메뉴 건너뛰기




Volumn 54, Issue , 2016, Pages 342-350

Characteristics and emulsifying properties of acid and acid-heat induced egg white protein

Author keywords

Acid heat induced; Egg white; Emulsifying properties; Physicochemical characteristics; Structure

Indexed keywords

DROPS; EMULSIFICATION; EMULSIONS; HYDROPHOBICITY; PHASE INTERFACES; PHASE SEPARATION; PROTEINS; STABILITY;

EID: 84946404991     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2015.09.026     Document Type: Article
Times cited : (104)

References (28)
  • 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. Comparison of protein surface hydrophobicity measured at various pH values using three different fluorescent probes. Journal of Agricultural and Food Chemistry 2000, 48(2):328-334.
    • (2000) Journal of Agricultural and Food Chemistry , vol.48 , Issue.2 , pp. 328-334
    • Alizadeh-Pasdar, N.1    Li-Chan, E.C.2
  • 2
    • 85168409788 scopus 로고    scopus 로고
    • Effect of pH and NaCl on the emulsifying properties of a napin protein isolate
    • Cheung L., Wanasundara J., Nickerson M.T. Effect of pH and NaCl on the emulsifying properties of a napin protein isolate. Food Biophysics 2014, 1-9.
    • (2014) Food Biophysics , pp. 1-9
    • Cheung, L.1    Wanasundara, J.2    Nickerson, M.T.3
  • 4
    • 84894472336 scopus 로고    scopus 로고
    • Emulsifying properties and oil/water (O/W) interface adsorption behavior of heated soy proteins: effects of heating concentration, homogenizer rotating speed, and salt addition level
    • Cui Z., Chen Y., Kong X., Zhang C., Hua Y. Emulsifying properties and oil/water (O/W) interface adsorption behavior of heated soy proteins: effects of heating concentration, homogenizer rotating speed, and salt addition level. Journal of Agricultural and Food Chemistry 2014, 62(7):1634-1642.
    • (2014) Journal of Agricultural and Food Chemistry , vol.62 , Issue.7 , pp. 1634-1642
    • Cui, Z.1    Chen, Y.2    Kong, X.3    Zhang, C.4    Hua, Y.5
  • 5
    • 84884261042 scopus 로고    scopus 로고
    • Protein concentration and protein-exposed hydrophobicity as dominant parameters determining the flocculation of protein-stabilized oil-in-water emulsions
    • Delahaije R.J., Wierenga P.A., van Nieuwenhuijzen N.H., Giuseppin M.L., Gruppen H. Protein concentration and protein-exposed hydrophobicity as dominant parameters determining the flocculation of protein-stabilized oil-in-water emulsions. Langmuir 2013, 29(37):11567-11574.
    • (2013) Langmuir , vol.29 , Issue.37 , pp. 11567-11574
    • Delahaije, R.J.1    Wierenga, P.A.2    van Nieuwenhuijzen, N.H.3    Giuseppin, M.L.4    Gruppen, H.5
  • 6
    • 33846557563 scopus 로고    scopus 로고
    • Stability of acidic egg white protein emulsions containing xanthan gum
    • Drakos A., Kiosseoglou V. Stability of acidic egg white protein emulsions containing xanthan gum. Journal of Agricultural and Food Chemistry 2006, 54(26):10164-10169.
    • (2006) Journal of Agricultural and Food Chemistry , vol.54 , Issue.26 , pp. 10164-10169
    • Drakos, A.1    Kiosseoglou, V.2
  • 7
    • 0032553843 scopus 로고    scopus 로고
    • Characterization of aggregation phenomena by means of acoustic and electroacoustic spectroscopy
    • Dukhin A.S., Goetz P.J. Characterization of aggregation phenomena by means of acoustic and electroacoustic spectroscopy. Colloids and Surfaces A: Physicochemical and Engineering Aspects 1998, 144(1):49-58.
    • (1998) Colloids and Surfaces A: Physicochemical and Engineering Aspects , vol.144 , Issue.1 , pp. 49-58
    • Dukhin, A.S.1    Goetz, P.J.2
  • 8
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
    • de la Fuente M.A., Singh H., Hemar Y. Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends in Food Science & Technology 2002, 13(8):262-274.
    • (2002) Trends in Food Science & Technology , vol.13 , Issue.8 , pp. 262-274
    • de la Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 11
    • 70349215199 scopus 로고    scopus 로고
    • Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes
    • Jiang J., Chen J., Xiong Y.L. Structural and emulsifying properties of soy protein isolate subjected to acid and alkaline pH-shifting processes. Journal of Agricultural and Food Chemistry 2009, 57(16):7576-7583.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , Issue.16 , pp. 7576-7583
    • Jiang, J.1    Chen, J.2    Xiong, Y.L.3
  • 12
    • 0002765706 scopus 로고
    • Changes in the emulsifying and foaming properties of proteins during heat denaturation
    • Kato A., Osako Y., Matsudomi N., Kobayashi K. Changes in the emulsifying and foaming properties of proteins during heat denaturation. Agricultural and Biological Chemistry 1983, 47(1):33-37.
    • (1983) Agricultural and Biological Chemistry , vol.47 , Issue.1 , pp. 33-37
    • Kato, A.1    Osako, Y.2    Matsudomi, N.3    Kobayashi, K.4
  • 13
    • 70149119887 scopus 로고    scopus 로고
    • Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate
    • Keerati-u-rai M., Corredig M. Heat-induced changes in oil-in-water emulsions stabilized with soy protein isolate. Food Hydrocolloids 2009, 23(8):2141-2148.
    • (2009) Food Hydrocolloids , vol.23 , Issue.8 , pp. 2141-2148
    • Keerati-u-rai, M.1    Corredig, M.2
  • 14
    • 11844284817 scopus 로고    scopus 로고
    • Influence of protein concentration and order of addition on thermal stability of β-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH
    • Kim H., Decker E.A., McClements D.J. Influence of protein concentration and order of addition on thermal stability of β-lactoglobulin stabilized n-hexadecane oil-in-water emulsions at neutral pH. Langmuir 2005, 21(1):134-139.
    • (2005) Langmuir , vol.21 , Issue.1 , pp. 134-139
    • Kim, H.1    Decker, E.A.2    McClements, D.J.3
  • 15
    • 0030295334 scopus 로고    scopus 로고
    • The applications of Raman spectroscopy in food science
    • Li-Chan E.C.Y. The applications of Raman spectroscopy in food science. Trends in Food Science & Technology 1996, 7(11).
    • (1996) Trends in Food Science & Technology , vol.7 , Issue.11
    • Li-Chan, E.C.Y.1
  • 16
    • 0034301848 scopus 로고    scopus 로고
    • Competitive displacement of β-lactoglobulin from the air/water interface by sodium dodecyl sulfate
    • Mackie A.R., Gunning A.P., Wilde P.J., Morris V.J. Competitive displacement of β-lactoglobulin from the air/water interface by sodium dodecyl sulfate. Langmuir 2000, 16(21):8176-8181.
    • (2000) Langmuir , vol.16 , Issue.21 , pp. 8176-8181
    • Mackie, A.R.1    Gunning, A.P.2    Wilde, P.J.3    Morris, V.J.4
  • 21
    • 79952534865 scopus 로고    scopus 로고
    • Formation of nanoemulsions stabilized by model food-grade emulsifiers using high-pressure homogenization: factors affecting particle size
    • Qian C., McClements D.J. Formation of nanoemulsions stabilized by model food-grade emulsifiers using high-pressure homogenization: factors affecting particle size. Food Hydrocolloids 2011, 25(5):1000-1008.
    • (2011) Food Hydrocolloids , vol.25 , Issue.5 , pp. 1000-1008
    • Qian, C.1    McClements, D.J.2
  • 22
    • 75149162776 scopus 로고    scopus 로고
    • Effect of heat treatment on milk protein functionality at emulsion interfaces. A review
    • Raikos V. Effect of heat treatment on milk protein functionality at emulsion interfaces. A review. Food Hydrocolloids 2010, 24(4):259-265.
    • (2010) Food Hydrocolloids , vol.24 , Issue.4 , pp. 259-265
    • Raikos, V.1
  • 23
    • 12344326655 scopus 로고    scopus 로고
    • Interfacial, foaming and emulsifying characteristics of sodium caseinate as influenced by protein concentration in solution
    • Sánchez C.C., Patino J.M.R. Interfacial, foaming and emulsifying characteristics of sodium caseinate as influenced by protein concentration in solution. Food Hydrocolloids 2005, 19(3):407-416.
    • (2005) Food Hydrocolloids , vol.19 , Issue.3 , pp. 407-416
    • Sánchez, C.C.1    Patino, J.M.R.2
  • 24
    • 67651115509 scopus 로고    scopus 로고
    • Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions
    • Schmitt C., Bovay C., Vuilliomenet A.-M., Rouvet M., Bovetto L., Barbar R., et al. Multiscale characterization of individualized β-lactoglobulin microgels formed upon heat treatment under narrow pH range conditions. Langmuir 2009, 25(14):7899-7909.
    • (2009) Langmuir , vol.25 , Issue.14 , pp. 7899-7909
    • Schmitt, C.1    Bovay, C.2    Vuilliomenet, A.-M.3    Rouvet, M.4    Bovetto, L.5    Barbar, R.6
  • 26
    • 79961022888 scopus 로고    scopus 로고
    • Aspects of milk-protein-stabilised emulsions
    • Singh H. Aspects of milk-protein-stabilised emulsions. Food Hydrocolloids 2011, 25(8):1938-1944.
    • (2011) Food Hydrocolloids , vol.25 , Issue.8 , pp. 1938-1944
    • Singh, H.1
  • 27
    • 34249865663 scopus 로고    scopus 로고
    • Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding
    • Sivakumar R., G K.H. Conformational and rheological changes in catfish myosin as affected by different acids during acid-induced unfolding and refolding. Journal of Agricultural and Food Chemistry 2007, 55(10):4144-4153.
    • (2007) Journal of Agricultural and Food Chemistry , vol.55 , Issue.10 , pp. 4144-4153
    • Sivakumar, R.1
  • 28
    • 79952532377 scopus 로고    scopus 로고
    • Physicochemical properties of lactoferrin stabilized oil-in-water emulsions: effects of pH, salt and heating
    • Tokle T., McClements D.J. Physicochemical properties of lactoferrin stabilized oil-in-water emulsions: effects of pH, salt and heating. Food Hydrocolloids 2010, 25(5):976-982.
    • (2010) Food Hydrocolloids , vol.25 , Issue.5 , pp. 976-982
    • Tokle, T.1    McClements, D.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.