메뉴 건너뛰기




Volumn 94, Issue 1, 2017, Pages 89-97

Physicochemical and functional properties of protein isolates obtained from several pea cultivars

Author keywords

[No Author keywords available]

Indexed keywords

EMULSIFICATION; OILS AND FATS; PROTEINS;

EID: 85014111808     PISSN: 00090352     EISSN: 19433638     Source Type: Journal    
DOI: 10.1094/CCHEM-04-16-0097-FI     Document Type: Article
Times cited : (61)

References (46)
  • 1
    • 79958034324 scopus 로고    scopus 로고
    • Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate
    • Adebiyi, A. P., and Aluko, R. E. 2011. Functional properties of protein fractions obtained from commercial yellow field pea (Pisum sativum L.) seed protein isolate. Food Chem. 128:902-908.
    • (2011) Food Chem , vol.128 , pp. 902-908
    • Adebiyi, A.P.1    Aluko, R.E.2
  • 2
    • 0032936698 scopus 로고    scopus 로고
    • Solubilized wheat protein isolate: Functional properties and potential food applications
    • Ahmedna, M., Prinyawiwatkul, W., and Rao, R. M. 1999. Solubilized wheat protein isolate: Functional properties and potential food applications. J. Agric. Food Chem. 47:1340-1345.
    • (1999) J. Agric. Food Chem , vol.47 , pp. 1340-1345
    • Ahmedna, M.1    Prinyawiwatkul, W.2    Rao, R.M.3
  • 3
    • 0036205439 scopus 로고    scopus 로고
    • Protein-lipid interactions in food systems: A review
    • Alzagtat, A. A., and Alli, I. 2002. Protein-lipid interactions in food systems: A review. Int. J. Food Sci. Nutr. 53:249-260.
    • (2002) Int. J. Food Sci. Nutr , vol.53 , pp. 249-260
    • Alzagtat, A.A.1    Alli, I.2
  • 4
    • 0004202155 scopus 로고    scopus 로고
    • AOAC, 18th Ed. AOAC International: Gaithersburg, MD
    • AOAC. 2005. Official Method of Analysis, 18th Ed. AOAC International: Gaithersburg, MD.
    • (2005) Official Method of Analysis
  • 6
    • 78650970923 scopus 로고    scopus 로고
    • Profile and functional properties of seed proteins from six pea (Pisum sativum) genotypes
    • Barac, M., Cabrilo, S., Pesic, M., Stanojevic, S., Zilic, S., Macej, O., and Ristic, N. 2010. Profile and functional properties of seed proteins from six pea (Pisum sativum) genotypes. Int. J. Mol. Sci. 11:4973-4990.
    • (2010) Int. J. Mol. Sci , vol.11 , pp. 4973-4990
    • Barac, M.1    Cabrilo, S.2    Pesic, M.3    Stanojevic, S.4    Zilic, S.5    Macej, O.6    Ristic, N.7
  • 7
    • 60349108930 scopus 로고    scopus 로고
    • Dissecting the proteome of pea mature seeds reveals the phenotypic plasticity of seed protein composition
    • Bourgeois,M., Jacquin, F., Savois,V., Sommerer,N., Labas, V.,Henry,C., and Burstin, J. 2009. Dissecting the proteome of pea mature seeds reveals the phenotypic plasticity of seed protein composition. Proteomics 9:254-271.
    • (2009) Proteomics , vol.9 , pp. 254-271
    • Bourgeois, M.1    Jacquin, F.2    Savois, V.3    Sommerer, N.4    Labas, V.5    Henry, C.6    Burstin, J.7
  • 8
    • 75149128950 scopus 로고    scopus 로고
    • Pulse proteins: Processing, characterization, functional properties and applications in food and feed
    • Boye, J., Zare, F., and Pletch, A. 2010a. Pulse proteins: Processing, characterization, functional properties and applications in food and feed. Food Res. Int. 43:414-431.
    • (2010) Food Res. Int , vol.43 , pp. 414-431
    • Boye, J.1    Zare, F.2    Pletch, A.3
  • 9
    • 75149150222 scopus 로고    scopus 로고
    • Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques
    • Boye, J. I., Askay, S., Roufik, S., Ribéreau, S., Mondor, M., Farnworth, E., and Rajamohamad, S. H. 2010b. Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques. Food Res. Int. 43:537-546.
    • (2010) Food Res. Int , vol.43 , pp. 537-546
    • Boye, J.I.1    Askay, S.2    Roufik, S.3    Ribéreau, S.4    Mondor, M.5    Farnworth, E.6    Rajamohamad, S.H.7
  • 10
    • 0043003962 scopus 로고
    • Quantitative variability in Pisum seed globulins: Its assessment and significance
    • Casey, R., Sharman, J. E., Wright, D. J., Bacon, J. R., and Guldager, P. 1982. Quantitative variability in Pisum seed globulins: Its assessment and significance. Plant Foods Hum. Nutr. 31:333-346.
    • (1982) Plant Foods Hum. Nutr , vol.31 , pp. 333-346
    • Casey, R.1    Sharman, J.E.2    Wright, D.J.3    Bacon, J.R.4    Guldager, P.5
  • 11
    • 0032053769 scopus 로고    scopus 로고
    • Functional properties of flours prepared from three Chinese indigenous legume seeds
    • Chau, C. F., and Cheung, P. C. K. 1998. Functional properties of flours prepared from three Chinese indigenous legume seeds. Food Chem. 61:429-433.
    • (1998) Food Chem , vol.61 , pp. 429-433
    • Chau, C.F.1    Cheung, P.C.K.2
  • 13
    • 84982560079 scopus 로고
    • A comparison of interfacial behaviours of pea (Pisum sativum L.) legumin and vicilin at air/water interface
    • Dagorn-Scaviner, C., Gueguen, J., and Lefebvre, J. 1986. A comparison of interfacial behaviours of pea (Pisum sativum L.) legumin and vicilin at air/water interface. Food/Nahrung 30:337-347.
    • (1986) Food/Nahrung , vol.30 , pp. 337-347
    • Dagorn-Scaviner, C.1    Gueguen, J.2    Lefebvre, J.3
  • 14
    • 17644396054 scopus 로고    scopus 로고
    • Protein stabilization of emulsions and foams
    • Damodaran, S. 2005. Protein stabilization of emulsions and foams. J. Food Sci. 70:R54-R66.
    • (2005) J. Food Sci , vol.70 , pp. R54-R66
    • Damodaran, S.1
  • 16
    • 84986799915 scopus 로고
    • Quantitative and qualitative variability of pea (Pisum sativum L.) protein composition
    • Gueguen, J., and Barbot, J. 1988. Quantitative and qualitative variability of pea (Pisum sativum L.) protein composition. J. Sci. Food Agric. 42:209-224.
    • (1988) J. Sci. Food Agric , vol.42 , pp. 209-224
    • Gueguen, J.1    Barbot, J.2
  • 18
    • 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., and Nickerson, M. 2011. Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Res. Int. 44:2742-2750.
    • (2011) Food Res. Int , vol.44 , pp. 2742-2750
    • Karaca, A.C.1    Low, N.2    Nickerson, M.3
  • 19
    • 58149333536 scopus 로고    scopus 로고
    • Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean-French bean 7S globulin exhibits excellent properties
    • Kimura, A., Fukuda, T., Zhang, M., Motoyama, S., Maruyama, N., and Utsumi, S. 2008. Comparison of physicochemical properties of 7S and 11S globulins from pea, fava bean, cowpea, and French bean with those of soybean-French bean 7S globulin exhibits excellent properties. J. Agric. Food Chem. 56:10273-10279.
    • (2008) J. Agric. Food Chem , vol.56 , pp. 10273-10279
    • Kimura, A.1    Fukuda, T.2    Zhang, M.3    Motoyama, S.4    Maruyama, N.5    Utsumi, S.6
  • 20
    • 0001186821 scopus 로고
    • Functional properties of proteins: Possible relationships between structure and function in foams
    • Kinsella, J. E. 1981. Functional properties of proteins: Possible relationships between structure and function in foams. Food Chem. 7:273-288.
    • (1981) Food Chem , vol.7 , pp. 273-288
    • Kinsella, J.E.1
  • 21
    • 0024822645 scopus 로고
    • Proteins in whey: Chemical, physical, and functional properties
    • Kinsella, J. E., and Whitehead, D. M. 1989. Proteins in whey: Chemical, physical, and functional properties. Adv. Food Nutr. Res. 33:343-438.
    • (1989) Adv. Food Nutr. Res , vol.33 , pp. 343-438
    • Kinsella, J.E.1    Whitehead, D.M.2
  • 22
    • 0003295698 scopus 로고
    • Functional properties of pea globulin fractions
    • Koyoro, H., and Powers, J. R. 1987. Functional properties of pea globulin fractions. Cereal Chem. 64:97-101.
    • (1987) Cereal Chem , vol.64 , pp. 97-101
    • Koyoro, H.1    Powers, J.R.2
  • 23
    • 84894615140 scopus 로고    scopus 로고
    • The effect of pH and heat pre-treatments on the physiochemical and emulsifying properties of b-lactoglobulin
    • Lam, R. S. H., and Nickerson, M. T. 2014. The effect of pH and heat pre-treatments on the physiochemical and emulsifying properties of b-lactoglobulin. Food Biophys. 9:20-28.
    • (2014) Food Biophys , vol.9 , pp. 20-28
    • Lam, R.S.H.1    Nickerson, M.T.2
  • 24
    • 33646364376 scopus 로고    scopus 로고
    • Composition and functional properties of soy protein isolates prepared using alternative defatting and extraction procedures
    • L'hocine, L., Boye, J. I., and Arcand, Y. 2006. Composition and functional properties of soy protein isolates prepared using alternative defatting and extraction procedures. J. Food Sci. 71:C137-C145.
    • (2006) J. Food Sci , vol.71 , pp. C137-C145
    • L'Hocine, L.1    Boye, J.I.2    Arcand, Y.3
  • 25
    • 75149117226 scopus 로고    scopus 로고
    • Effect of pH on the functional behavior of pea proteins isolate-gum Arabic complexes
    • Liu, S., Elmer, C., Low, N. H., and Nickerson, M. T. 2010. Effect of pH on the functional behavior of pea proteins isolate-gum Arabic complexes. Food Res. Int. 43:489-495.
    • (2010) Food Res. Int , vol.43 , pp. 489-495
    • Liu, S.1    Elmer, C.2    Low, N.H.3    Nickerson, M.T.4
  • 26
    • 84859924712 scopus 로고    scopus 로고
    • Agronomical factors influencing the legumin/vicilin ratio in pea (Pisum sativum L.) seeds
    • Mertens, C., Dehon, L., Bourgeois, A., Verhaeghe-Cartrysse, C., and Blecker, C. 2012. Agronomical factors influencing the legumin/vicilin ratio in pea (Pisum sativum L.) seeds. J. Sci. Food Agric. 92: 1591-1596.
    • (2012) J. Sci. Food Agric , vol.92 , pp. 1591-1596
    • Mertens, C.1    Dehon, L.2    Bourgeois, A.3    Verhaeghe-Cartrysse, C.4    Blecker, C.5
  • 28
    • 33847230230 scopus 로고    scopus 로고
    • Differences in chemical composition of field pea (Pisum sativum) cultivars: Effects of cultivation area and year
    • Nikolopoulou, D., Grigorakis, K., Stasini, M., Alexis, M. N., and Iliadis, K. 2007. Differences in chemical composition of field pea (Pisum sativum) cultivars: Effects of cultivation area and year. Food Chem. 103:847-852.
    • (2007) Food Chem , vol.103 , pp. 847-852
    • Nikolopoulou, D.1    Grigorakis, K.2    Stasini, M.3    Alexis, M.N.4    Iliadis, K.5
  • 29
    • 2442434766 scopus 로고    scopus 로고
    • Characterization of pea vicilin 1. Denoting convicilin as the a-subunit of the Pisum vicilin family
    • O'Kane, F. E., Happe, R. P., Vereijken, J. M., Gruppen, H., and van Boekel, M. A. J. S. 2004. Characterization of pea vicilin 1. Denoting convicilin as the a-subunit of the Pisum vicilin family. J. Agric. Food Chem. 52:3141-3148.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 3141-3148
    • O'Kane, F.E.1    Happe, R.P.2    Vereijken, J.M.3    Gruppen, H.4    Van Boekel, M.A.J.S.5
  • 31
    • 0020158221 scopus 로고
    • Quantitative studies on the cotyledonary proteins in the genus Pisum
    • Schroeder, H. E. 1982. Quantitative studies on the cotyledonary proteins in the genus Pisum. J. Sci. Food Agric. 33:623-633.
    • (1982) J. Sci. Food Agric , vol.33 , pp. 623-633
    • Schroeder, H.E.1
  • 32
    • 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., and Rana, J. C. 2015. Structural and functional characterization of kidney bean and field pea protein isolates: A comparative study. Food Hydrocolloids 43:679-689.
    • (2015) Food Hydrocolloids , vol.43 , pp. 679-689
    • Shevkani, K.1    Singh, N.2    Kaur, A.3    Rana, J.C.4
  • 34
    • 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., Warkentin, T. D., and Nickerson, M. T. 2015b. Functional attributes of pea protein isolates prepared using different extraction methods and cultivars. Food Res. Int. 76:31-38.
    • (2015) Food Res. Int , vol.76 , pp. 31-38
    • Stone, A.K.1    Karalash, A.2    Tyler, R.T.3    Warkentin, T.D.4    Nickerson, M.T.5
  • 35
    • 80155211192 scopus 로고    scopus 로고
    • Formation and functionality of whey protein isolate-(Kappa-, iota-, and lambda-type) carrageenan electrostatic complexes
    • Stone, A. K., and Nickerson, M. T. 2012. Formation and functionality of whey protein isolate-(Kappa-, iota-, and lambda-type) carrageenan electrostatic complexes. Food Hydrocolloids 27:271-277.
    • (2012) Food Hydrocolloids , vol.27 , pp. 271-277
    • Stone, A.K.1    Nickerson, M.T.2
  • 36
    • 0025422167 scopus 로고
    • Pea and lentil protein extraction and functionality
    • Swanson, B. G. 1990. Pea and lentil protein extraction and functionality. J. AOCS 67:276-280.
    • (1990) J. AOCS , vol.67 , pp. 276-280
    • Swanson, B.G.1
  • 37
    • 67349134524 scopus 로고    scopus 로고
    • Characterization of lipoxygenase from pea seeds (Pisum sativum var. Telephone L.)
    • Szymanowska, U., Jakubczyk, A., Baraniak, B., and Kur, A. 2009. Characterization of lipoxygenase from pea seeds (Pisum sativum var. Telephone L.). Food Chem. 116:906-910.
    • (2009) Food Chem , vol.116 , pp. 906-910
    • Szymanowska, U.1    Jakubczyk, A.2    Baraniak, B.3    Kur, A.4
  • 38
    • 84877926082 scopus 로고    scopus 로고
    • Physicochemical and functional properties of protein concentrates from pulses
    • Toews, R., and Wang, N. 2013. Physicochemical and functional properties of protein concentrates from pulses. Food Res. Int. 52:445-451.
    • (2013) Food Res. Int , vol.52 , pp. 445-451
    • Toews, R.1    Wang, N.2
  • 42
    • 79952752991 scopus 로고    scopus 로고
    • Physiochemical, thermal and functional characterization of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): A comparative study with soy (Glycine max) and pea (Pisum sativum L.)
    • Withana-Gamage, T. S., Wanasundara, J. P. D., Pietrasik, Z., and Shand, P. J. 2011. Physiochemical, thermal and functional characterization of protein isolates from Kabuli and Desi chickpea (Cicer arietinum L.): A comparative study with soy (Glycine max) and pea (Pisum sativum L.). J. Sci. Food Agric. 91:1022-1031.
    • (2011) J. Sci. Food Agric , vol.91 , pp. 1022-1031
    • Withana-Gamage, T.S.1    Wanasundara, J.P.D.2    Pietrasik, Z.3    Shand, P.J.4
  • 43
    • 0038315338 scopus 로고    scopus 로고
    • A comparison of the buttermilk solids functional properties to nonfat dried milk, soy protein isolate, dried egg white, and egg yolk powders
    • Wong, P. Y. Y., and Kitts, D. D. 2003. A comparison of the buttermilk solids functional properties to nonfat dried milk, soy protein isolate, dried egg white, and egg yolk powders. J. Dairy Sci. 86: 746-754.
    • (2003) J. Dairy Sci , vol.86 , pp. 746-754
    • Wong, P.Y.Y.1    Kitts, D.D.2
  • 45
    • 65849415996 scopus 로고    scopus 로고
    • Foams prepared from whey protein isolate and egg white protein: 1. Physical, microstructural, and interfacial properties
    • Yang, X., Berry, T. K., and Foegeding, E. A. 2009. Foams prepared from whey protein isolate and egg white protein: 1. Physical, microstructural, and interfacial properties. J. Food Sci. 74:E259-E268.
    • (2009) J. Food Sci , vol.74 , pp. E259-E268
    • Yang, X.1    Berry, T.K.2    Foegeding, E.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.