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Volumn 47, Issue , 2018, Pages 292-300

Modulation of the emulsifying properties of pea globulin soluble aggregates by dynamic high-pressure fluidization

Author keywords

Aggregate; Emulsion; High dynamic pressure; Microfluidization; Pea globulin; Thermal denaturation

Indexed keywords

AGGREGATES; DROPS; EMULSIFICATION; EMULSIONS; FLOCCULATION; FLUIDIZATION; HYDROPHOBICITY; PARTICLE SIZE; PROTEINS; SULFUR COMPOUNDS;

EID: 85044003116     PISSN: 14668564     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.ifset.2018.03.015     Document Type: Article
Times cited : (64)

References (44)
  • 1
    • 79958034324 scopus 로고    scopus 로고
    • Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate
    • Adebiyi, Q.P., Aluko, R.E., Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate. Food Chemistry 128 (2011), 902–908.
    • (2011) Food Chemistry , vol.128 , pp. 902-908
    • Adebiyi, Q.P.1    Aluko, R.E.2
  • 3
    • 0004202155 scopus 로고
    • Official methods of analysis
    • 15th ed. Association of Official Analytical Chemists, Inc. Arlington, VA
    • AOAC. Association of Official Analytical Chemists International, Official methods of analysis. 15th ed., 1990, Association of Official Analytical Chemists, Inc., Arlington, VA.
    • (1990)
    • AOAC. Association of Official Analytical Chemists International1
  • 4
    • 30344478568 scopus 로고    scopus 로고
    • Functional properties of whey proteins as affected by dynamic high-pressure treatment
    • Bouaouina, H., Desrumaux, A., Loisel, C., Legrand, J., Functional properties of whey proteins as affected by dynamic high-pressure treatment. International Dairy Journal 16 (2006), 275–284.
    • (2006) International Dairy Journal , vol.16 , pp. 275-284
    • Bouaouina, H.1    Desrumaux, A.2    Loisel, C.3    Legrand, J.4
  • 5
    • 0004992931 scopus 로고    scopus 로고
    • Pea globulins
    • P.R. Shewry R. Casey Kluwer Academic Publishers Dordrecht, The Netherlands
    • Casey, R., Domoney, C., Pea globulins. Shewry, P.R., Casey, R., (eds.) Seed Proteins, 1999, Kluwer Academic Publishers, Dordrecht, The Netherlands, 171–208.
    • (1999) Seed Proteins , pp. 171-208
    • Casey, R.1    Domoney, C.2
  • 6
    • 84964409730 scopus 로고    scopus 로고
    • Heat-induced soluble protein aggregates from mixed pea globulins and β-lactoglobulin
    • Chihi, M., Mession, J.L., Sok, N., Saurel, R., Heat-induced soluble protein aggregates from mixed pea globulins and β-lactoglobulin. Journal of Agricultural and Food Chemistry 64 (2016), 2780–2791.
    • (2016) Journal of Agricultural and Food Chemistry , vol.64 , pp. 2780-2791
    • Chihi, M.1    Mession, J.L.2    Sok, N.3    Saurel, R.4
  • 7
    • 0347469014 scopus 로고    scopus 로고
    • Large scale procedure for fractionation of albumins and globulins from pea seeds
    • Crévieu, I., Berot, S., Gueguen, J., Large scale procedure for fractionation of albumins and globulins from pea seeds. Food/Nahrung 40 (1996), 237–244.
    • (1996) Food/Nahrung , vol.40 , pp. 237-244
    • Crévieu, I.1    Berot, S.2    Gueguen, J.3
  • 8
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S., Protein stabilization of emulsions and foams. Journal of Food Science 70 (2006), R54–R66.
    • (2006) Journal of Food Science , vol.70 , pp. R54-R66
    • Damodaran, S.1
  • 9
    • 77957016943 scopus 로고    scopus 로고
    • Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds
    • Deng, Q., Wang, L., Wei, F., Xie, B., Huang, F.H., Huang, W., Xue, S., Functional properties of protein isolates, globulin and albumin extracted from Ginkgo biloba seeds. Food Chemistry 124 (2011), 1458–1465.
    • (2011) Food Chemistry , vol.124 , pp. 1458-1465
    • Deng, Q.1    Wang, L.2    Wei, F.3    Xie, B.4    Huang, F.H.5    Huang, W.6    Xue, S.7
  • 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 92 (2009), 1387–1397.
    • (2009) Journal of Dairy Science , vol.92 , pp. 1387-1397
    • Dissanayake, M.1    Vasiljevic, T.2
  • 12
    • 0001190763 scopus 로고    scopus 로고
    • High pressure promotes β-lactoglobulin aggregation through SH/SS interchange reactions
    • Funtenberger, S., Dumay, E., Cheftel, J., High pressure promotes β-lactoglobulin aggregation through SH/SS 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.3
  • 13
    • 0018980315 scopus 로고
    • Isoelectric focusing properties and carbohydrate content of pea (Pisum sativum) legumin
    • Gatehouse, J.A., Croy, R.R.D., Boulter, D., Isoelectric focusing properties and carbohydrate content of pea (Pisum sativum) legumin. Biochemistry Journal 185 (1980), 497–503.
    • (1980) Biochemistry Journal , vol.185 , pp. 497-503
    • Gatehouse, J.A.1    Croy, R.R.D.2    Boulter, D.3
  • 14
    • 0000008542 scopus 로고    scopus 로고
    • Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds
    • Hoffmann, M.A.M., van Mil, P.J.J.M., Heat-induced aggregation of β-lactoglobulin: role of the free thiol group and disulfide bonds. Journal of Agricultural and Food Chemistry 45 (1997), 2942–2948.
    • (1997) Journal of Agricultural and Food Chemistry , vol.45 , pp. 2942-2948
    • Hoffmann, M.A.M.1    van Mil, P.J.J.M.2
  • 15
    • 0344011091 scopus 로고    scopus 로고
    • High pressure microfluidization treatment of heat denatured whey proteins for improved functionality
    • Iordache, M., Jelen, P., High pressure microfluidization treatment of heat denatured whey proteins for improved functionality. Innovative Food Science & Emerging Technologies 4 (2003), 367–376.
    • (2003) Innovative Food Science & Emerging Technologies , vol.4 , pp. 367-376
    • Iordache, M.1    Jelen, P.2
  • 16
    • 80054693820 scopus 로고    scopus 로고
    • Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction
    • Karaca, A.C., Low, N., Nickerson, M., Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Research International 44 (2011), 2742–2750.
    • (2011) Food Research International , vol.44 , pp. 2742-2750
    • Karaca, A.C.1    Low, N.2    Nickerson, M.3
  • 17
    • 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 624 (1980), 13–20.
    • (1980) Biochimica et Biophysica Acta , vol.624 , pp. 13-20
    • Kato, A.1    Nakai, S.2
  • 18
    • 66149085355 scopus 로고    scopus 로고
    • Effect of dynamic high pressure homogenization on the aggregation state of soy protein
    • Keerati-u-rai, M., Corredig, M., Effect of dynamic high pressure homogenization on the aggregation state of soy protein. Journal of Agricultural and Food Chemistry 57 (2009), 3556–3562.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 3556-3562
    • Keerati-u-rai, M.1    Corredig, M.2
  • 19
    • 0009681073 scopus 로고
    • Heterogeneity in subunit composition of the legumin of Pisum sativum
    • Krishina, T.G., Croy, R.R.D., Boulter, D., Heterogeneity in subunit composition of the legumin of Pisum sativum. Phytochemistry 18 (1979), 1879–1880.
    • (1979) Phytochemistry , vol.18 , pp. 1879-1880
    • Krishina, T.G.1    Croy, R.R.D.2    Boulter, D.3
  • 20
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U.K., Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227 (1970), 680–685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 22
    • 84877314473 scopus 로고    scopus 로고
    • pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins
    • Liang, H.N., Tang, C.H., pH-dependent emulsifying properties of pea [Pisum sativum (L.)] proteins. Food Hydrocolloids 33 (2013), 309–319.
    • (2013) Food Hydrocolloids , vol.33 , pp. 309-319
    • Liang, H.N.1    Tang, C.H.2
  • 23
    • 84901250363 scopus 로고    scopus 로고
    • Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0
    • Liang, H.N., Tang, C.H., Pea protein exhibits a novel Pickering stabilization for oil-in-water emulsions at pH 3.0. LWT- Food Science and Technology 58 (2014), 463–469.
    • (2014) LWT- Food Science and Technology , vol.58 , pp. 463-469
    • Liang, H.N.1    Tang, C.H.2
  • 24
    • 84884488895 scopus 로고    scopus 로고
    • Soy protein nanoparticle aggregates as Pickering stabilizers for oil-in-water emulsions
    • Liu, F., Tang, C.H., Soy protein nanoparticle aggregates as Pickering stabilizers for oil-in-water emulsions. Journal of Agricultural and Food Chemistry 61 (2013), 8888–8898.
    • (2013) Journal of Agricultural and Food Chemistry , vol.61 , pp. 8888-8898
    • Liu, F.1    Tang, C.H.2
  • 25
    • 84929191400 scopus 로고    scopus 로고
    • Soy glycinin as food-grade Pickering stabilizers: Part. I. Structural characteristics, emulsifying properties and adsorption/arrangement at interface
    • Liu, F., Tang, C.H., Soy glycinin as food-grade Pickering stabilizers: Part. I. Structural characteristics, emulsifying properties and adsorption/arrangement at interface. Food Hydrocolloids 60 (2016), 606–619.
    • (2016) Food Hydrocolloids , vol.60 , pp. 606-619
    • Liu, F.1    Tang, C.H.2
  • 26
    • 67649210997 scopus 로고    scopus 로고
    • Characterization and high-pressure microfluidization-induced activation of polyphenoloxidase from Chinese pear (Pyrus pyrifolia Nakai)
    • Liu, W., Liu, J.H., Xie, M.Y., Liu, C.M., Liu, W.L., Wan, J., Characterization and high-pressure microfluidization-induced activation of polyphenoloxidase from Chinese pear (Pyrus pyrifolia Nakai). Journal of Agricultural and Food Chemistry 57 (2009), 5376–5380.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 5376-5380
    • Liu, W.1    Liu, J.H.2    Xie, M.Y.3    Liu, C.M.4    Liu, W.L.5    Wan, J.6
  • 27
    • 84871941838 scopus 로고    scopus 로고
    • The role of glycinin in the formation of gel-like soy protein-stabilized emulsions
    • Luo, L.J., Liu, F., Tang, C.H., The role of glycinin in the formation of gel-like soy protein-stabilized emulsions. Food Hydrocolloids 32 (2013), 97–105.
    • (2013) Food Hydrocolloids , vol.32 , pp. 97-105
    • Luo, L.J.1    Liu, F.2    Tang, C.H.3
  • 29
    • 84921993092 scopus 로고    scopus 로고
    • Effect of globular pea proteins fractionation on their heat-induced aggregation and acid cold-set gelation
    • Mession, J.L., Chihi, M.L., Sok, N., Saurel, R., Effect of globular pea proteins fractionation on their heat-induced aggregation and acid cold-set gelation. Food Hydrocolloids 46 (2015), 233–243.
    • (2015) Food Hydrocolloids , vol.46 , pp. 233-243
    • Mession, J.L.1    Chihi, M.L.2    Sok, N.3    Saurel, R.4
  • 30
    • 84873628903 scopus 로고    scopus 로고
    • Thermal denaturation of pea globulins (Pisum sativum L.)—Molecular interactions leading to heat-induced protein aggregation
    • Mession, J.L., Sok, N., Assifaoui, A., Saurel, R., Thermal denaturation of pea globulins (Pisum sativum L.)—Molecular interactions leading to heat-induced protein aggregation. Journal of Agricultural and Food Chemistry 61 (2013), 1196–1204.
    • (2013) Journal of Agricultural and Food Chemistry , vol.61 , pp. 1196-1204
    • Mession, J.L.1    Sok, N.2    Assifaoui, A.3    Saurel, R.4
  • 31
    • 79961023076 scopus 로고    scopus 로고
    • β-Lactoglobulin and WPI aggregates: Formation, structure and applications
    • Nicolai, T., Britten, M., Schmitt, C., β-Lactoglobulin and WPI aggregates: Formation, structure and applications. Food Hydrocolloids 25 (2011), 1945–1962.
    • (2011) Food Hydrocolloids , vol.25 , pp. 1945-1962
    • Nicolai, T.1    Britten, M.2    Schmitt, C.3
  • 32
    • 84883781030 scopus 로고    scopus 로고
    • Fibrillization of whey proteins improves foaming capacity and foam stability at low protein concentrations
    • Oboroceanu, D., Zang, L., Magner, E., Auty, M.A.E., Fibrillization of whey proteins improves foaming capacity and foam stability at low protein concentrations. Journal of Food Engineering 121 (2014), 102–111.
    • (2014) Journal of Food Engineering , vol.121 , pp. 102-111
    • Oboroceanu, D.1    Zang, L.2    Magner, E.3    Auty, M.A.E.4
  • 33
    • 84937239500 scopus 로고    scopus 로고
    • Effects of heat treatment on the emulsifying properties of pea proteins
    • Peng, W., Kong, X., Chen, Y., Zhang, C., Yang, Y., Hua, Y., Effects of heat treatment on the emulsifying properties of pea proteins. Food Hydrocolloids 52 (2016), 301–310.
    • (2016) Food Hydrocolloids , vol.52 , pp. 301-310
    • Peng, W.1    Kong, X.2    Chen, Y.3    Zhang, C.4    Yang, Y.5    Hua, Y.6
  • 34
    • 77957782799 scopus 로고    scopus 로고
    • β-Conglycinin and glycinin soybean protein emulsions treated by combined temperature–high-pressure treatment
    • Puppo, M.C., Beaumal, V., Speroni, F., de Lamballerie, M., Añon, M.C., Anton, M., β-Conglycinin and glycinin soybean protein emulsions treated by combined temperature–high-pressure treatment. Food Hydrocolloids 25 (2011), 389–397.
    • (2011) Food Hydrocolloids , vol.25 , pp. 389-397
    • Puppo, M.C.1    Beaumal, V.2    Speroni, F.3    de Lamballerie, M.4    Añon, M.C.5    Anton, M.6
  • 35
    • 0004007590 scopus 로고
    • Control of colloid stability through zeta potential
    • Livingston Publishing Company Wynnewood, PA
    • Riddick, T.M., Control of colloid stability through zeta potential. 1968, Livingston Publishing Company, Wynnewood, PA.
    • (1968)
    • Riddick, T.M.1
  • 36
    • 19944379827 scopus 로고    scopus 로고
    • Heat-induced soy-whey proteins interactions: Formation of soluble and insoluble protein complexes
    • Roesch, R.R., Corredig, M., Heat-induced soy-whey proteins interactions: Formation of soluble and insoluble protein complexes. Journal of Agricultural and Food Chemistry 53 (2005), 3476–3482.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 3476-3482
    • Roesch, R.R.1    Corredig, M.2
  • 38
    • 33846642594 scopus 로고    scopus 로고
    • Physicochemical and textural properties of heat-induced pea protein isolate gels
    • Shand, P.J., Ya, H., Pietrasik, Z., Wanasundara, P.K.J.P.D., Physicochemical and textural properties of heat-induced pea protein isolate gels. Food Chemistry 102 (2007), 1119–1130.
    • (2007) Food Chemistry , vol.102 , pp. 1119-1130
    • Shand, P.J.1    Ya, H.2    Pietrasik, Z.3    Wanasundara, P.K.J.P.D.4
  • 39
    • 84888033533 scopus 로고    scopus 로고
    • Characteristics and oxidative stability of soy protein-stabilized oil-in-water emulsions: Influence of ionic strength and heat pretreatment
    • Shao, Y., Tang, C.H., Characteristics and oxidative stability of soy protein-stabilized oil-in-water emulsions: Influence of ionic strength and heat pretreatment. Food Hydrocolloids 37 (2014), 149–158.
    • (2014) Food Hydrocolloids , vol.37 , pp. 149-158
    • Shao, Y.1    Tang, C.H.2
  • 40
    • 84859152164 scopus 로고    scopus 로고
    • Microfluidization as a potential technique to modify surface properties of soy protein isolate
    • Shen, L., Tang, C.H., Microfluidization as a potential technique to modify surface properties of soy protein isolate. Food Research International 48 (2012), 108–118.
    • (2012) Food Research International , vol.48 , pp. 108-118
    • Shen, L.1    Tang, C.H.2
  • 41
    • 77953912253 scopus 로고    scopus 로고
    • Effects of calcium and high pressure on soybean proteins: A calorimetric study
    • Speroni, F., Anon, M.C., de Lamballerie, M., Effects of calcium and high pressure on soybean proteins: A calorimetric study. Food Research International 43 (2010), 1347–1355.
    • (2010) Food Research International , vol.43 , pp. 1347-1355
    • Speroni, F.1    Anon, M.C.2    de Lamballerie, M.3
  • 42
    • 77956613058 scopus 로고    scopus 로고
    • Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate
    • Sun, X.D., Arntfield, S.D., Gelation properties of salt-extracted pea protein isolate induced by heat treatment: Effect of heating and cooling rate. Food Chemistry 124 (2011), 1011–1016.
    • (2011) Food Chemistry , vol.124 , pp. 1011-1016
    • Sun, X.D.1    Arntfield, S.D.2
  • 43
    • 84861798810 scopus 로고    scopus 로고
    • Cold, gel-like soy protein emulsions by microfluidization: Emulsion characteristics, rheological and microstructural properties, and gelling mechanism
    • Tang, C., Liu, F., Cold, gel-like soy protein emulsions by microfluidization: Emulsion characteristics, rheological and microstructural properties, and gelling mechanism. Food Hydrocolloids 30 (2013), 61–72.
    • (2013) Food Hydrocolloids , vol.30 , pp. 61-72
    • Tang, C.1    Liu, F.2
  • 44
    • 33751341296 scopus 로고    scopus 로고
    • Adsorption at the air–water interface and emulsification properties of grain legume protein derivatives from pea and broad bean
    • Tsoukala, A., Papalamprou, E., Makri, E., Doxastakis, G., Braudo, E.E., Adsorption at the air–water interface and emulsification properties of grain legume protein derivatives from pea and broad bean. Colloids and Surfaces B: Biointerfaces 53 (2006), 203–208.
    • (2006) Colloids and Surfaces B: Biointerfaces , vol.53 , pp. 203-208
    • Tsoukala, A.1    Papalamprou, E.2    Makri, E.3    Doxastakis, G.4    Braudo, E.E.5


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