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Volumn 119, Issue , 2019, Pages 444-454

Drying method determines the structure and the solubility of microfluidized pea globulin aggregates

Author keywords

Aggregate; Freeze drying; High dynamic pressure; Microfluidization; Microscopy; Pea globulin; Solubility; Spray drying; Structure; Suspension stability

Indexed keywords

DRYING; HYDROPHOBICITY; MICROSCOPIC EXAMINATION; PROTEINS; SOLUBILITY; SPRAY DRYING; STABILITY; STRUCTURE (COMPOSITION);

EID: 85061613365     PISSN: 09639969     EISSN: 18737145     Source Type: Journal    
DOI: 10.1016/j.foodres.2019.02.015     Document Type: Article
Times cited : (26)

References (42)
  • 1
    • 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
  • 3
    • 0032058092 scopus 로고    scopus 로고
    • Functional properties of faba bean (Vicia faba) protein flour dried by spray drying and freeze drying
    • Cepeda, E., Villaran, M.C., Aranguiz, N., Functional properties of faba bean (Vicia faba) protein flour dried by spray drying and freeze drying. Journal of Food Engineering 36 (1998), 303–310.
    • (1998) Journal of Food Engineering , vol.36 , pp. 303-310
    • Cepeda, E.1    Villaran, M.C.2    Aranguiz, N.3
  • 4
    • 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
  • 5
    • 85041679301 scopus 로고    scopus 로고
    • A systematical study of the overall influence of carbon allotrope additives on performance, stability and redispeersibility of magnetorheological fluids
    • Cvek, M., Mrlik, M., Moucka, R., Sedlacik, M., A systematical study of the overall influence of carbon allotrope additives on performance, stability and redispeersibility of magnetorheological fluids. Colloids and Surfaces, A: Physicochemical and Engineering Aspects 543 (2018), 83–92.
    • (2018) Colloids and Surfaces, A: Physicochemical and Engineering Aspects , vol.543 , pp. 83-92
    • Cvek, M.1    Mrlik, M.2    Moucka, R.3    Sedlacik, M.4
  • 6
    • 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
  • 7
    • 27544467437 scopus 로고    scopus 로고
    • Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy
    • Ellepola, S.W., Choi, S.M., Ma, C.Y., Conformational study of globulin from rice (Oryza sativa) seeds by Fourier-transform infrared spectroscopy. International Journal of Biological Macromolecules 37 (2005), 12–20.
    • (2005) International Journal of Biological Macromolecules , vol.37 , pp. 12-20
    • Ellepola, S.W.1    Choi, S.M.2    Ma, C.Y.3
  • 9
    • 85027583704 scopus 로고    scopus 로고
    • Grass pea (Lathyrus sativus L.) protein isolate: The effect of extraction optimization and drying methods on the structure and functional properties
    • Feyzi, S., Milani, E., Golimovahhed, Q.A., Grass pea (Lathyrus sativus L.) protein isolate: The effect of extraction optimization and drying methods on the structure and functional properties. Food Hydrocolloids 74 (2018), 187–196.
    • (2018) Food Hydrocolloids , vol.74 , pp. 187-196
    • Feyzi, S.1    Milani, E.2    Golimovahhed, Q.A.3
  • 10
    • 0037290325 scopus 로고    scopus 로고
    • Impact of processing on functional properties of protein products from wrinkled peas
    • Fuhrmeister, N.H., Meuser, F., Impact of processing on functional properties of protein products from wrinkled peas. Journal of Food Engineering 56 (2003), 119–129.
    • (2003) Journal of Food Engineering , vol.56 , pp. 119-129
    • Fuhrmeister, N.H.1    Meuser, F.2
  • 11
    • 84857051506 scopus 로고    scopus 로고
    • Properties of spray-dried food flavours microencapsulated zith two-layered membranes: Roles of interfacial interactions and water
    • Gharsallaoui, A., Roudaut, G., Beney, L., Chambin, O., Voilley, A., Saurel, R., Properties of spray-dried food flavours microencapsulated zith two-layered membranes: Roles of interfacial interactions and water. Food Chemistry 132 (2012), 1713–1720.
    • (2012) Food Chemistry , vol.132 , pp. 1713-1720
    • Gharsallaoui, A.1    Roudaut, G.2    Beney, L.3    Chambin, O.4    Voilley, A.5    Saurel, R.6
  • 12
    • 84962682261 scopus 로고    scopus 로고
    • Effect of drying methods on physico-chemical and functional properties of chickpea protein concentrates
    • Ghribi, A.M., Gafsi, I.M., Blecker, C., Danthine, S., Attia, H., Besbes, S., Effect of drying methods on physico-chemical and functional properties of chickpea protein concentrates. Journal of Food Engineering 165 (2015), 179–188.
    • (2015) Journal of Food Engineering , vol.165 , pp. 179-188
    • Ghribi, A.M.1    Gafsi, I.M.2    Blecker, C.3    Danthine, S.4    Attia, H.5    Besbes, S.6
  • 13
    • 84952863030 scopus 로고    scopus 로고
    • Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate
    • Gong, K.J., Si, A.M., Liu, H.Z., Liu, L., Hu, H., Adhikari, B., Wang, Q., Emulsifying properties and structure changes of spray and freeze-dried peanut protein isolate. Journal of Food Engineering 170 (2016), 33–40.
    • (2016) Journal of Food Engineering , vol.170 , pp. 33-40
    • Gong, K.J.1    Si, A.M.2    Liu, H.Z.3    Liu, L.4    Hu, H.5    Adhikari, B.6    Wang, Q.7
  • 14
    • 77954751565 scopus 로고    scopus 로고
    • Effects of drying methods on physicochemical and functional properties of soy protein isolates
    • Hu, X., Cheng, Y., Fan, J., Lu, Z., Yamaki, K., Li, L., Effects of drying methods on physicochemical and functional properties of soy protein isolates. Journal of Food Processing & Preservation 34 (2010), 520–540.
    • (2010) Journal of Food Processing & Preservation , vol.34 , pp. 520-540
    • Hu, X.1    Cheng, Y.2    Fan, J.3    Lu, Z.4    Yamaki, K.5    Li, L.6
  • 15
    • 80051784470 scopus 로고    scopus 로고
    • Physicochemical and functional properties of lentil protein isolates prepared by different drying methods
    • Joshi, M., Adhikari, B., Aldred, P., Panozzo, J.F., Kasapis, S., Physicochemical and functional properties of lentil protein isolates prepared by different drying methods. Food Chemistry 129 (2011), 1513–1522.
    • (2011) Food Chemistry , vol.129 , pp. 1513-1522
    • Joshi, M.1    Adhikari, B.2    Aldred, P.3    Panozzo, J.F.4    Kasapis, S.5
  • 16
    • 52649129277 scopus 로고    scopus 로고
    • Structure of heat-induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate
    • Jung, J.M., Savin, G., Pouzot, M., Schmitt, C., Mezzenga, R., Structure of heat-induced β-lactoglobulin aggregates and their complexes with sodium-dodecyl sulfate. Biomacromolecules 9 (2008), 2477–2486.
    • (2008) Biomacromolecules , vol.9 , pp. 2477-2486
    • Jung, J.M.1    Savin, G.2    Pouzot, M.3    Schmitt, C.4    Mezzenga, R.5
  • 17
    • 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
  • 18
    • 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
  • 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
    • 85041439600 scopus 로고    scopus 로고
    • Pea protein isolates: Structure, extraction and functionality
    • Lam, A.C.Y., Tyler, R.T., Nickerson, M.T., Pea protein isolates: Structure, extraction and functionality. Food Reviews International 34 (2018), 126–147.
    • (2018) Food Reviews International , vol.34 , pp. 126-147
    • Lam, A.C.Y.1    Tyler, R.T.2    Nickerson, M.T.3
  • 21
    • 85057535916 scopus 로고    scopus 로고
    • Solid dispersion-based spray-drying improves solubility and mitigates beany flavor of pea protein isolae
    • Lan, Y., Xu, M., Ohm, J.B., Chen, B., Rao, J., Solid dispersion-based spray-drying improves solubility and mitigates beany flavor of pea protein isolae. Food Chemistry, 2018, 10.1016/j.foodchem.2018.11.074.
    • (2018) Food Chemistry
    • Lan, Y.1    Xu, M.2    Ohm, J.B.3    Chen, B.4    Rao, J.5
  • 22
    • 0029269767 scopus 로고
    • Modeling segregation of solute material during drying of liquid foods
    • Meerdink, G., Van't Riet, K., Modeling segregation of solute material during drying of liquid foods. AICHE Journal 41 (1995), 732–736.
    • (1995) AICHE Journal , vol.41 , pp. 732-736
    • Meerdink, G.1    Van't Riet, K.2
  • 25
    • 84860604080 scopus 로고    scopus 로고
    • Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behaviour in admixture with alginate
    • Mession, J.L., Assifaoui, A., Cayot, P., Saurel, R., Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behaviour in admixture with alginate. Food Hydrocolloids 29 (2012), 335–346.
    • (2012) Food Hydrocolloids , vol.29 , pp. 335-346
    • Mession, J.L.1    Assifaoui, A.2    Cayot, P.3    Saurel, R.4
  • 26
    • 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
  • 28
    • 79961023076 scopus 로고    scopus 로고
    • Beta-lactoglobulin and WPI aggregates: Formation, structure and applications
    • Nicolai, T., Britten, M., Schmitt, C., Beta-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
  • 30
    • 85044003116 scopus 로고    scopus 로고
    • Modulation of the emulsifying properties of pea globulin soluble aggregates by dynamic high-pressure fluidization
    • Oliete, B., Potin, F., Cases, E., Saurel, R., Modulation of the emulsifying properties of pea globulin soluble aggregates by dynamic high-pressure fluidization. Innovative Food Science and Emerging Technologies 47 (2018), 292–300.
    • (2018) Innovative Food Science and Emerging Technologies , vol.47 , pp. 292-300
    • Oliete, B.1    Potin, F.2    Cases, E.3    Saurel, R.4
  • 31
    • 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
  • 32
    • 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.K., 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.K.4
  • 33
    • 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
  • 34
    • 84908551315 scopus 로고    scopus 로고
    • Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study
    • Shevkani, K., Singh, N., Kaur, A., Rana, J.C., Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study. Food Hydrocolloids 43 (2015), 679–689.
    • (2015) Food Hydrocolloids , vol.43 , pp. 679-689
    • Shevkani, K.1    Singh, N.2    Kaur, A.3    Rana, J.C.4
  • 35
    • 84938748915 scopus 로고    scopus 로고
    • Functional attributes of pea protein isolates prepared using different extraction methods and cultivars
    • Stone, A.K., Karalash, A., Tyler, R.T., Zarkentin, T.D., Nickerson, M.T., Functional attributes of pea protein isolates prepared using different extraction methods and cultivars. Food Research International 76 (2015), 31–38.
    • (2015) Food Research International , vol.76 , pp. 31-38
    • Stone, A.K.1    Karalash, A.2    Tyler, R.T.3    Zarkentin, T.D.4    Nickerson, M.T.5
  • 37
    • 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
  • 38
    • 67349182649 scopus 로고    scopus 로고
    • Physicochemical, functional and structural properties of vicilin-rich protein isolates from three Phaseolus legumes: Effect of heat treatment
    • Tang, C.H., Sun, X., Yin, S.W., Physicochemical, functional and structural properties of vicilin-rich protein isolates from three Phaseolus legumes: Effect of heat treatment. Food Hydrocolloids 23 (2009), 1771–1778.
    • (2009) Food Hydrocolloids , vol.23 , pp. 1771-1778
    • Tang, C.H.1    Sun, X.2    Yin, S.W.3
  • 39
    • 84901802353 scopus 로고    scopus 로고
    • Relationship between secondary structure and surface hydrophobicity of soybean protein isolate subjected to heat treatment. Journal of Chemistry
    • Wang, Z., Li, Y., Jiang,L., Qi, B., & Zhou, L. (2014). Relationship between secondary structure and surface hydrophobicity of soybean protein isolate subjected to heat treatment. Journal of Chemistry, https://doi.org/10.1155/2014/475389.
    • (2014)
    • Wang, Z.1    Li, Y.2    Jiang, L.3    Qi, B.4    Zhou, L.5
  • 40
    • 85048191525 scopus 로고    scopus 로고
    • Effects of high pressure homogenization on faba bean protein aggregation in relation to solubility and interfacial properties
    • Yang, J., Liu, G., Zeng, H., Chen, L., Effects of high pressure homogenization on faba bean protein aggregation in relation to solubility and interfacial properties. Food Hydrocolloids 83 (2018), 275–286.
    • (2018) Food Hydrocolloids , vol.83 , pp. 275-286
    • Yang, J.1    Liu, G.2    Zeng, H.3    Chen, L.4
  • 41
    • 84862788892 scopus 로고    scopus 로고
    • Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study
    • Zhang, J., Liang, L., Tian, Z., Chen, L., Subirade, M., Preparation and in vitro evaluation of calcium-induced soy protein isolate nanoparticles and their formation mechanism study. Food Chemistry 133 (2012), 390–399.
    • (2012) Food Chemistry , vol.133 , pp. 390-399
    • Zhang, J.1    Liang, L.2    Tian, Z.3    Chen, L.4    Subirade, M.5
  • 42
    • 84879301636 scopus 로고    scopus 로고
    • Effects of spray drying and freeze drying on the properties of protein isolate from rice dreg protein
    • Zhao, Q., Xiong, H., Selomulya, C., Chen, X.D., Huang, S., Ruan, X., Sun, W., Effects of spray drying and freeze drying on the properties of protein isolate from rice dreg protein. Food and Bioprocess Technology 6 (2013), 1759–1769.
    • (2013) Food and Bioprocess Technology , vol.6 , pp. 1759-1769
    • Zhao, Q.1    Xiong, H.2    Selomulya, C.3    Chen, X.D.4    Huang, S.5    Ruan, X.6    Sun, W.7


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