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Volumn 81, Issue 3, 2004, Pages 225-230

Rheological Properties of Sodium Caprate-Induced β-Lactoglobulin Gel and Changes in Secondary Structure During Gelation

Author keywords

Fatty acid salt; FTIR; Gelation; Sodium caprate; lactoglobulin; sheet

Indexed keywords

AGGLOMERATION; DISSOCIATION; FOURIER TRANSFORM INFRARED SPECTROSCOPY; GELATION; GELS; HEAT TREATMENT; PROTEINS; RHEOLOGY; SODIUM COMPOUNDS; VISCOELASTICITY;

EID: 2042504366     PISSN: 0003021X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s11746-004-0886-7     Document Type: Article
Times cited : (6)

References (14)
  • 1
    • 0347037555 scopus 로고
    • Formation of Transparent Gels of Sesame 13S Globulin: Effects of Fatty Acid Salts
    • Yuno-Ohta, N., H. Maeda, M. Okada, and K. Hasegawa, Formation of Transparent Gels of Sesame 13S Globulin: Effects of Fatty Acid Salts, J. Food Sci. 57:86-90 (1992).
    • (1992) J. Food Sci. , vol.57 , pp. 86-90
    • Yuno-Ohta, N.1    Maeda, H.2    Okada, M.3    Hasegawa, K.4
  • 2
    • 0542364404 scopus 로고
    • Relationship Between the Functional Properties and Microstructure of Food Protein Gel: Effects of Fatty Acid Salts
    • edited by K. Nishinari and E. Doi, Plenum Press, New York
    • Yuno-Ohta, N., H. Ohta, H. Maeda, M. Okada, and K. Hasegawa, Relationship Between the Functional Properties and Microstructure of Food Protein Gel: Effects of Fatty Acid Salts, in Food Hydrocolloids: Structures, Properties, and Functions, edited by K. Nishinari and E. Doi, Plenum Press, New York, 1994, pp. 371-374.
    • (1994) Food Hydrocolloids: Structures, Properties, and Functions , pp. 371-374
    • Yuno-Ohta, N.1    Ohta, H.2    Maeda, H.3    Okada, M.4    Hasegawa, K.5
  • 3
    • 10544256186 scopus 로고    scopus 로고
    • Gelation Properties of Ovalbumin as Affected by Fatty Acid Salts
    • Yuno-Ohta, N., H. Toryu, T. Higasa, H. Maeda, M. Okada, and H. Ohta, Gelation Properties of Ovalbumin as Affected by Fatty Acid Salts, J. Food Sci. 61:906-910, 920 (1996).
    • (1996) J. Food Sci. , vol.61 , pp. 906-910
    • Yuno-Ohta, N.1    Toryu, H.2    Higasa, T.3    Maeda, H.4    Okada, M.5    Ohta, H.6
  • 4
    • 0013147617 scopus 로고    scopus 로고
    • Formation of Fatty Acid Salt-Induced Gel of Ovalbumin and the Mechanism for Gelation
    • Yuno-Ohta, N., T. Higasa, E. Tatsumi, H. Sakurai, R. Asano, and M. Hirose, Formation of Fatty Acid Salt-Induced Gel of Ovalbumin and the Mechanism for Gelation, J. Agric. Food Chem. 46:4518-4523 (1998).
    • (1998) J. Agric. Food Chem. , vol.46 , pp. 4518-4523
    • Yuno-Ohta, N.1    Higasa, T.2    Tatsumi, E.3    Sakurai, H.4    Asano, R.5    Hirose, M.6
  • 5
    • 84987260295 scopus 로고
    • Gelation of β-Lactglobulin: Effects of Sodium Chloride and Calcium Chloride on the Rheological and Structural Properties of Gels
    • Mulvihill, D.M., and J.E. Kinsella, Gelation of β-Lactglobulin: Effects of Sodium Chloride and Calcium Chloride on the Rheological and Structural Properties of Gels, J. Food Sci. 53:231-236 (1988).
    • (1988) J. Food Sci. , vol.53 , pp. 231-236
    • Mulvihill, D.M.1    Kinsella, J.E.2
  • 6
    • 0024815231 scopus 로고
    • Interaction of Fatty Acids with β-Lactoglobulin and Albumin from Ruminant Milk
    • Perez, M.D., C. Daiz de Villegas, L. Sanchez, P. Aranda, J.M. Ena, and M. Calvo, Interaction of Fatty Acids with β-Lactoglobulin and Albumin from Ruminant Milk, J. Biochem. 106:1094-1097 (1989).
    • (1989) J. Biochem. , vol.106 , pp. 1094-1097
    • Perez, M.D.1    Daiz de Villegas, C.2    Sanchez, L.3    Aranda, P.4    Ena, J.M.5    Calvo, M.6
  • 7
    • 0032003930 scopus 로고    scopus 로고
    • Effect of the Binding of Palmitic Acid to β-Lactoglobulin on Its Gelation Properties
    • Puyol, P., M.D. Perez, J. Burgos, and M. Calvo, Effect of the Binding of Palmitic Acid to β-Lactoglobulin on Its Gelation Properties, Int. Dairy J. 8:119-123 (1998).
    • (1998) Int. Dairy J. , vol.8 , pp. 119-123
    • Puyol, P.1    Perez, M.D.2    Burgos, J.3    Calvo, M.4
  • 8
    • 0017172023 scopus 로고
    • Raman Spectroscopic Study of the Proteins of Egg White
    • Painter, P.C., and J.L. Koenig, Raman Spectroscopic Study of the Proteins of Egg White, Biopolymers 15:2155-2166 (1976).
    • (1976) Biopolymers , vol.15 , pp. 2155-2166
    • Painter, P.C.1    Koenig, J.L.2
  • 9
    • 0022691315 scopus 로고
    • Examination of the Secondary Structure of Protein by Deconvolved FTIR Spectra
    • Byler, D.M., and H. Susi, Examination of the Secondary Structure of Protein by Deconvolved FTIR Spectra, Biopolymers 25:469-487 (1986).
    • (1986) Biopolymers , vol.25 , pp. 469-487
    • Byler, D.M.1    Susi, H.2
  • 10
    • 0023837785 scopus 로고
    • New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra
    • Surewicz, W.K., and H.H. Mantsch, New Insight into Protein Secondary Structure from Resolution-Enhanced Infrared Spectra, Biochim. Biophys. Acta 952:115-130 (1988).
    • (1988) Biochim. Biophys. Acta , vol.952 , pp. 115-130
    • Surewicz, W.K.1    Mantsch, H.H.2
  • 11
    • 0030088058 scopus 로고    scopus 로고
    • Effect of Physicochemical Factors on the Secondary Structure of β-Lactoglobulin
    • Boye, J.I., A.A. Ismail, and I. Alli, Effect of Physicochemical Factors on the Secondary Structure of β-Lactoglobulin, J. Dairy Res. 63:97-109 (1996).
    • (1996) J. Dairy Res. , vol.63 , pp. 97-109
    • Boye, J.I.1    Ismail, A.A.2    Alli, I.3
  • 12
    • 0038761793 scopus 로고    scopus 로고
    • Structural and Interaction Properties of β-Lactoglobulin as Studied by FTIR Spectroscopy
    • Lefevre, T., and M. Subirade, Structural and Interaction Properties of β-Lactoglobulin as Studied by FTIR Spectroscopy, Int. J. Food Sci. Technol. 34:419-428 (1999).
    • (1999) Int. J. Food Sci. Technol. , vol.34 , pp. 419-428
    • Lefevre, T.1    Subirade, M.2
  • 13
    • 0028290324 scopus 로고
    • Reversible and Irreversible Modifications of β-Lactoglobulin upon Exposure to Heat
    • Cairoli, S., S. Iametti, and F. Bonomi, Reversible and Irreversible Modifications of β-Lactoglobulin upon Exposure to Heat, J. Protein Chem. 13:547-554 (1994).
    • (1994) J. Protein Chem. , vol.13 , pp. 547-554
    • Cairoli, S.1    Iametti, S.2    Bonomi, F.3
  • 14
    • 0028985708 scopus 로고
    • Thermal Denaturation of β-Lactoglobulin: Effect of Protein Concentration at pH 6.75 and 8.05
    • Qi, X.L., S. Brownlow, C. Holt, and P. Sellers, Thermal Denaturation of β-Lactoglobulin: Effect of Protein Concentration at pH 6.75 and 8.05, Biochim. Biophys. Acta 1248:43-49 (1995).
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 43-49
    • Qi, X.L.1    Brownlow, S.2    Holt, C.3    Sellers, P.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.