T.T.2
  • 81
    • 84981611610 scopus 로고
    • The fluorescence of native, denatured and reduced-denatured proteins
    • M. J. Kronman and L. G. Holmes, The fluorescence of native, denatured and reduced-denatured proteins, Photochem. Photobiol. 74:113 (1971).
    • (1971) Photochem. Photobiol. , vol.74 , pp. 113
    • Kronman, M.J.1    Holmes, L.G.2
  • 82
    • 0000079360 scopus 로고
    • Study of thermal dénaturation of oat globulin by ultraviolet and fluorescence spectrophotometry
    • C.-Y. Ma, and V. R. Harwalkar, Study of thermal dénaturation of oat globulin by ultraviolet and fluorescence spectrophotometry, J. Agric. Food Chem. 36:155 (1988).
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 155
    • Ma, C.-Y.1    Harwalkar, V.R.2
  • 84
    • 84986492402 scopus 로고
    • Heat-induced transitions in the protein-protein interaction of bovine natural actomyosin
    • G. R. Ziegler and J. C. Acton, Heat-induced transitions in the protein-protein interaction of bovine natural actomyosin, J. Food Biochem. 8:25 (1984).
    • (1984) J. Food Biochem. , vol.8 , pp. 25
    • Ziegler, G.R.1    Acton, J.C.2
  • 86
    • 0000373478 scopus 로고
    • Infrared spectra and chain conformation of proteins
    • S. Krimm, Infrared spectra and chain conformation of proteins, J. Mol. Biol. 4:528 (1962).
    • (1962) J. Mol. Biol. , vol.4 , pp. 528
    • Krimm, S.1
  • 87
    • 0015438002 scopus 로고
    • Infrared spectroscopy-conformation
    • H. Susi, Infrared spectroscopy-conformation, Meth. Enzymol. 26:455 (1972).
    • (1972) Meth. Enzymol. , vol.26 , pp. 455
    • Susi, H.1
  • 88
    • 0021115861 scopus 로고
    • Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra
    • H. Susi and D. M. Byler, Protein structure by Fourier transform infrared spectroscopy: Second derivative spectra, Biochim. Biophys. Acta 115:391 (1983).
    • (1983) Biochim. Biophys. Acta , vol.115 , pp. 391
    • Susi, H.1    Byler, D.M.2
  • 89
    • 0000642472 scopus 로고
    • Resolution-enhanced Fourier transform infrared spectroscopy of enzymes
    • H. Susi and D. M. Byler, Resolution-enhanced Fourier transform infrared spectroscopy of enzymes, Meth. Enzymol. 130:291 (1986).
    • (1986) Meth. Enzymol. , vol.130 , pp. 291
    • Susi, H.1    Byler, D.M.2
  • 90
    • 0023837785 scopus 로고
    • New insight into protein secondary structure from resolution-enhanced infrared spectra. Review
    • W. K. Surewicz and H. H. Mantsch, New insight into protein secondary structure from resolution-enhanced infrared spectra. Review, Biochim. Biophys. Acta 952:115 (1988).
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 91
    • 0023008334 scopus 로고
    • Vibrational spectroscopy and conformation of potides, polypeptides and proteins
    • S. Krimm and J. Bandekar. Vibrational spectroscopy and conformation of potides, polypeptides and proteins, Adv. Prot. Chem. 3.5:181 (1986).
    • (1986) Adv. Prot. Chem , vol.3 , Issue.5 , pp. 181
    • Krimm, S.1    Bandekar, J.2
  • 92
    • 0023693897 scopus 로고
    • Structural and conformational changes of β-lactoglobulin B: An infrared spectroscopic study of the effect of pH and temperature
    • H. F. Casal. U. Kohler, and H. H. Mantsch, Structural and conformational changes of β-lactoglobulin B: an infrared spectroscopic study of the effect of pH and temperature, Biochim. Biophys. Acta 957:1 1 (1988).
    • (1988) Biochim. Biophys. Acta , vol.957 , Issue.1 , pp. 1
    • Casal, H.F.1    Kohler, U.2    Mantsch, H.H.3
  • 93
    • 0000942193 scopus 로고
    • Jr. Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein
    • D. M. Byler and H. M. Farrell, Jr. Infrared spectroscopic evidence for calcium ion interaction with carboxylate groups of casein, J. Dairy Sci. 72:1719 (1989).
    • (1989) J. Dairy Sci. , vol.72 , pp. 1719
    • Byler, D.M.1    Farrell, H.M.2
  • 94
    • 0024291328 scopus 로고
    • Infrared spectroscopic analysis of salt bridge formation between cytochrome h5 and cytochrome c
    • 5 and cytochrome c, Biochemistry 27:7991 (1988).
    • (1988) Biochemistry , vol.27 , pp. 7991
    • Holloway, P.W.1    Mantsch, H.H.2
  • 95
    • 0026642332 scopus 로고
    • Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy
    • A. A. Ismail, H. H. Mantsch, and P. T. T. Wong, Aggregation of chymotrypsinogen: Portrait by infrared spectroscopy, Biochim. Biophys. Acta 1121:183 (1992).
    • (1992) Biochim. Biophys. Acta , vol.1121 , pp. 183
    • Ismail, A.A.1    Mantsch, H.H.2    Wong, P.T.T.3
  • 96
    • 0024822645 scopus 로고
    • Proteins in whey: Chemical, physical and functional properties
    • J. E. Kinsella, and D. M. Whitehead, Proteins in whey: Chemical, physical and functional properties. Adv. Food Nutr. Res. 33:343 (1989).
    • (1989) Adv. Food Nutr. Res. , vol.33 , pp. 343
    • Kinsella, J.E.1    Whitehead, D.M.2
  • 97
    • 0019536747 scopus 로고
    • Infrared and laser Raman spectroscopic studies of thermally-induced globular proteins gels
    • A. H. Clark, D. H. P. Saunderson, and A. Suggett. Infrared and laser Raman spectroscopic studies of thermally-induced globular proteins gels. Int. J. Pept. Prot. Res. 17:353 (1981).
    • (1981) Int. J. Pept. Prot. Res. , vol.17 , pp. 353
    • Clark, A.H.1    Saunderson, D.H.P.2    Suggett, A.3
  • 98
    • 85052703697 scopus 로고
    • Physical measurements of structure
    • Garland Publishing Inc., New York
    • J. Kyte. Physical measurements of structure, Structure in Protein Chemistry, Garland Publishing Inc., New York, 1995, p. 393.
    • (1995) Structure in Protein Chemistry , pp. 393
    • Kyte, J.1
  • 99
    • 33845279681 scopus 로고
    • Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: Effect on gelation
    • S. Damodaran, Refolding of thermally unfolded soy proteins during the cooling regime of the gelation process: Effect on gelation, J. Agric. Food Chem. 136:262 (1988).
    • (1988) J. Agric. Food Chem , vol.136 , pp. 262
    • Damodaran, S.1
  • 100
    • 24544447317 scopus 로고
    • Heat-induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy
    • H. E. Matsuura and M. C. Manning, Heat-induced gel formation of β-lactoglobulin: A study on the secondary and tertiary structure as followed by circular dichroism spectroscopy, J. Agric. Food Chem. 42:1650 (1994).
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 1650
    • Matsuura, H.E.1    Manning, M.C.2
  • 102
    • 0002762455 scopus 로고
    • Heat-induced changes in the proteins of whey protein concentrate
    • E. Li-Chan. Heat-induced changes in the proteins of whey protein concentrate. J. Food Sci. 48:47(1983).
    • (1983) J. Food Sci , vol.48 , pp. 47
    • Li-Chan, E.1
  • 104
    • 0001345473 scopus 로고
    • Analysis of whey proteins by high performance liquid chromatography
    • R. J. Pearce. Analysis of whey proteins by high performance liquid chromatography, Aust. J. Dairy. Technol. 38:1 14 (1983).
    • (1983) Aust. J. Dairy. Technol. , vol.1 , Issue.14 , pp. 38
    • Pearce, R.J.1
  • 105
    • 0024315816 scopus 로고
    • Application of reversed phase high-performance liquid chromatography to the separation of peptides from phosphorylated and dephosphorylated casein hydrolysates
    • L. Femieux and J. Amiot, Application of reversed phase high-performance liquid chromatography to the separation of peptides from phosphorylated and dephosphorylated casein hydrolysates. J. Chromatog. 473:189 (1989).
    • (1989) J. Chromatog. , vol.473 , pp. 189
    • Femieux, L.1    Amiot, J.2
  • 106
    • 84948513466 scopus 로고
    • Capillary electrophoresis analysis of species variation in the tryptic maps of cytochrom C
    • (J. J. Villafraca. ed.), Academic Press, New York
    • M. P. Young and M. Merion, Capillary electrophoresis analysis of species variation in the tryptic maps of cytochrom C, Current Research in Protein Chemistry: Techniques, Structure and Function (J. J. Villafraca. ed.), Academic Press, New York. 1989, p. 217.
    • (1989) Current Research in Protein Chemistry: Techniques, Structure and Function , pp. 217
    • Young, M.P.1    Merion, M.2
  • 110
    • 0019522169 scopus 로고
    • Confirmation of molecular weight of Aspergillus oryzae a-amylase using the low angle laser light scattering technique in combination with high pressure silica gel chromatography
    • T. Takagi, Confirmation of molecular weight of Aspergillus oryzae a-amylase using the low angle laser light scattering technique in combination with high pressure silica gel chromatography, J. Biochem. 89:363 (1981).
    • (1981) J. Biochem. , vol.89 , pp. 363
    • Takagi, T.1
  • 111
    • 0000502119 scopus 로고
    • Determination of molecular weight of soluble ovalbumin aggregates during heat denaturation using low angle light scattering technique
    • A. Kato, Y. Nagase, N. Matsudomi, and K. Kobayashi, Determination of molecular weight of soluble ovalbumin aggregates during heat denaturation using low angle light scattering technique, Agrie. Biol. Chem. 47:1829 (1983).
    • (1983) Agrie. Biol. Chem. , vol.47 , pp. 1829
    • Kato, A.1    Nagase, Y.2    Matsudomi, N.3    Kobayashi, K.4
  • 112
    • 0003784982 scopus 로고
    • Physicochemical characterization of heat-induced soluble aggregates of bovine globulin
    • S. Hayakawa, Y. Suzuki, R. Nakamura, and Y. Sata, Physicochemical characterization of heat-induced soluble aggregates of bovine globulin. Agrie. Biol. Chem. 47:395 (1983).
    • (1983) Agrie. Biol. Chem. , vol.47 , pp. 395
    • Hayakawa, S.1    Suzuki, Y.2    Nakamura, R.3    Sata, Y.4
  • 114
    • 0015143060 scopus 로고
    • Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribo-nuclease and myoglobin
    • P. L. Privalov, N. N. Khechinashvili, and B. P. Atanaasov, Thermodynamic analysis of thermal transitions in globular proteins. I. Calorimetric study of chymotrypsinogen, ribo-nuclease and myoglobin. Biopolymers 10:1865 (1971).
    • (1971) Biopolymers , vol.10 , pp. 1865
    • Privalov, P.L.1    Khechinashvili, N.N.2    Atanaasov, B.P.3
  • 115
    • 0342421704 scopus 로고
    • Effect of sodium and calcium addition on thermal denaturation of apo-lactalbumin: A differential scanning calorimetry study
    • P. Relkin, B. Launay, and L. Eynard, Effect of sodium and calcium addition on thermal denaturation of apo-lactalbumin: A differential scanning calorimetry study, J. Dairx Sci. 76: 36 (1993).
    • (1993) J. Dairx Sci. , vol.76 , pp. 36
    • Relkin, P.1    Launay, B.2    Eynard, L.3
  • 116
    • 85025543314 scopus 로고
    • Some physico-chemical aspects of protein processing into foodstuffs
    • V. B. Tolstoguzov, Some physico-chemical aspects of protein processing into foodstuffs. Food Hydrocolloids 2:339 (1988).
    • (1988) Food Hydrocolloids , vol.2 , pp. 339
    • Tolstoguzov, V.B.1
  • 119
    • 0007419939 scopus 로고
    • Rheology of fluid foods
    • C. Rha, Rheology of fluid foods, Food Technol. 32(7):77 (1978).
    • (1978) Food Technol , vol.32 , Issue.7 , pp. 77
    • Rha, C.1
  • 120
    • 0002814094 scopus 로고
    • Rheological properties of heat induced β-lactoglobulin gels
    • M. Paulsson, P. Dejmek, and T. Van Vliet, Rheological properties of heat induced β-lactoglobulin gels, J. Dairy Sci. 73:45 (1990).
    • (1990) J. Dairy Sci. , vol.73 , pp. 45
    • Paulsson, M.1    Dejmek, P.2    Van Vliet, T.3
  • 121
    • 38149145844 scopus 로고
    • Muscle protein gelation at low ionic strength
    • A. P. Stone and D. W. Stanley, Muscle protein gelation at low ionic strength. Food Res. Int. 27:155 (1994).
    • (1994) Food Res. Int , vol.27 , pp. 155
    • Stone, A.P.1    Stanley, D.W.2
  • 122
    • 0002666893 scopus 로고
    • Thermal denaturation and aggregation of β-lactoglobulin at pH 2.5. Effect of ionic strength and protein concentration
    • V. R. Harwalkar and M. Kalab, Thermal denaturation and aggregation of β-lactoglobulin at pH 2.5. Effect of ionic strength and protein concentration, Milchwissenschaft 40:31 (1985).
    • (1985) Milchwissenschaft , vol.40 , pp. 31
    • Harwalkar, V.R.1    Kalab, M.2
  • 123
    • 0000017090 scopus 로고
    • Microstructure of isoelectric precipitates from β-lactoglobulin solution heated at various pH values
    • V. R. Harwalkar and M. Kalab, Microstructure of isoelectric precipitates from β-lactoglobulin solution heated at various pH values, Milchwissenschaft 40:665 (1985).
    • (1985) Milchwissenschaft , vol.40 , pp. 665
    • Harwalkar, V.R.1    Kalab, M.2
  • 124
    • 0029373912 scopus 로고
    • Advances in the application of ultrasound in food analysis and processing
    • D. J. McClements, Advances in the application of ultrasound in food analysis and processing, Trends Food Sci. Technol. 6:293 (1995).
    • (1995) Trends Food Sci. Technol. , vol.6 , pp. 293
    • McClements, D.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.