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Volumn 48, Issue 2, 2012, Pages 520-527

Formation of electrostatic complexes involving mixtures of lentil protein isolates and gum Arabic polysaccharides

Author keywords

Associative phase separation; Complex coacervation; Gum Arabic; Lentil protein isolates

Indexed keywords

ACID TITRATION; COMPLEX COACERVATION; COMPLEX FORMATIONS; DESTABILIZING AGENTS; ELECTROSTATIC ATTRACTIVE FORCES; ELECTROSTATIC COMPLEXES; ELEVATED TEMPERATURE; GUM ARABIC; HYDROPHOBIC INTERACTIONS; INSOLUBLE COMPLEXES; ISO-ELECTRIC POINTS; MIXING RATIOS; PH-DEPENDENT; PROTEIN ISOLATES; SURFACE HYDROPHOBICITY; TURBIDIMETRIC ANALYSIS;

EID: 84862158139     PISSN: 09639969     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodres.2012.05.012     Document Type: Article
Times cited : (79)

References (49)
  • 1
    • 0034641186 scopus 로고    scopus 로고
    • Interactions and compatibility of ribuloso-1,5-bisphosphate carboxylase/oxygenase from alfalfa with pectin in aqueous medium
    • Antonov Y.A., Soshinsky A. Interactions and compatibility of ribuloso-1,5-bisphosphate carboxylase/oxygenase from alfalfa with pectin in aqueous medium. International Journal of Biological Macromolecules 2000, 27:279-285.
    • (2000) International Journal of Biological Macromolecules , vol.27 , pp. 279-285
    • Antonov, Y.A.1    Soshinsky, A.2
  • 2
    • 0004202155 scopus 로고    scopus 로고
    • Association of Official Analytical Chemists, Washington, DC, AOAC
    • AOAC Official methods of analysis 1995, Association of Official Analytical Chemists, Washington, DC. 16 ed.
    • (1995) Official methods of analysis
  • 3
    • 0004202155 scopus 로고    scopus 로고
    • Association of Official Analytical Chemists, Washington, DC, AOAC
    • AOAC Official methods of analysis 2003, Association of Official Analytical Chemists, Washington, DC. 17 ed.
    • (2003) Official methods of analysis
  • 4
    • 77956738783 scopus 로고    scopus 로고
    • Effect of ionic strength on surface-selective patch binding-induced phase separation and coacervation in similarly charged gelatin-agar molecular systems
    • Boral S., Bohidar H.B. Effect of ionic strength on surface-selective patch binding-induced phase separation and coacervation in similarly charged gelatin-agar molecular systems. The Journal of Physical Chemistry. B 2010, 114:12027-12035.
    • (2010) The Journal of Physical Chemistry. B , vol.114 , pp. 12027-12035
    • Boral, S.1    Bohidar, H.B.2
  • 5
    • 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., Aksay S., Roufik S., Ribéreau S., Mondor M., Farnworth E., et al. Comparison of the functional properties of pea, chickpea and lentil protein concentrates processed using ultrafiltration and isoelectric precipitation techniques. Food Research International 2010, 43:537-546.
    • (2010) Food Research International , vol.43 , pp. 537-546
    • Boye, J.I.1    Aksay, S.2    Roufik, S.3    Ribéreau, S.4    Mondor, M.5    Farnworth, E.6
  • 6
    • 75149128950 scopus 로고    scopus 로고
    • Pulse proteins: processing, characterization, functional properties and applications in food and feed
    • Boye J., Zare F., Pletch A. Pulse proteins: processing, characterization, functional properties and applications in food and feed. Food Research International 2010, 43:414-431.
    • (2010) Food Research International , vol.43 , pp. 414-431
    • Boye, J.1    Zare, F.2    Pletch, A.3
  • 7
    • 80054693820 scopus 로고    scopus 로고
    • Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction
    • Can Karaca A., Low N., Nickerson M. Emulsifying properties of chickpea, faba bean, lentil and pea proteins produced by isoelectric precipitation and salt extraction. Food Research International 2011, 44:2742-2750.
    • (2011) Food Research International , vol.44 , pp. 2742-2750
    • Can Karaca, A.1    Low, N.2    Nickerson, M.3
  • 8
    • 33749559429 scopus 로고    scopus 로고
    • Conformational modifications of α-gliadin and globulin proteins upon complex coacervates formation with gum Arabic as studied by Raman microspectroscopy
    • Chourpa I., Ducel V., Richard J., Dubois O., Boury F. Conformational modifications of α-gliadin and globulin proteins upon complex coacervates formation with gum Arabic as studied by Raman microspectroscopy. Biomacromolecules 2006, 7:2616-2623.
    • (2006) Biomacromolecules , vol.7 , pp. 2616-2623
    • Chourpa, I.1    Ducel, V.2    Richard, J.3    Dubois, O.4    Boury, F.5
  • 9
    • 0006341159 scopus 로고    scopus 로고
    • Influence of κ-carrageenan on the properties of a protein-stabilized emulsion
    • Dickinson E., Pawlowsky K. Influence of κ-carrageenan on the properties of a protein-stabilized emulsion. Food Hydrocolloids 1998, 12:417-423.
    • (1998) Food Hydrocolloids , vol.12 , pp. 417-423
    • Dickinson, E.1    Pawlowsky, K.2
  • 14
    • 0036838148 scopus 로고    scopus 로고
    • Interbiopolymer complexing between β-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration
    • Girard M., Turgeon S.L., Gauthier S.F. Interbiopolymer complexing between β-lactoglobulin and low- and high-methylated pectin measured by potentiometric titration and ultrafiltration. Food Hydrocolloids 2002, 16:585-591.
    • (2002) Food Hydrocolloids , vol.16 , pp. 585-591
    • Girard, M.1    Turgeon, S.L.2    Gauthier, S.F.3
  • 15
    • 34548590740 scopus 로고    scopus 로고
    • Surface patch binding induced intermolecular complexation and phase separation in aqueous solutions of similarly charged gelatin-chitosan molecules
    • Gupta A.N., Hohidar H.B., Aswal V.K. Surface patch binding induced intermolecular complexation and phase separation in aqueous solutions of similarly charged gelatin-chitosan molecules. The Journal of Physical Chemistry. B 2007, 111:1137-10145.
    • (2007) The Journal of Physical Chemistry. B , vol.111 , pp. 1137-10145
    • Gupta, A.N.1    Hohidar, H.B.2    Aswal, V.K.3
  • 17
    • 0034158011 scopus 로고    scopus 로고
    • PH-induced coacervation in complexes of bovine serum albumin and cationic polyelectrolytes
    • Kaibara K., Okazaki T., Bohidar H.B., Dubin P.L. pH-induced coacervation in complexes of bovine serum albumin and cationic polyelectrolytes. Biomacromolecules 2000, 1:100-107.
    • (2000) Biomacromolecules , vol.1 , pp. 100-107
    • Kaibara, K.1    Okazaki, T.2    Bohidar, H.B.3    Dubin, P.L.4
  • 18
    • 0019331914 scopus 로고
    • Hydrophobicity determined by fluorescence probe methods and its correlation with surface properties of proteins
    • Kato A., Nakai S. Hydrophobicity determined by fluorescence probe methods 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
  • 19
    • 78751569666 scopus 로고    scopus 로고
    • Associative phase separation involving canola protein isolate with both sulphated and carboxylated polysaccharides
    • Klassen D.R., Elmer C.M., Nickerson M.T. Associative phase separation involving canola protein isolate with both sulphated and carboxylated polysaccharides. Food Chemistry 2011, 126:1094-1101.
    • (2011) Food Chemistry , vol.126 , pp. 1094-1101
    • Klassen, D.R.1    Elmer, C.M.2    Nickerson, M.T.3
  • 20
    • 80052739097 scopus 로고    scopus 로고
    • Complex coacervation of pea protein isolate and alginate polysaccharides
    • Klemmer K.J., Waldner L., Stone A., Low N.H., Nickerson M.T. Complex coacervation of pea protein isolate and alginate polysaccharides. Food Chemistry 2012, 130:710-715.
    • (2012) Food Chemistry , vol.130 , pp. 710-715
    • Klemmer, K.J.1    Waldner, L.2    Stone, A.3    Low, N.H.4    Nickerson, M.T.5
  • 21
    • 0028366358 scopus 로고
    • Determination of tryptophan in feedstuffs: Comparison of sodium hydroxide and barium hydroxide as hydrolysing agents
    • Landry J., Delhaye S. Determination of tryptophan in feedstuffs: Comparison of sodium hydroxide and barium hydroxide as hydrolysing agents. Food Chemistry 1993, 49:95-97.
    • (1993) Food Chemistry , vol.49 , pp. 95-97
    • Landry, J.1    Delhaye, S.2
  • 22
    • 33846563050 scopus 로고    scopus 로고
    • Chemical and functional quality of protein isolated from alkaline extraction of Australian lentil cultivars: Matilda and Digger
    • Lee H.C., Htoon A.K., Uthayakumaran S., Paterson J.L. Chemical and functional quality of protein isolated from alkaline extraction of Australian lentil cultivars: Matilda and Digger. Food Chemistry 2007, 102:1199-1207.
    • (2007) Food Chemistry , vol.102 , pp. 1199-1207
    • Lee, H.C.1    Htoon, A.K.2    Uthayakumaran, S.3    Paterson, J.L.4
  • 25
    • 75149117226 scopus 로고    scopus 로고
    • Effect of pH on the functional behaviour of pea protein isolate-gum Arabic complexes
    • Liu S., Elmer C., Low N.H., Nickerson M.T. Effect of pH on the functional behaviour of pea protein isolate-gum Arabic complexes. Food Research International 2010, 43:489-495.
    • (2010) Food Research International , vol.43 , pp. 489-495
    • Liu, S.1    Elmer, C.2    Low, N.H.3    Nickerson, M.T.4
  • 26
    • 64549148052 scopus 로고    scopus 로고
    • Effect of pH, salt and biopolymer ratio on the formation of pea protein isolate-gum Arabic complexes
    • Liu S., Low N.H., Nickerson M.T. Effect of pH, salt and biopolymer ratio on the formation of pea protein isolate-gum Arabic complexes. Journal of Agricultural and Food Chemistry 2009, 57:1521-1526.
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , pp. 1521-1526
    • Liu, S.1    Low, N.H.2    Nickerson, M.T.3
  • 27
    • 34347252586 scopus 로고    scopus 로고
    • The effect of heating on β-lactoglobulin-chitosan mixtures as influenced by pH and ionic strength
    • Mounsey J.S., O'Kennedy B.T., Fenelon M.A., Brodkorb A. The effect of heating on β-lactoglobulin-chitosan mixtures as influenced by pH and ionic strength. Food Hydrocolloids 2008, 22:65-73.
    • (2008) Food Hydrocolloids , vol.22 , pp. 65-73
    • Mounsey, J.S.1    O'Kennedy, B.T.2    Fenelon, M.A.3    Brodkorb, A.4
  • 28
    • 51049087218 scopus 로고    scopus 로고
    • Influence of preparation methods on physicochemical and gelation properties of chickpea protein isolates
    • Papalamprou E.M., Doxastakis G.I., Biliaderis C.G., Kiosseoglou V. Influence of preparation methods on physicochemical and gelation properties of chickpea protein isolates. Food Hydrocolloids 2009, 23:337-343.
    • (2009) Food Hydrocolloids , vol.23 , pp. 337-343
    • Papalamprou, E.M.1    Doxastakis, G.I.2    Biliaderis, C.G.3    Kiosseoglou, V.4
  • 29
    • 0002050733 scopus 로고
    • Soy proteins
    • Applied Science Publishers, London, B.J.F. Hudson (Ed.)
    • Pearson A.M. Soy proteins. Developments in food proteins 1983, 67-108. Applied Science Publishers, London. B.J.F. Hudson (Ed.).
    • (1983) Developments in food proteins , pp. 67-108
    • Pearson, A.M.1
  • 30
    • 75149190029 scopus 로고    scopus 로고
    • Bioactive proteins and peptides in pulse crops: Pea, chickpea and lentil
    • Roy F., Boye J.I., Simpson B.K. Bioactive proteins and peptides in pulse crops: Pea, chickpea and lentil. Food Research International 2010, 43:432-442.
    • (2010) Food Research International , vol.43 , pp. 432-442
    • Roy, F.1    Boye, J.I.2    Simpson, B.K.3
  • 32
    • 0000061602 scopus 로고    scopus 로고
    • Complex coacervation between β-lactoglobulin and acacia gum in aqueous medium
    • Schmitt C., Sanchez C., Thomas F., Hardy J. Complex coacervation between β-lactoglobulin and acacia gum in aqueous medium. Food Hydrocolloids 1999, 13:483-496.
    • (1999) Food Hydrocolloids , vol.13 , pp. 483-496
    • Schmitt, C.1    Sanchez, C.2    Thomas, F.3    Hardy, J.4
  • 35
    • 80155211192 scopus 로고    scopus 로고
    • Formation and functionality of whey protein isolate-(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes
    • Stone A.K., Nickerson M.T. Formation and functionality of whey protein isolate-(kappa-, iota-, and lambda-type) carrageenan electrostatic complexes. Food Hydrocolloids 2012, 27:271-277.
    • (2012) Food Hydrocolloids , vol.27 , pp. 271-277
    • Stone, A.K.1    Nickerson, M.T.2
  • 37
    • 85025569807 scopus 로고
    • Functional properties of food proteins and role of protein-polysaccharide interaction
    • Tolstoguzov V.B. Functional properties of food proteins and role of protein-polysaccharide interaction. Food Hydrocolloids 1991, 4:429-468.
    • (1991) Food Hydrocolloids , vol.4 , pp. 429-468
    • Tolstoguzov, V.B.1
  • 39
    • 17644362353 scopus 로고    scopus 로고
    • Emulsifying characteristics of commercial canola protein-hydrocolloid systems
    • Uruakpa F.O., Arntfield S.D. Emulsifying characteristics of commercial canola protein-hydrocolloid systems. Food Research International 2005, 38:659-672.
    • (2005) Food Research International , vol.38 , pp. 659-672
    • Uruakpa, F.O.1    Arntfield, S.D.2
  • 40
    • 25144503257 scopus 로고    scopus 로고
    • Surface hydrophobicity of commercial canola proteins mixed with κ-carrageenan or guar gum
    • Uruakpa F.O., Arntfield S.D. Surface hydrophobicity of commercial canola proteins mixed with κ-carrageenan or guar gum. Food Chemistry 2006, 95:255-263.
    • (2006) Food Chemistry , vol.95 , pp. 255-263
    • Uruakpa, F.O.1    Arntfield, S.D.2
  • 41
    • 33645959501 scopus 로고    scopus 로고
    • Impact of urea on the microstructure of commercial canola protein-carrageenan network: A research note
    • Uruakpa F.O., Arntfield S.D. Impact of urea on the microstructure of commercial canola protein-carrageenan network: A research note. International of Biological Macromolecules 2006, 38:115-119.
    • (2006) International of Biological Macromolecules , vol.38 , pp. 115-119
    • Uruakpa, F.O.1    Arntfield, S.D.2
  • 42
    • 80052436861 scopus 로고    scopus 로고
    • A review of the early developments in thermodynamic of complex coacervation phase separation
    • Veis A. A review of the early developments in thermodynamic of complex coacervation phase separation. Advances in Colloid and Interfacial Science 2011, 167:2-11.
    • (2011) Advances in Colloid and Interfacial Science , vol.167 , pp. 2-11
    • Veis, A.1
  • 43
    • 27744562666 scopus 로고    scopus 로고
    • Optimization of laboratory dehulling process for lentil (Lens culinaris)
    • Wang N. Optimization of laboratory dehulling process for lentil (Lens culinaris). Cereal Chemistry 2005, 82:671-676.
    • (2005) Cereal Chemistry , vol.82 , pp. 671-676
    • Wang, N.1
  • 45
    • 0242576090 scopus 로고    scopus 로고
    • Complex formation of whey proteins: Exocellular polysaccharide EPS B40
    • Weinbreck F., Nieuwenhuijse H., Robijn G.W., de Kruif C.G. Complex formation of whey proteins: Exocellular polysaccharide EPS B40. Langmuir 2003, 19:9404-9410.
    • (2003) Langmuir , vol.19 , pp. 9404-9410
    • Weinbreck, F.1    Nieuwenhuijse, H.2    Robijn, G.W.3    de Kruif, C.G.4
  • 48
    • 0023009833 scopus 로고
    • An evaluation of the waters pico-tag system for the amino-acid analysis of food materials
    • White J.A., Hart R.J., Fry J.C. An evaluation of the waters pico-tag system for the amino-acid analysis of food materials. Journal of Automatic Chemistry 1986, 8:170-177.
    • (1986) Journal of Automatic Chemistry , vol.8 , pp. 170-177
    • White, J.A.1    Hart, R.J.2    Fry, J.C.3
  • 49
    • 38749097811 scopus 로고    scopus 로고
    • Complexation between milk proteins and polysaccharides via electrostatic interaction: Principles and applications - A review
    • Ye A. Complexation between milk proteins and polysaccharides via electrostatic interaction: Principles and applications - A review. International Journal of Food and Technology 2008, 43:406-415.
    • (2008) International Journal of Food and Technology , vol.43 , pp. 406-415
    • Ye, A.1


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