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Volumn 60, Issue 1, 2015, Pages 427-434

The effect of pH and temperature pre-treatments on the physicochemical and emulsifying properties of whey protein isolate

Author keywords

Emulsions; Hydrophobicity; Interface; Temperature; Whey protein isolate

Indexed keywords

DAIRIES; EMULSIONS; HYDROPHOBICITY; INTERFACES (MATERIALS); PHYSICOCHEMICAL PROPERTIES; PROTEINS; TEMPERATURE;

EID: 85027932498     PISSN: 00236438     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.lwt.2014.07.031     Document Type: Article
Times cited : (121)

References (40)
  • 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. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry 2000, 48:328-334.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.Y.2
  • 3
    • 84870932654 scopus 로고    scopus 로고
    • Association of Official Analytical Chemists, Washington, DC
    • AOAC Official method of analysis 2003, Association of Official Analytical Chemists, Washington, DC. 17th ed.
    • (2003) Official method of analysis
  • 4
    • 0041885362 scopus 로고    scopus 로고
    • Thermal modifications of structure and co-denaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases
    • Bertrand-Harb C., Baday A., Dalgalarrondo M., Chobert J.M., Haertle T. Thermal modifications of structure and co-denaturation of α-lactalbumin and β-lactoglobulin induce changes of solubility and susceptibility to proteases. Nahrung Food 2002, 46:283-289.
    • (2002) Nahrung Food , vol.46 , pp. 283-289
    • Bertrand-Harb, C.1    Baday, A.2    Dalgalarrondo, M.3    Chobert, J.M.4    Haertle, T.5
  • 5
    • 0033858518 scopus 로고    scopus 로고
    • Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study
    • Boye J.I., Alli I. Thermal denaturation of mixtures of α-lactalbumin and β-lactoglobulin: a differential scanning calorimetric study. Food Research International 2000, 33:673-682.
    • (2000) Food Research International , vol.33 , pp. 673-682
    • Boye, J.I.1    Alli, I.2
  • 6
    • 0039136058 scopus 로고    scopus 로고
    • Ultrasonic spectrometry study of the influence of temperature on whey protein aggregation
    • Bryant C.M., McClements D.J. Ultrasonic spectrometry study of the influence of temperature on whey protein aggregation. Food Hydrocolloids 1999, 13:439-444.
    • (1999) Food Hydrocolloids , vol.13 , pp. 439-444
    • Bryant, C.M.1    McClements, D.J.2
  • 7
    • 0000318442 scopus 로고
    • Irreversible heat denaturation of bovine α-lactalbuin
    • Chaplin L.C., Lyster R.L.J. Irreversible heat denaturation of bovine α-lactalbuin. Journal of Dairy Science 1986, 53:249-258.
    • (1986) Journal of Dairy Science , vol.53 , pp. 249-258
    • Chaplin, L.C.1    Lyster, R.L.J.2
  • 8
    • 0001042101 scopus 로고    scopus 로고
    • Amino Acids, peptides and proteins
    • Marcel Dekker, New York, NY, USA, O.R. Fennema (Ed.)
    • Damodaran N.S. Amino Acids, peptides and proteins. Food chemistry 1996, 321. Marcel Dekker, New York, NY, USA. 3rd ed. O.R. Fennema (Ed.).
    • (1996) Food chemistry , pp. 321
    • Damodaran, N.S.1
  • 9
    • 0035146503 scopus 로고    scopus 로고
    • Milk protein interfacial layers and the relationship to emulsion stability and rheology
    • Dickinson E. Milk protein interfacial layers and the relationship to emulsion stability and rheology. Colloids and Surfaces B- Biointerfaces 2001, 20:197-210.
    • (2001) Colloids and Surfaces B- Biointerfaces , vol.20 , pp. 197-210
    • Dickinson, E.1
  • 10
    • 65249156463 scopus 로고    scopus 로고
    • Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing
    • Dissanayake M., Vasiljevic T. Functional properties of whey proteins affected by heat treatment and hydrodynamic high-pressure shearing. Journal of Dairy Science 2009, 92:1387-1397.
    • (2009) Journal of Dairy Science , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 13
    • 0001592750 scopus 로고    scopus 로고
    • Heat-induced interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin
    • Gezimati J., Creamer L.K., Singh H. Heat-induced interactions and gelation of mixtures of β-lactoglobulin and α-lactalbumin. Journal of Agricultural and Food Chemistry 1997, 45:1130-1136.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 1130-1136
    • Gezimati, J.1    Creamer, L.K.2    Singh, H.3
  • 14
    • 70149121260 scopus 로고    scopus 로고
    • Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry
    • Haug I.J., Skar H.M., Vegarud G.E., Langsrud T., Draget K.I. Electrostatic effects on β-lactoglobulin transitions during heat denaturation as studied by differential scanning calorimetry. Food Hydrocolloids 2009, 23:2287-2293.
    • (2009) Food Hydrocolloids , vol.23 , pp. 2287-2293
    • Haug, I.J.1    Skar, H.M.2    Vegarud, G.E.3    Langsrud, T.4    Draget, K.I.5
  • 16
    • 0036230909 scopus 로고    scopus 로고
    • Changed protein structures of bovine β-lactoglobulin b and α-latalbumin as a consequence of heat treatment
    • Hong Y.H., Creamer L.K. Changed protein structures of bovine β-lactoglobulin b and α-latalbumin as a consequence of heat treatment. International Dairy Journal 2002, 12:345-359.
    • (2002) International Dairy Journal , vol.12 , pp. 345-359
    • Hong, Y.H.1    Creamer, L.K.2
  • 17
    • 84867746711 scopus 로고    scopus 로고
    • Combined effect of heat treatment and ionic strength on the functionality of whey proteins
    • Hussain R., Gaiani C., Jeandel C., Ghanbaja J., Scher J. Combined effect of heat treatment and ionic strength on the functionality of whey proteins. Journal of Dairy Science 2012, 95:6260-6273.
    • (2012) Journal of Dairy Science , vol.95 , pp. 6260-6273
    • Hussain, R.1    Gaiani, C.2    Jeandel, C.3    Ghanbaja, J.4    Scher, J.5
  • 19
    • 0019331914 scopus 로고
    • Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins
    • Kato A., Nakai S. Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochimica et Biophysica Acta 1980, 624:13-20.
    • (1980) Biochimica et Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 20
    • 0142123418 scopus 로고    scopus 로고
    • Characterization of soluble aggregates from whey protein isolate
    • Kazmierski M., Corredig M. Characterization of soluble aggregates from whey protein isolate. Food Hydrocolloids 2003, 17:685-692.
    • (2003) Food Hydrocolloids , vol.17 , pp. 685-692
    • Kazmierski, M.1    Corredig, M.2
  • 22
    • 33846839238 scopus 로고    scopus 로고
    • Protein particulates: another generic form of protein aggregation?
    • Krebs M.R.H., Devlin G.L., Donald A.M. Protein particulates: another generic form of protein aggregation?. Biophysical Journal 2007, 92:1336-1342.
    • (2007) Biophysical Journal , vol.92 , pp. 1336-1342
    • Krebs, M.R.H.1    Devlin, G.L.2    Donald, A.M.3
  • 23
    • 57749118622 scopus 로고    scopus 로고
    • Comparative study on heat stability and functionality of camel and bovine milk whey proteins
    • Laleye L.C., Jobe B., Wasesa A.A.H. Comparative study on heat stability and functionality of camel and bovine milk whey proteins. Journal of Dairy Science 2008, 91:4527-4534.
    • (2008) Journal of Dairy Science , vol.91 , pp. 4527-4534
    • Laleye, L.C.1    Jobe, B.2    Wasesa, A.A.H.3
  • 25
    • 0346336103 scopus 로고    scopus 로고
    • Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin b and α-lactalbumin
    • Livney Y.D., Verespej E., Dalgleish D.G. Steric effects governing disulfide bond interchange during thermal aggregation in solutions of β-lactoglobulin b and α-lactalbumin. Journal of Agricultural and Food Chemistry 2003, 51:8098-8106.
    • (2003) Journal of Agricultural and Food Chemistry , vol.51 , pp. 8098-8106
    • Livney, Y.D.1    Verespej, E.2    Dalgleish, D.G.3
  • 26
    • 84862540847 scopus 로고    scopus 로고
    • Effect of NaCl addition during diafiltration on the solubility, hydrophobicity, and disulfide bonds of 80% milk protein concentrate powder
    • Mao X.Y., Tong P.S., Gualco S., Vink S. Effect of NaCl addition during diafiltration on the solubility, hydrophobicity, and disulfide bonds of 80% milk protein concentrate powder. Journal of Dairy Science 2012, 95:3481-3488.
    • (2012) Journal of Dairy Science , vol.95 , pp. 3481-3488
    • Mao, X.Y.1    Tong, P.S.2    Gualco, S.3    Vink, S.4
  • 28
    • 34250001656 scopus 로고    scopus 로고
    • Conditions limiting the influence of thiol-disulphide interchange reactions on the heat-induced aggregation kinetics of β-lactoglobulin
    • Mounsey J.S., O'Kennedy B.T. Conditions limiting the influence of thiol-disulphide interchange reactions on the heat-induced aggregation kinetics of β-lactoglobulin. International Dairy Journal 2007, 17:1034-1042.
    • (2007) International Dairy Journal , vol.17 , pp. 1034-1042
    • Mounsey, J.S.1    O'Kennedy, B.T.2
  • 29
    • 0002348148 scopus 로고
    • Arapid method for the determination of whey-protein denaturation
    • Parris N., Baginski M.A. Arapid method for the determination of whey-protein denaturation. Journal of Dairy Science 1991, 74:58-64.
    • (1991) Journal of Dairy Science , vol.74 , pp. 58-64
    • Parris, N.1    Baginski, M.A.2
  • 30
    • 33947092713 scopus 로고
    • Emulsifying properties of proteins: evaluation of a turbidimetric technique
    • Pearce K.N., Kinsella J.E. Emulsifying properties of proteins: evaluation of a turbidimetric technique. Journal of Agricultural and Food Chemistry 1978, 26:716-723.
    • (1978) Journal of Agricultural and Food Chemistry , vol.26 , pp. 716-723
    • Pearce, K.N.1    Kinsella, J.E.2
  • 31
    • 0342421704 scopus 로고
    • Effect of sodium and calcium addition on thermal denaturation of apo-lactalbumin: a differential scanning calorimetry study
    • Relkin P., Launay B., Eynard L. Effect of sodium and calcium addition on thermal denaturation of apo-lactalbumin: a differential scanning calorimetry study. Journal of Dairy Science 1993, 76:36-47.
    • (1993) Journal of Dairy Science , vol.76 , pp. 36-47
    • Relkin, P.1    Launay, B.2    Eynard, L.3
  • 34
    • 17144389124 scopus 로고
    • Thermal decomposition of α-lactalbumin. 1. Destruction of cysteine residues
    • Schnack U., Klostermeyer H. Thermal decomposition of α-lactalbumin. 1. Destruction of cysteine residues. Milchwisenschaft 1980, 35:206-208.
    • (1980) Milchwisenschaft , vol.35 , pp. 206-208
    • Schnack, U.1    Klostermeyer, H.2
  • 35
    • 0034462997 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin A nad B with α-lactalbumin
    • Schokker E.P., Singh H., Creamer L.K. Heat-induced aggregation of β-lactoglobulin A nad B with α-lactalbumin. International Dairy Journal 2000, 10:843-853.
    • (2000) International Dairy Journal , vol.10 , pp. 843-853
    • Schokker, E.P.1    Singh, H.2    Creamer, L.K.3
  • 36
    • 67349109504 scopus 로고    scopus 로고
    • Characteristics of milk
    • CRC Press Taylor & Francis Group, Boca Raton, FL, USA, S. Damodaran, K. Parkin, O.R. Fennema (Eds.)
    • Swaisgood H.E. Characteristics of milk. Fennema's food chemistry 2008, 885-921. CRC Press Taylor & Francis Group, Boca Raton, FL, USA. 4th ed. S. Damodaran, K. Parkin, O.R. Fennema (Eds.).
    • (2008) Fennema's food chemistry , pp. 885-921
    • Swaisgood, H.E.1
  • 38
    • 0002609034 scopus 로고
    • Relationships of hydrophobicity to emulsifying properties of heat denatured proteins
    • Voutsinas L.P., Cheung E., Nakai S. Relationships of hydrophobicity to emulsifying properties of heat denatured proteins. Journal of Food Science 1983, 48:26-32.
    • (1983) Journal of Food Science , vol.48 , pp. 26-32
    • Voutsinas, L.P.1    Cheung, E.2    Nakai, S.3
  • 40
    • 77956131588 scopus 로고    scopus 로고
    • Kinetics of formation and physicochemical characterization of thermally-induced β-lactoglobulin aggregates
    • Zúñiga R.N., Tolkach A., Kulozik U., Aguilera J.M. Kinetics of formation and physicochemical characterization of thermally-induced β-lactoglobulin aggregates. Journal of Food Science 2010, 75:E261-E268.
    • (2010) Journal of Food Science , vol.75 , pp. E261-E268
    • Zúñiga, R.N.1    Tolkach, A.2    Kulozik, U.3    Aguilera, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.