메뉴 건너뛰기




Volumn 44, Issue 12, 1996, Pages 3793-3798

Analysis of Structural Properties and Immunochemical Reactivity of Heat-Treated Ovalbumin

Author keywords

Denaturation; Heat treatment; Immunochemical reactivity; Ovalbumin

Indexed keywords


EID: 0001265611     PISSN: 00218561     EISSN: None     Source Type: Journal    
DOI: 10.1021/jf950470q     Document Type: Article
Times cited : (31)

References (42)
  • 1
    • 0000401058 scopus 로고
    • Role of disulfide bonds in determining rheological and microstructural properties of heat-induced protein networks from ovalbumin and vicilin
    • Arntfield, S.; Murray, D.; Ismond, M. A. H. Role of disulfide bonds in determining rheological and microstructural properties of heat-induced protein networks from ovalbumin and vicilin. J. Agric. Food Chem. 1991, 39, 1378-1385.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 1378-1385
    • Arntfield, S.1    Murray, D.2    Ismond, M.A.H.3
  • 2
    • 85032119438 scopus 로고
    • Determinations of SH and SS groups in some food proteins using Ellman's reagent
    • Beveridge, A.; Toma, S. J.; Nakai, S. Determinations of SH and SS groups in some food proteins using Ellman's reagent. J. Food Sci. 1970, 39, 49-51.
    • (1970) J. Food Sci. , vol.39 , pp. 49-51
    • Beveridge, A.1    Toma, S.J.2    Nakai, S.3
  • 3
    • 0027954096 scopus 로고
    • Thermal stability of a neutral protease of Aspergillus oryzae
    • Bombara, N.; Pilosof, A. M. R.; Añón, M. C. Thermal stability of a neutral protease of Aspergillus oryzae. J. Food Biochem. 1994, 18, 31-41.
    • (1994) J. Food Biochem. , vol.18 , pp. 31-41
    • Bombara, N.1    Pilosof, A.M.R.2    Añón, M.C.3
  • 4
    • 84987343882 scopus 로고
    • Immunochemical properties of native and heat denatured ovalbumin
    • Breton, C.; Phan Thanh; Paraf, A. Immunochemical properties of native and heat denatured ovalbumin. J. Food Sci. 1988, 53, 222-225.
    • (1988) J. Food Sci. , vol.53 , pp. 222-225
    • Breton, C.1    Phan Thanh2    Paraf, A.3
  • 5
    • 84987299275 scopus 로고
    • Immunochemical identification and quantification of ovalbumin additive in canned mushrooms
    • Breton, C.; Phan Thanh; Paraf, A. Immunochemical identification and quantification of ovalbumin additive in canned mushrooms. J. Food Sci. 1988, 53, 226-230.
    • (1988) J. Food Sci. , vol.53 , pp. 226-230
    • Breton, C.1    Phan Thanh2    Paraf, A.3
  • 7
    • 0001340043 scopus 로고
    • Optimization of a competitive ELISA with polyclonal antibodies for quantification of prolamins in food
    • Chirdo, F. G.; Añón, M. C.; Fossat, C. A. Optimization of a competitive ELISA with polyclonal antibodies for quantification of prolamins in food. Food Agric. Immunol. 1995, 7, 333-343.
    • (1995) Food Agric. Immunol. , vol.7 , pp. 333-343
    • Chirdo, F.G.1    Añón, M.C.2    Fossat, C.A.3
  • 8
    • 0003144164 scopus 로고
    • Selective cyanilation of sulfhydryl groups II. On the synthesis of 2-nitro-5-thiocyanobenzoic acid
    • Degani, Y.; Patchornik, A. Selective cyanilation of sulfhydryl groups II. On the synthesis of 2-nitro-5-thiocyanobenzoic acid. J. Org. Chem. 1971, 36, 2727-2728.
    • (1971) J. Org. Chem. , vol.36 , pp. 2727-2728
    • Degani, Y.1    Patchornik, A.2
  • 9
    • 0003323578 scopus 로고
    • Relationship of SH groups to functionality of ovalbumin
    • Kinsella, J. E., Soucie, W. G., Eds.; AOCS: Champaign, IL
    • Doi, E.; Kitabatake, N.; Hatta, H.; Koseki, T. Relationship of SH groups to functionality of ovalbumin. In Food Proteins; Kinsella, J. E., Soucie, W. G., Eds.; AOCS: Champaign, IL, 1989.
    • (1989) Food Proteins
    • Doi, E.1    Kitabatake, N.2    Hatta, H.3    Koseki, T.4
  • 10
    • 0023601497 scopus 로고
    • Effects of limited proteolysis on functionality of ovalbumin
    • Doi, E.; Koseki, T.; Kitabatake, N. Effects of limited proteolysis on functionality of ovalbumin. J. Am. Oil Chem. Soc. 1987, 64, 1697-1703.
    • (1987) J. Am. Oil Chem. Soc. , vol.64 , pp. 1697-1703
    • Doi, E.1    Koseki, T.2    Kitabatake, N.3
  • 11
    • 0016923455 scopus 로고
    • A differential scanning calorimetric study of conversion of ovalbumin to S-ovalbumin in eggs
    • Donovan, J.; Mapes, C. A differential scanning calorimetric study of conversion of ovalbumin to S-ovalbumin in eggs. J. Sci. Food Agric. 1976, 27, 197-204.
    • (1976) J. Sci. Food Agric. , vol.27 , pp. 197-204
    • Donovan, J.1    Mapes, C.2
  • 12
  • 13
    • 0012716869 scopus 로고
    • On the effect of the denaturation degree of food proteins on their functional properties
    • Schwenke, K. D., Mothes, R., Eds.; VCH: Weinheim
    • Grinberg, V. Y.; Burova, T. V.; Grinberg, N. V.; Mashkeivich, A. Y. On the effect of the denaturation degree of food proteins on their functional properties. In Food Proteins. Structure and Functionality; Schwenke, K. D., Mothes, R., Eds.; VCH: Weinheim, 1993.
    • (1993) Food Proteins. Structure and Functionality
    • Grinberg, V.Y.1    Burova, T.V.2    Grinberg, N.V.3    Mashkeivich, A.Y.4
  • 14
    • 0001221912 scopus 로고
    • Contribution of the hydrophobycity, net charge and sulfhydryl groups to thermal properties of ovalbumin
    • Hayakawa, S.; Nakai, S. Contribution of the hydrophobycity, net charge and sulfhydryl groups to thermal properties of ovalbumin. Can. Inst. Food Sci. Technol. J. 1985, 18, 290-295.
    • (1985) Can. Inst. Food Sci. Technol. J. , vol.18 , pp. 290-295
    • Hayakawa, S.1    Nakai, S.2
  • 15
    • 84986747311 scopus 로고
    • Effects of pH and neutral salts on th formation and quality of thermal aggregates of ovalbumin. A study on thermal aggregation and denaturation
    • Hegg, P.; Martens, H.; Löfqvist, B. Effects of pH and neutral salts on th formation and quality of thermal aggregates of ovalbumin. A study on thermal aggregation and denaturation. J. Sci. Food Agric. 1979, 30, 981-993.
    • (1979) J. Sci. Food Agric. , vol.30 , pp. 981-993
    • Hegg, P.1    Martens, H.2    Löfqvist, B.3
  • 16
    • 0000528731 scopus 로고
    • Lysozymes in eggs and plasma from chicken, duck and goose: Choice and use of mAbs to detect adulterants in "foie gras"
    • Hemmen, F.; Paraf, A.; Smith-Gill, S. Lysozymes in eggs and plasma from chicken, duck and goose: choice and use of mAbs to detect adulterants in "foie gras". J. Food Sci. 1993, 58, 1291-1299.
    • (1993) J. Food Sci. , vol.58 , pp. 1291-1299
    • Hemmen, F.1    Paraf, A.2    Smith-Gill, S.3
  • 17
    • 0001232044 scopus 로고
    • Reactions of food proteins during processing and storage and their nutritional consequences
    • Hudson, B. J. F., Ed.; Elsevier Applied Science: Essex, U.K.
    • Hurrel, R. F. Reactions of food proteins during processing and storage and their nutritional consequences. In Developments in Food Proteins-3. Hudson, B. J. F., Ed.; Elsevier Applied Science: Essex, U.K., 1984.
    • (1984) Developments in Food Proteins , vol.3
    • Hurrel, R.F.1
  • 18
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescent probe method and its correlation with surface properties of proteins
    • Kato, A.; Nakai, S. Hydrophobicity determined by a fluorescent probe method and its correlation with surface properties of proteins. Biochim. Biophys. Acta 1980, 624, 13-20.
    • (1980) Biochim. Biophys. Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 19
    • 84954875344 scopus 로고
    • Effects of partial denaturation on surface properties of ovalbumin and lysozyme
    • Kato, A.; Tsutsui, N.; Kobayashi, K.; Nakai, S. Effects of partial denaturation on surface properties of ovalbumin and lysozyme. Agric. Biol. Chem. 1981, 45, 2755-2760.
    • (1981) Agric. Biol. Chem. , vol.45 , pp. 2755-2760
    • Kato, A.1    Tsutsui, N.2    Kobayashi, K.3    Nakai, S.4
  • 20
    • 0000758433 scopus 로고
    • Estimation of the molecular weight distribution of heat induced ovalbumin aggregates by the low angle laser light scattering technique combined with high performance gel chromatography
    • Kato, A.; Takagi, T. Estimation of the molecular weight distribution of heat induced ovalbumin aggregates by the low angle laser light scattering technique combined with high performance gel chromatography. J. Agric. Food Sci. 1987, 35, 633-637.
    • (1987) J. Agric. Food Sci. , vol.35 , pp. 633-637
    • Kato, A.1    Takagi, T.2
  • 21
    • 0001109729 scopus 로고
    • Formation of intermolecular beta sheet structure during heat denaturation of ovalbumin
    • Kato, A.; Takagi, T. Formation of intermolecular beta sheet structure during heat denaturation of ovalbumin. J. Agric. Food Chem. 1988, 36, 1156-1159.
    • (1988) J. Agric. Food Chem. , vol.36 , pp. 1156-1159
    • Kato, A.1    Takagi, T.2
  • 22
  • 23
    • 0023972819 scopus 로고
    • Conformational changes in ovalbumin at acid pH
    • Koseki, T.; Kitabatake, N.; Doi, E. Conformational changes in ovalbumin at acid pH. J. Biochem. 1988, 103, 425-430.
    • (1988) J. Biochem. , vol.103 , pp. 425-430
    • Koseki, T.1    Kitabatake, N.2    Doi, E.3
  • 25
    • 0001759849 scopus 로고
    • Surface hydrophobicity and aggregation of beta lactoglobulin heated at neutral pH
    • Lalignat, A.; Dumay, E.; Valencia, C.; Cheftel, J. C. Surface hydrophobicity and aggregation of beta lactoglobulin heated at neutral pH. J. Agric. Food Chem. 1991, 39, 2147-2155.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 2147-2155
    • Lalignat, A.1    Dumay, E.2    Valencia, C.3    Cheftel, J.C.4
  • 26
    • 0019984788 scopus 로고
    • Clinical and immunological study of allergy to hens egg white. Antigens in hens egg white studied by crossed immunoelectrophoresis
    • Langland, T. A. Clinical and immunological study of allergy to hens egg white. Antigens in hens egg white studied by crossed immunoelectrophoresis. Allergy 1982, 37, 323.
    • (1982) Allergy , vol.37 , pp. 323
    • Langland, T.A.1
  • 27
    • 0345606736 scopus 로고
    • Denaturation of wheat germ protein during drying
    • Lupanc, C. E.; Añón, M. C. Denaturation of wheat germ protein during drying. Cereal Chem. 1986, 63, 259-262.
    • (1986) Cereal Chem. , vol.63 , pp. 259-262
    • Lupanc, C.E.1    Añón, M.C.2
  • 28
    • 0000015429 scopus 로고
    • Emulsifying and structural properties of ovalbumin
    • Mine, Y.; Noutomi, T.; Haga, N. Emulsifying and structural properties of ovalbumin. J. Agric. Food Chem. 1991, 39, 443-446.
    • (1991) J. Agric. Food Chem. , vol.39 , pp. 443-446
    • Mine, Y.1    Noutomi, T.2    Haga, N.3
  • 29
    • 0005386010 scopus 로고
    • Effects of heating on protein functionality
    • Dixon Philips, R., Finley, J. W., Eds.; Marcel Dekker: New York
    • Nakai, S.; Li-Chan, E. Effects of heating on protein functionality. In Protein Quality and the Effects of Processing; Dixon Philips, R., Finley, J. W., Eds.; Marcel Dekker: New York, 1989.
    • (1989) Protein Quality and the Effects of Processing
    • Nakai, S.1    Li-Chan, E.2
  • 30
    • 0000373062 scopus 로고
    • Factors contributing to the heat induced aggregation of ovalbumin
    • Nakamura, R.; Sugiyama, H.; Sato, Y. Factors contributing to the heat induced aggregation of ovalbumin. Agric. Biol. Chem. 1978, 42, 819-824.
    • (1978) Agric. Biol. Chem. , vol.42 , pp. 819-824
    • Nakamura, R.1    Sugiyama, H.2    Sato, Y.3
  • 31
    • 0039863427 scopus 로고
    • Structural changes and metabolism of proteins following heat denaturation
    • Cherry, J. P., Ed.; ACS Symposium Series 206; American Chemical Society: Washington, DC
    • Neucere, J. N.; Cherry, J. P. Structural changes and metabolism of proteins following heat denaturation. In Food Protein Deterioration. Mechanisms and Functionality; Cherry, J. P., Ed.; ACS Symposium Series 206; American Chemical Society: Washington, DC, 1982.
    • (1982) Food Protein Deterioration. Mechanisms and Functionality
    • Neucere, J.N.1    Cherry, J.P.2
  • 32
    • 0014895111 scopus 로고
    • Kinetic analysis of derivative curves in thermal analysis
    • Ozawa, T. Kinetic analysis of derivative curves in thermal analysis. J. Thermal Anal. 1970, 2, 301.
    • (1970) J. Thermal Anal. , vol.2 , pp. 301
    • Ozawa, T.1
  • 33
    • 0001289346 scopus 로고
    • Effect of thermal and proteolytic processing on glycinin, the 11S globulin of soy (Glicine max): A study utilizing monoclonal and polyclonal antibodies
    • Plumb, G. W.; Mills, E. N. C.; Tatton, U.; D'ursel, C. C. M.; Lambert, N.; Morgan, M. R. A. Effect of thermal and proteolytic processing on glycinin, the 11S globulin of soy (Glicine max): a study utilizing monoclonal and polyclonal antibodies. J. Agric. Food Chem. 1994, 42, 834-840.
    • (1994) J. Agric. Food Chem. , vol.42 , pp. 834-840
    • Plumb, G.W.1    Mills, E.N.C.2    Tatton, U.3    D'ursel, C.C.M.4    Lambert, N.5    Morgan, M.R.A.6
  • 34
    • 0018416496 scopus 로고
    • Ellman's reagent 5,5′-dithiobis(2-nitrobenzoic) acid-a reexamination
    • Riddles, P.; Berkeley, R.; Zerner, B. Ellman's reagent 5,5′-dithiobis(2-nitrobenzoic) acid-a reexamination. Anal. Biochem. 1979, 94, 75-81.
    • (1979) Anal. Biochem. , vol.94 , pp. 75-81
    • Riddles, P.1    Berkeley, R.2    Zerner, B.3
  • 35
    • 84987368819 scopus 로고
    • Thermal denaturation of hen egg white studied by chromatographic and immunochemical techniques
    • Sajdok, J.; Pozárková, D.; Rauch, P.; Kás, J. Thermal denaturation of hen egg white studied by chromatographic and immunochemical techniques. J. Food Sci. 1989, 54, 906-908.
    • (1989) J. Food Sci. , vol.54 , pp. 906-908
    • Sajdok, J.1    Pozárková, D.2    Rauch, P.3    Kás, J.4
  • 36
    • 0000393823 scopus 로고
    • Monoclonal antibody sandwich enzymeimmune assays for determination of gluten in foods
    • Skerrit, J. H.; Hill, A. S. Monoclonal antibody sandwich enzymeimmune assays for determination of gluten in foods. J. Agric. Food Chem. 1990, 38, 1771-1778.
    • (1990) J. Agric. Food Chem. , vol.38 , pp. 1771-1778
    • Skerrit, J.H.1    Hill, A.S.2
  • 37
    • 0038272798 scopus 로고
    • Polyclonal antisera against unheated and heated common wheat specific gamma and omega gliadins for detection of adulteration of Durum wheat and Durum wheat products with common wheats
    • Stevenson, A.; McCarthy, P. K.; Griffin, M. Polyclonal antisera against unheated and heated common wheat specific gamma and omega gliadins for detection of adulteration of Durum wheat and Durum wheat products with common wheats. Food Agric. Immunol. 1994, 6, 435-442.
    • (1994) Food Agric. Immunol. , vol.6 , pp. 435-442
    • Stevenson, A.1    McCarthy, P.K.2    Griffin, M.3
  • 38
    • 0026718498 scopus 로고
    • Dependence of reaction rate of 5,5′-dithiobis(2-nitrobenzoic) acid to free sulfhydryl groups of bovine serum albumin and ovalbumin on the protein conformations
    • Takeda, K.; Shigemura, A.; Hamada, S.; Gu, W.; Fang, D.; Sasa, K.; Hachiya, K. Dependence of reaction rate of 5,5′-dithiobis(2-nitrobenzoic) acid to free sulfhydryl groups of bovine serum albumin and ovalbumin on the protein conformations. J. Protein Chem. 1992, 11, 187-192.
    • (1992) J. Protein Chem. , vol.11 , pp. 187-192
    • Takeda, K.1    Shigemura, A.2    Hamada, S.3    Gu, W.4    Fang, D.5    Sasa, K.6    Hachiya, K.7
  • 39
    • 84986849824 scopus 로고
    • Use of specific polyclonal antibodies to detect heat treatment of ovalbumin in mushrooms
    • Varshney, G.; Paraf, A. Use of specific polyclonal antibodies to detect heat treatment of ovalbumin in mushrooms. J. Sci. Food Agric. 1990, 52, 261-274.
    • (1990) J. Sci. Food Agric. , vol.52 , pp. 261-274
    • Varshney, G.1    Paraf, A.2
  • 40
    • 84985233013 scopus 로고
    • Structure of native and heat-denatured ovalbumin as revealed by monoclonal antibodies: Epitopic changes during heat treatment
    • Varshney, G. C.; Mahana, W.; Filloux, A. M.; Venien, A.; Paraf, A. Structure of native and heat-denatured ovalbumin as revealed by monoclonal antibodies: epitopic changes during heat treatment. J. Food Sci. 1991, 56 (1), 224-233.
    • (1991) J. Food Sci. , vol.56 , Issue.1 , pp. 224-233
    • Varshney, G.C.1    Mahana, W.2    Filloux, A.M.3    Venien, A.4    Paraf, A.5
  • 41
    • 84987300697 scopus 로고
    • Denaturation kinetics of myofibrillar proteins in bovine muscle
    • Wagner, J. R.; Añón, M. C. Denaturation kinetics of myofibrillar proteins in bovine muscle. J. Food Technol. 1985, 20, 1547-1550, 1563.
    • (1985) J. Food Technol. , vol.20 , pp. 1547-1550
    • Wagner, J.R.1    Añón, M.C.2
  • 42
    • 0014868899 scopus 로고
    • Passive hemaglutination. II-Titration of antibody against dererminants unique for aggregated denatured bovine serum albumin and further studies on gelatin
    • Wolberg, G.; Liu, C. T.; Adler, F. L. Passive hemaglutination. II-Titration of antibody against dererminants unique for aggregated denatured bovine serum albumin and further studies on gelatin. J. Immunol. 1970, 105, 797-801.
    • (1970) J. Immunol. , vol.105 , pp. 797-801
    • Wolberg, G.1    Liu, C.T.2    Adler, F.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.