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Volumn 40, Issue 7, 2007, Pages 1167-1175

Effects of pulsed electric fields on physicochemical properties of soybean protein isolates

Author keywords

Physicochemical properties; Protein aggregation; Protein structure; Pulsed electric fields; Soybean protein isolates

Indexed keywords

ELECTRIC FIELD EFFECTS; PROTEINS;

EID: 34247211578     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2006.08.015     Document Type: Article
Times cited : (179)

References (35)
  • 4
    • 85032119438 scopus 로고
    • Determination of SH- and SS-groups in some food proteins using Ellman's reagent
    • Beveridge T., Toma S.J., and Nakai S. Determination of SH- and SS-groups in some food proteins using Ellman's reagent. Journal of Food Science 39 (1974) 49-51
    • (1974) Journal of Food Science , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.3
  • 6
    • 0001190763 scopus 로고    scopus 로고
    • High-pressure promotes β-lactoglobulin aggregation through SH/S-S interchange reactions
    • Funtenberger S., Dumay E., and Cheftel J.C. High-pressure promotes β-lactoglobulin aggregation through SH/S-S interchange reactions. Journal of Agricultural and Food Chemistry 45 (1997) 912-921
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 912-921
    • Funtenberger, S.1    Dumay, E.2    Cheftel, J.C.3
  • 7
    • 84985200365 scopus 로고
    • Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins
    • Hayakawa S., and Nakai S. Relationships of hydrophobicity and net charge to the solubility of milk and soy proteins. Journal of Food Science 50 (1985) 486-491
    • (1985) Journal of Food Science , vol.50 , pp. 486-491
    • Hayakawa, S.1    Nakai, S.2
  • 8
    • 12344322894 scopus 로고    scopus 로고
    • Properties of soy protein isolate prepared from aqueous alcohol washed soy flakes
    • Hua Y.F., Huang Y.R., Qiu A.Y., and Liu X.Y. Properties of soy protein isolate prepared from aqueous alcohol washed soy flakes. Food Research International 38 (2005) 273-279
    • (2005) Food Research International , vol.38 , pp. 273-279
    • Hua, Y.F.1    Huang, Y.R.2    Qiu, A.Y.3    Liu, X.Y.4
  • 9
    • 0033486337 scopus 로고    scopus 로고
    • High intensity pulsed electric fields applied to egg white: Effect on salmonella enteritidis inactivation and protein denaturation
    • Jeantet R., Baron F., Nau F., Roignant M., and Brule G. High intensity pulsed electric fields applied to egg white: Effect on salmonella enteritidis inactivation and protein denaturation. Journal of Food Protection 62 12 (1999) 1381-1386
    • (1999) Journal of Food Protection , vol.62 , Issue.12 , pp. 1381-1386
    • Jeantet, R.1    Baron, F.2    Nau, F.3    Roignant, M.4    Brule, G.5
  • 11
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe methods and its correlation with surface properties of proteins
    • Kato A., and Nakai S. Hydrophobicity determined by a fluorescence probe methods and its correlation with surface properties of proteins. Biochimica et Biophysica Acta 624 (1980) 13-20
    • (1980) Biochimica et Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 12
    • 13244259221 scopus 로고    scopus 로고
    • Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G
    • Li S.Q., Bomser A.B., and Zhang Q.H. Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G. Journal of Agricultural and Food Chemistry 53 (2005) 663-670
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 663-670
    • Li, S.Q.1    Bomser, A.B.2    Zhang, Q.H.3
  • 15
    • 0038528531 scopus 로고    scopus 로고
    • Commercial-scale pulsed electric field processing of orange juice
    • Min S., Jin Z.T., Min S.K., Yeom H., and Zhang Q.H. Commercial-scale pulsed electric field processing of orange juice. Journal of Food Science 68 (2003) 1265-1271
    • (2003) Journal of Food Science , vol.68 , pp. 1265-1271
    • Min, S.1    Jin, Z.T.2    Min, S.K.3    Yeom, H.4    Zhang, Q.H.5
  • 17
    • 0035021485 scopus 로고    scopus 로고
    • Emulsifying properties of high-pressure soy protein isolates and 7S and 11S globulins
    • Molina E., Papadopoulou A., and Ledward D.A. Emulsifying properties of high-pressure soy protein isolates and 7S and 11S globulins. Food Hydrocolloids 15 (2001) 263-269
    • (2001) Food Hydrocolloids , vol.15 , pp. 263-269
    • Molina, E.1    Papadopoulou, A.2    Ledward, D.A.3
  • 18
    • 33845550183 scopus 로고
    • Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity
    • Nakai S. Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. Journal of Agricultural and Food Chemistry 31 (1983) 676-683
    • (1983) Journal of Agricultural and Food Chemistry , vol.31 , pp. 676-683
    • Nakai, S.1
  • 19
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: Evaluation of a turbidimetric technique
    • Pearce K.N., and Kinsella J.E. Emulsifying properties of proteins: Evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 26 (1978) 716-723
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 20
    • 0742288323 scopus 로고    scopus 로고
    • Pulsed electric fields on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
    • Perez O.E., and Pilosof A.M.R. Pulsed electric fields on the molecular structure and gelation of β-lactoglobulin concentrate and egg white. Food Research International 37 (2004) 102-110
    • (2004) Food Research International , vol.37 , pp. 102-110
    • Perez, O.E.1    Pilosof, A.M.R.2
  • 21
    • 84907421519 scopus 로고
    • Relationship between the method of obtention and the structural and functional properties of soy protein isolates. 2. Surface properties
    • Petruccelli S., and Anon. Relationship between the method of obtention and the structural and functional properties of soy protein isolates. 2. Surface properties. Journal of Agricultural and Food Chemistry 42 (1994) 2170-2176
    • (1994) Journal of Agricultural and Food Chemistry , vol.42 , pp. 2170-2176
    • Petruccelli, S.1
  • 23
    • 0345320385 scopus 로고    scopus 로고
    • Soybean protein dispersions at acidic pH. Thermal and rheological behavior
    • Puppo M.C., and Anon. Soybean protein dispersions at acidic pH. Thermal and rheological behavior. Journal of Food Science 64 (1999) 50-56
    • (1999) Journal of Food Science , vol.64 , pp. 50-56
    • Puppo, M.C.1
  • 24
    • 84907421742 scopus 로고
    • Gelation of soybean protein isolates on acidic condition. Effect of pH and protein concentration
    • Puppo M.C., Lupano C.E., and Anon. Gelation of soybean protein isolates on acidic condition. Effect of pH and protein concentration. Journal of Agricultural and Food Chemistry 43 (1995) 2353-2361
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2353-2361
    • Puppo, M.C.1    Lupano, C.E.2
  • 25
    • 0000681416 scopus 로고
    • Pulsed electric fields treatment chamber design for liquid food pasteurisation using a finite element method
    • Qin B., Zhang Q., Barbosa-Canovas G.V., Swanson B.G., and Pedrow P.D. Pulsed electric fields treatment chamber design for liquid food pasteurisation using a finite element method. Transactions of ASAE 38 2 (1995) 557-565
    • (1995) Transactions of ASAE , vol.38 , Issue.2 , pp. 557-565
    • Qin, B.1    Zhang, Q.2    Barbosa-Canovas, G.V.3    Swanson, B.G.4    Pedrow, P.D.5
  • 26
    • 84907421527 scopus 로고
    • Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions
    • Sorgentini D.A., Wagner J.R., and Anon. Effects of thermal treatment of soy protein isolate on the characteristics and structure-function relationship of soluble and insoluble fractions. Journal of Agricultural and Food Chemistry 43 (1995) 2471-2479
    • (1995) Journal of Agricultural and Food Chemistry , vol.43 , pp. 2471-2479
    • Sorgentini, D.A.1    Wagner, J.R.2
  • 28
    • 0000810637 scopus 로고
    • Structure-function relationships in food proteins: Subunit interactions in heat-inducted gelation of 7S, 11S, and soy isolate proteins
    • Utsumi S., and Kinsella J.E. Structure-function relationships in food proteins: Subunit interactions in heat-inducted gelation of 7S, 11S, and soy isolate proteins. Journal of Agricultural and Food Chemistry 33 (1985) 297-303
    • (1985) Journal of Agricultural and Food Chemistry , vol.33 , pp. 297-303
    • Utsumi, S.1    Kinsella, J.E.2
  • 31
    • 0001129215 scopus 로고    scopus 로고
    • Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid- treated soy isolates
    • Wagner J.R., Sorgentini D.A., and Anon. Thermal and electrophoretic behavior, hydrophobicity, and some functional properties of acid- treated soy isolates. Journal of Agricultural and Food Chemistry 44 (1996) 1881-1889
    • (1996) Journal of Agricultural and Food Chemistry , vol.44 , pp. 1881-1889
    • Wagner, J.R.1    Sorgentini, D.A.2
  • 32
    • 0035804537 scopus 로고    scopus 로고
    • Critical factors determing inactivation kinetics by pulsed electric field food processing
    • Wouters P.C., Alvarez I., and Raso J. Critical factors determing inactivation kinetics by pulsed electric field food processing. Trends in Food Science & Technology 12 (2001) 112-121
    • (2001) Trends in Food Science & Technology , vol.12 , pp. 112-121
    • Wouters, P.C.1    Alvarez, I.2    Raso, J.3
  • 33
    • 34247187913 scopus 로고
    • Molecular understanding of heat-induced phenomena of soybean protein
    • Yamauchi F., Yamagishi T., and Iwabuchi S. Molecular understanding of heat-induced phenomena of soybean protein. Food Review International 7 (1991) 721-729
    • (1991) Food Review International , vol.7 , pp. 721-729
    • Yamauchi, F.1    Yamagishi, T.2    Iwabuchi, S.3
  • 34
    • 9344267178 scopus 로고    scopus 로고
    • Effects of pulsed electric fields on the activity and structure of pepsin
    • Yang R.J., Li S.Q., and Zhang Q.H. Effects of pulsed electric fields on the activity and structure of pepsin. Journal of Agricultural and Food Chemistry 52 (2004) 7400-7406
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , pp. 7400-7406
    • Yang, R.J.1    Li, S.Q.2    Zhang, Q.H.3
  • 35
    • 0033045451 scopus 로고    scopus 로고
    • Inactivation of papain by pulsed electric fields in a continuous system
    • Yeom H.W., Zhang Q.H., and Dunne C.P. Inactivation of papain by pulsed electric fields in a continuous system. Food Chemistry 67 (1999) 53-59
    • (1999) Food Chemistry , vol.67 , pp. 53-59
    • Yeom, H.W.1    Zhang, Q.H.2    Dunne, C.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.