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Volumn 4, Issue 8, 2011, Pages 1341-1348

Pulsed Electric Field-Induced Structural Modification of Whey Protein Isolate

Author keywords

Intrinsic fluorescence intensity; Protein structure; Pulsed electric fields (PEF); Surface hydrophobicity; Whey protein isolate (WPI)

Indexed keywords

INTRINSIC FLUORESCENCE; PROTEIN STRUCTURE; PULSED ELECTRIC FIELD; SURFACE HYDROPHOBICITY; WHEY PROTEIN ISOLATE;

EID: 80053560151     PISSN: 19355130     EISSN: 19355149     Source Type: Journal    
DOI: 10.1007/s11947-009-0266-z     Document Type: Article
Times cited : (103)

References (48)
  • 1
    • 0034001548 scopus 로고    scopus 로고
    • Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes
    • Alizadeh-Pasdar, N., & Li-Chan, E. C. Y. (2000). Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural & Food Chemistry, 48(2), 328-334.
    • (2000) Journal of Agricultural & Food Chemistry , vol.48 , Issue.2 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 6
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • Dissanayake, M., & Vasiljevic, T. (2009). Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science, 92, 1387-1397.
    • (2009) Journal of Dairy Science , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 7
    • 0025929570 scopus 로고
    • Fluorescence techniques for studying protein structure
    • Eftink, M. R. (1991). Fluorescence techniques for studying protein structure. Methods of Biochemical Analysis, 35, 127-205.
    • (1991) Methods of Biochemical Analysis , vol.35 , pp. 127-205
    • Eftink, M.R.1
  • 8
    • 0027958069 scopus 로고
    • The use of fluorescence methods to monitor unfolding transitions in proteins
    • Eftink, M. R. (1994). The use of fluorescence methods to monitor unfolding transitions in proteins. Biophysical Journal, 66, 482-501.
    • (1994) Biophysical Journal , vol.66 , pp. 482-501
    • Eftink, M.R.1
  • 10
    • 15044348987 scopus 로고    scopus 로고
    • Utilization of front-face fluorescence spectroscopy for analysis of process cheese functionality
    • Garimella-Purna, S. K., Prow, L. A., & Metzger, L. E. (2005). Utilization of front-face fluorescence spectroscopy for analysis of process cheese functionality. Journal of Dairy Science, 88, 470-477.
    • (2005) Journal of Dairy Science , vol.88 , pp. 470-477
    • Garimella-Purna, S.K.1    Prow, L.A.2    Metzger, L.E.3
  • 11
    • 0007757078 scopus 로고
    • Spectrofluorometric study on surface hydrophobicity of bovine casein micelles in suspension and during enzymic coagulation
    • Gatti, C. A., Risso, P. H., & Pires, M. S. (1995). Spectrofluorometric study on surface hydrophobicity of bovine casein micelles in suspension and during enzymic coagulation. Journal of Agricultural & Food Chemistry, 43, 2339-2344.
    • (1995) Journal of Agricultural & Food Chemistry , vol.43 , pp. 2339-2344
    • Gatti, C.A.1    Risso, P.H.2    Pires, M.S.3
  • 12
    • 0000538001 scopus 로고
    • Front-face fluorescence applied to structural studies of proteins and lipid-protein interactions of visco-elastic food products. 1-Designing of front-face adaptor and validity of front-face fluorescence measurements
    • Genot, C., Tonetti, F., Montenay-Garestier, T., & Drapon, R. (1992). Front-face fluorescence applied to structural studies of proteins and lipid-protein interactions of visco-elastic food products. 1-Designing of front-face adaptor and validity of front-face fluorescence measurements. Sciences des Aliments, 12(2), 199-212.
    • (1992) Sciences Des Aliments , vol.12 , Issue.2 , pp. 199-212
    • Genot, C.1    Tonetti, F.2    Montenay-Garestier, T.3    Drapon, R.4
  • 13
    • 84987322003 scopus 로고
    • Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals
    • Hayakawa, I., Kajihara, J., Morikawa, K., Oda, M., & Fujio, Y. (1992). Denaturation of bovine serum albumin (BSA) and ovalbumin by high pressure, heat and chemicals. Journal of Food Science, 57, 288-292.
    • (1992) Journal of Food Science , vol.57 , pp. 288-292
    • Hayakawa, I.1    Kajihara, J.2    Morikawa, K.3    Oda, M.4    Fujio, Y.5
  • 14
    • 0032842614 scopus 로고    scopus 로고
    • Inactivation of Bacillus subtilis by high intensity pulsed electric fields under close to isothermal conditions
    • Heinz, V., Phillips, S. T., Zenker, M., & Knorr, D. (1999). Inactivation of Bacillus subtilis by high intensity pulsed electric fields under close to isothermal conditions. Food Biotechnology, 13, 155-168.
    • (1999) Food Biotechnology , vol.13 , pp. 155-168
    • Heinz, V.1    Phillips, S.T.2    Zenker, M.3    Knorr, D.4
  • 15
    • 0041349500 scopus 로고    scopus 로고
    • Fluorescence spectroscopy investigation of acid- or rennet-induced coagulation of milk
    • Herbert, S., Riaublanc, A., Bouchet, B., Gallant, D. J., & Dufour, E. (1999). Fluorescence spectroscopy investigation of acid- or rennet-induced coagulation of milk. Journal of Dairy Science, 82, 2056-2062.
    • (1999) Journal of Dairy Science , vol.82 , pp. 2056-2062
    • Herbert, S.1    Riaublanc, A.2    Bouchet, B.3    Gallant, D.J.4    Dufour, E.5
  • 16
    • 0030784326 scopus 로고    scopus 로고
    • Effects of high field electric pulses on the activity of selected enzymes
    • Ho, S. Y., Mittal, G. S., & Cross, J. D. (1997). Effects of high field electric pulses on the activity of selected enzymes. Journal of Food Engineering, 31, 69-84.
    • (1997) Journal of Food Engineering , vol.31 , pp. 69-84
    • Ho, S.Y.1    Mittal, G.S.2    Cross, J.D.3
  • 18
    • 30344474283 scopus 로고    scopus 로고
    • Structure and surface properties of the serum heat-induced protein aggregates isolated from heated skim milk
    • Jean, K., Renan, M., Famelart, M., & Guyomarc'h, F. (2006). Structure and surface properties of the serum heat-induced protein aggregates isolated from heated skim milk. International Dairy Journal, 16, 303-315.
    • (2006) International Dairy Journal , vol.16 , pp. 303-315
    • Jean, K.1    Renan, M.2    Famelart, M.3    Guyomarc'h, F.4
  • 19
    • 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., & Brulé, G. (1999). High intensity pulsed electric fields applied to egg white: effect on Salmonella enteritidis inactivation and protein denaturation. Journal of Food Protection, 62(12), 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    Brulé, G.5
  • 20
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe methods and its correlation with surface properties of proteins
    • Kato, A., & Nakai, S. (1980). Hydrophobicity determined by a fluorescence probe methods and its correlation with surface properties of proteins. Biochimica et Biophysica Acta, 624, 13-20.
    • (1980) Biochimica Et Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 21
    • 0036882032 scopus 로고    scopus 로고
    • Determination of lactulose and furosine in milk using front-face fluorescence spectroscopy
    • Kulmyrzaev, A., & Defour, E. (2002). Determination of lactulose and furosine in milk using front-face fluorescence spectroscopy. Lait, 82, 725-735.
    • (2002) Lait , vol.82 , pp. 725-735
    • Kulmyrzaev, A.1    Defour, E.2
  • 22
    • 33745956074 scopus 로고    scopus 로고
    • Functional properties of high hydrostatic pressure-treated whey protein
    • Lee, W., Clark, S., & Swanson, B. G. (2006). Functional properties of high hydrostatic pressure-treated whey protein. Journal of Food Processing and Preservation, 30, 488-501.
    • (2006) Journal of Food Processing and Preservation , vol.30 , pp. 488-501
    • Lee, W.1    Clark, S.2    Swanson, B.G.3
  • 23
    • 34247211578 scopus 로고    scopus 로고
    • Effects of pulsed electric fields on physicochemical properties of soybean protein isolates
    • Li, Y., Chen, Z., & Mo, H. (2007). Effects of pulsed electric fields on physicochemical properties of soybean protein isolates. Lebensmittel-Wissenschaft und-Technologie, 40, 1167-1175.
    • (2007) Lebensmittel-Wissenschaft Und-Technologie , vol.40 , pp. 1167-1175
    • Li, Y.1    Chen, Z.2    Mo, H.3
  • 26
    • 0032839589 scopus 로고    scopus 로고
    • Effect of heat treatment on bovine α-lactoglobulin A, B, and C explored using thiol availability and fluorescence
    • Manderson, G. A., Hardman, M. J., & Creamer, L. K. (1998). Effect of heat treatment on bovine α-lactoglobulin A, B, and C explored using thiol availability and fluorescence. Journal of Agricultural & Food Chemistry, 47, 3617-3627.
    • (1998) Journal of Agricultural & Food Chemistry , vol.47 , pp. 3617-3627
    • Manderson, G.A.1    Hardman, M.J.2    Creamer, L.K.3
  • 28
    • 0000126233 scopus 로고
    • Proteins as fat substitutes
    • N. S. Hettiarachchy and G. R. Ziegler (Eds.), New York: Dekker
    • Miller, M. S. (1994). Proteins as fat substitutes. In N. S. Hettiarachchy & G. R. Ziegler (Eds.), Protein functionality in food systems (pp. 435-466). New York: Dekker.
    • (1994) Protein Functionality in Food Systems , pp. 435-466
    • Miller, M.S.1
  • 29
    • 0000891935 scopus 로고    scopus 로고
    • Effect of dry heat and mild alkaline treatment on functional properties of egg white proteins
    • Mine, Y. (1997). Effect of dry heat and mild alkaline treatment on functional properties of egg white proteins. Journal of Agricultural & Food Chemistry, 45(8), 2924-2928.
    • (1997) Journal of Agricultural & Food Chemistry , vol.45 , Issue.8 , pp. 2924-2928
    • Mine, Y.1
  • 30
    • 0034774241 scopus 로고    scopus 로고
    • Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties
    • Moro, A., Gatti, C., & Delorenzi, N. (2001). Hydrophobicity of whey protein concentrates measured by fluorescence quenching and its relation with surface functional properties. Journal of Agricultural & Food Chemistry, 49(10), 4784-4789.
    • (2001) Journal of Agricultural & Food Chemistry , vol.49 , Issue.10 , pp. 4784-4789
    • Moro, A.1    Gatti, C.2    Delorenzi, N.3
  • 31
    • 33845550183 scopus 로고
    • Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity
    • Nakai, S. (1983). Structure-function relationships of food proteins with an emphasis on the importance of protein hydrophobicity. Journal of Agricultural & Food Chemistry, 31, 676-683.
    • (1983) Journal of Agricultural & Food Chemistry , vol.31 , pp. 676-683
    • Nakai, S.1
  • 32
    • 0742288323 scopus 로고    scopus 로고
    • Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white
    • Perez, O. E., & Pilosof, A. M. R. (2004). Pulsed electric fields effects on the molecular structure and gelation of β-lactoglobulin concentrate and egg white. Food Research International, 37, 102-110.
    • (2004) Food Research International , vol.37 , pp. 102-110
    • Perez, O.E.1    Pilosof, A.M.R.2
  • 34
    • 77249118908 scopus 로고    scopus 로고
    • Influence of whey protein composite coatings on plum (Prunus domestica L.) fruit quality
    • doi:10.1007/s11947-007-0014-1
    • Reinoso, E., Mittal, G. S., & Lim, L.-T. (2008). Influence of whey protein composite coatings on plum (Prunus domestica L.) fruit quality. Food Bioprocess Technology, 1, 314-325. doi: 10. 1007/s11947-007-0014-1.
    • (2008) Food Bioprocess Technology , vol.1 , pp. 314-325
    • Reinoso, E.1    Mittal, G.S.2    Lim, L.-T.3
  • 35
    • 0032302761 scopus 로고    scopus 로고
    • Heat-induced gelation of globulin protein mixtures. A DSC and scanning electron microscopic study
    • Relkin, P., Meylheuc, T., Launay, B., & Raynal, K. (1998). Heat-induced gelation of globulin protein mixtures. A DSC and scanning electron microscopic study. Journal of Thermal Analysis & Calorimetry, 51(3), 747-756.
    • (1998) Journal of Thermal Analysis & Calorimetry , vol.51 , Issue.3 , pp. 747-756
    • Relkin, P.1    Meylheuc, T.2    Launay, B.3    Raynal, K.4
  • 36
    • 0026096545 scopus 로고
    • Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe
    • Semisotnov, G. V., Radionova, N. A., Razgulyaev, O. I., & Uversky, N. V. (1991). Study of the molten globule intermediate state in protein folding by a hydrophobic fluorescent probe. Biopolymers, 31, 119-128.
    • (1991) Biopolymers , vol.31 , pp. 119-128
    • Semisotnov, G.V.1    Radionova, N.A.2    Razgulyaev, O.I.3    Uversky, N.V.4
  • 37
    • 0029776440 scopus 로고    scopus 로고
    • The pressure-induced structural change of bovine beta-lactalbumin as studied by a fluorescence hydrophobic probe
    • Tanaka, N., Nakajima, K., & Kunugi, S. (1996). The pressure-induced structural change of bovine beta-lactalbumin as studied by a fluorescence hydrophobic probe. International Journal of Peptide & Protein Research, 48(3), 259-264.
    • (1996) International Journal of Peptide & Protein Research , vol.48 , Issue.3 , pp. 259-264
    • Tanaka, N.1    Nakajima, K.2    Kunugi, S.3
  • 39
    • 0020650276 scopus 로고
    • A simple turbidimetric method for determining the fat binding capacity of proteins
    • Voutsinas, L. P., & Nakai, S. (1983). A simple turbidimetric method for determining the fat binding capacity of proteins. Journal of Agricultural & Food Chemistry, 31, 58-63.
    • (1983) Journal of Agricultural & Food Chemistry , vol.31 , pp. 58-63
    • Voutsinas, L.P.1    Nakai, S.2
  • 40
    • 0035804537 scopus 로고    scopus 로고
    • Critical factors determining inactivation kinetics by pulsed electric field food processing
    • Wouters, P. C., Alvarez, I., & Raso, J. (2001). Critical factors determining inactivation kinetics by pulsed electric field food processing. Trends in Food Science & Technology, 12, 112-121.
    • (2001) Trends in Food Science & Technology , vol.12 , pp. 112-121
    • Wouters, P.C.1    Alvarez, I.2    Raso, J.3
  • 42
    • 84923833663 scopus 로고
    • Thermal aggregation of β-lactoglobulin: effect of pH, ionic environment, and thiol reagent
    • Xiong, Y. L., Karl, A. D., & Liping, W. (1993). Thermal aggregation of β-lactoglobulin: effect of pH, ionic environment, and thiol reagent. Journal of Dairy Science, 76, 70-77.
    • (1993) Journal of Dairy Science , vol.76 , pp. 70-77
    • Xiong, Y.L.1    Karl, A.D.2    Liping, W.3
  • 44
    • 33845621269 scopus 로고    scopus 로고
    • Enzymatic inactivation by pulsed electric fields: a review
    • G. V. Barbosa-Cánovas, Q. H. Zhang, and G. Tabilo-Munizaga (Eds.), Lancaster: Technomic
    • Yeom, H. W., & Zhang, Q. H. (2001). Enzymatic inactivation by pulsed electric fields: a review. In G. V. Barbosa-Cánovas, Q. H. Zhang & G. Tabilo-Munizaga (Eds.), Pulsed electric fields in food processing: fundamental aspects and applications (pp. 57-63). Lancaster: Technomic.
    • (2001) Pulsed Electric Fields in Food Processing: Fundamental Aspects and Applications , pp. 57-63
    • Yeom, H.W.1    Zhang, Q.H.2
  • 46
    • 33947423331 scopus 로고    scopus 로고
    • Inactivation effects of PEF on horseradish peroxidase (HRP) and pectinesterase (PE)
    • Zhang, R., Cheng, L., Wang, L., & Guan, Z. (2006). Inactivation effects of PEF on horseradish peroxidase (HRP) and pectinesterase (PE). IEEE Transactions on Plasma Science, 34(6), 2030-2036.
    • (2006) IEEE Transactions on Plasma Science , vol.34 , Issue.6 , pp. 2030-2036
    • Zhang, R.1    Cheng, L.2    Wang, L.3    Guan, Z.4
  • 47
    • 18344374395 scopus 로고    scopus 로고
    • Inactivation and conformational change of pectinesterase induced by pulsed electric field
    • Zhong, K., Hu, X., Chen, F., Wu, J., & Liao, X. (2005a). Inactivation and conformational change of pectinesterase induced by pulsed electric field. Transactions of the CSAE, 21(2), 149-152.
    • (2005) Transactions of the CSAE , vol.21 , Issue.2 , pp. 149-152
    • Zhong, K.1    Hu, X.2    Chen, F.3    Wu, J.4    Liao, X.5
  • 48
    • 15944425448 scopus 로고    scopus 로고
    • Inactivation and conformational change of horseradish peroxidase induced by pulsed electric field
    • Zhong, K., Hu, X., Zhao, G., Chen, F., & Liao, X. (2005b). Inactivation and conformational change of horseradish peroxidase induced by pulsed electric field. Food Chemistry, 92, 473-479.
    • (2005) Food Chemistry , vol.92 , pp. 473-479
    • Zhong, K.1    Hu, X.2    Zhao, G.3    Chen, F.4    Liao, X.5


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