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Volumn 77, Issue , 2018, Pages 75-84

The rheological and microstructural properties of pea, milk, mixed pea/milk gels and gelled emulsions designed by thermal, acid, and enzyme treatments

Author keywords

Confocal microscopy; Dairy products; Gels; Plant protein; Rheology

Indexed keywords

ENZYMES; FOOD PRODUCTS; FOOD STORAGE; GELATION;

EID: 85031322411     PISSN: 0268005X     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.foodhyd.2017.09.022     Document Type: Article
Times cited : (122)

References (36)
  • 1
    • 79951945134 scopus 로고    scopus 로고
    • Future protein supply
    • Aiking, H., Future protein supply. Trends in Food Science & Technology 22 (2011), 112–120, 10.1016/j.tifs.2010.04.005.
    • (2011) Trends in Food Science & Technology , vol.22 , pp. 112-120
    • Aiking, H.1
  • 2
    • 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 43 (2010), 537–546, 10.1016/j.foodres.2009.07.021.
    • (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
  • 3
    • 0033827807 scopus 로고    scopus 로고
    • Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein
    • Bryant, C.M., McClements, D.J., Influence of NaCl and CaCl2 on cold-set gelation of heat-denatured whey protein. Journal of Food Science 65 (2000), 801–804.
    • (2000) Journal of Food Science , vol.65 , pp. 801-804
    • Bryant, C.M.1    McClements, D.J.2
  • 4
    • 84964409730 scopus 로고    scopus 로고
    • Heat-induced soluble protein aggregates from mixed pea globulins and β-lactoglobulin
    • Chihi, M.-L., Mession, J., 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, 10.1021/acs.jafc.6b00087.
    • (2016) Journal of Agricultural and Food Chemistry , vol.64 , pp. 2780-2791
    • Chihi, M.-L.1    Mession, J.2    Sok, N.3    Saurel, R.4
  • 6
    • 0000298096 scopus 로고    scopus 로고
    • Properties of emulsions stabilized with milk proteins: Overview of some recent developments
    • Dickinson, E., Properties of emulsions stabilized with milk proteins: Overview of some recent developments. Journal of Dairy Science 80 (1997), 2607–2619.
    • (1997) Journal of Dairy Science , vol.80 , pp. 2607-2619
    • Dickinson, E.1
  • 7
    • 84933278260 scopus 로고    scopus 로고
    • Native-state pea albumin and globulin behavior upon transglutaminase treatment
    • Djoullah, A., Djemaoune, Y., Husson, F., Saurel, R., Native-state pea albumin and globulin behavior upon transglutaminase treatment. Process Biochemistry 50 (2015), 1284–1292, 10.1016/j.procbio.2015.04.021.
    • (2015) Process Biochemistry , vol.50 , pp. 1284-1292
    • Djoullah, A.1    Djemaoune, Y.2    Husson, F.3    Saurel, R.4
  • 8
    • 84930226204 scopus 로고    scopus 로고
    • Size measuring techniques as tool to monitor pea proteins intramolecular crosslinking by transglutaminase treatment
    • Djoullah, A., Krechiche, G., Husson, F., Saurel, R., Size measuring techniques as tool to monitor pea proteins intramolecular crosslinking by transglutaminase treatment. Food Chemistry 190 (2016), 197–200, 10.1016/j.foodchem.2015.05.091.
    • (2016) Food Chemistry , vol.190 , pp. 197-200
    • Djoullah, A.1    Krechiche, G.2    Husson, F.3    Saurel, R.4
  • 9
    • 84907221129 scopus 로고    scopus 로고
    • Action of microbial transglutaminase (MTGase) in the modification of food proteins: A review
    • Gaspar, A.L.C., de Góes-Favoni, S.P., Action of microbial transglutaminase (MTGase) in the modification of food proteins: A review. Food Chemistry 171 (2015), 315–322, 10.1016/j.foodchem.2014.09.019.
    • (2015) Food Chemistry , vol.171 , pp. 315-322
    • Gaspar, A.L.C.1    de Góes-Favoni, S.P.2
  • 12
    • 84957433472 scopus 로고    scopus 로고
    • Pea, chickpea and lentil protein Isolates: Physicochemical characterization and emulsifying properties
    • Ladjal-Ettoumi, Y., Boudries, H., Chibane, M., Romero, A., Pea, chickpea and lentil protein Isolates: Physicochemical characterization and emulsifying properties. Food Biophysics 11 (2016), 43–51, 10.1007/s11483-015-9411-6.
    • (2016) Food Biophysics , vol.11 , pp. 43-51
    • Ladjal-Ettoumi, Y.1    Boudries, H.2    Chibane, M.3    Romero, A.4
  • 13
    • 84870732630 scopus 로고    scopus 로고
    • Gelation of mixtures of soymilk and reconstituted skim milk subjected to combined acid and rennet
    • Lin, C., Hill, A., Corredig, M., Gelation of mixtures of soymilk and reconstituted skim milk subjected to combined acid and rennet. Journal of Texture Studies 43 (2012), 468–476, 10.1111/j.1745-4603.2012.00357.x.
    • (2012) Journal of Texture Studies , vol.43 , pp. 468-476
    • Lin, C.1    Hill, A.2    Corredig, M.3
  • 14
    • 0031200770 scopus 로고    scopus 로고
    • Formation and physical properties of acid milk gels: A review
    • Lucey, J.A., Singh, H., Formation and physical properties of acid milk gels: A review. Food Research Iniernational 30 (1998), 529–542.
    • (1998) Food Research Iniernational , vol.30 , pp. 529-542
    • Lucey, J.A.1    Singh, H.2
  • 15
    • 84960111522 scopus 로고    scopus 로고
    • Modulating the aggregation behaviour to restore the mechanical response of acid induced mixed gels of sodium caseinate and soy proteins
    • Martin, A.H., de los Reyes Jiménez, M.L., Pouvreau, L., Modulating the aggregation behaviour to restore the mechanical response of acid induced mixed gels of sodium caseinate and soy proteins. Food Hydrocolloids 58 (2016), 215–223, 10.1016/j.foodhyd.2016.02.029.
    • (2016) Food Hydrocolloids , vol.58 , pp. 215-223
    • Martin, A.H.1    de los Reyes Jiménez, M.L.2    Pouvreau, L.3
  • 16
    • 84951325942 scopus 로고    scopus 로고
    • Dairy proteins and soy proteins in infant foods nitrogen-to-protein conversion factors
    • Maubois, J.-L., Lorient, D., Dairy proteins and soy proteins in infant foods nitrogen-to-protein conversion factors. Dairy Science & Technology 96 (2016), 15–25, 10.1007/s13594-015-0271-0.
    • (2016) Dairy Science & Technology , vol.96 , pp. 15-25
    • Maubois, J.-L.1    Lorient, D.2
  • 17
    • 84860604080 scopus 로고    scopus 로고
    • Effect of pea proteins extraction and vicilin/legumin fractionation on the phase behavior 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 behavior in admixture with alginate. Food Hydrocolloids 29 (2012), 335–346, 10.1016/j.foodhyd.2012.03.003.
    • (2012) Food Hydrocolloids , vol.29 , pp. 335-346
    • Mession, J.-L.1    Assifaoui, A.2    Cayot, P.3    Saurel, R.4
  • 18
    • 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, 10.1016/j.foodhyd.2014.11.025.
    • (2015) Food Hydrocolloids , vol.46 , pp. 233-243
    • Mession, J.-L.1    Chihi, M.L.2    Sok, N.3    Saurel, R.4
  • 19
    • 84926365781 scopus 로고    scopus 로고
    • Quantitative analysis of the network structure that underlines the transitioning in mechanical responses of pea protein gels
    • Munialo, C.D., van der Linden, E., Ako, K., de Jongh, H.H.J., Quantitative analysis of the network structure that underlines the transitioning in mechanical responses of pea protein gels. Food Hydrocolloids 49 (2015), 104–117, 10.1016/j.foodhyd.2015.03.018.
    • (2015) Food Hydrocolloids , vol.49 , pp. 104-117
    • Munialo, C.D.1    van der Linden, E.2    Ako, K.3    de Jongh, H.H.J.4
  • 20
    • 84905647434 scopus 로고    scopus 로고
    • The ability to store energy in pea protein gels is set by network dimensions smaller than 50 nm
    • Munialo, C.D., van der Linden, E., de Jongh, H.H.J., The ability to store energy in pea protein gels is set by network dimensions smaller than 50 nm. Food Research International 64 (2014), 482–491, 10.1016/j.foodres.C2014.07.038.
    • (2014) Food Research International , vol.64 , pp. 482-491
    • Munialo, C.D.1    van der Linden, E.2    de Jongh, H.H.J.3
  • 22
    • 84907180879 scopus 로고    scopus 로고
    • Functional analysis of mildly refined fractions from yellow pea
    • Pelgrom, P.J.M., Boom, R.M., Schutyser, M.A.I., Functional analysis of mildly refined fractions from yellow pea. Food Hydrocolloids 44 (2015), 12–22, 10.1016/j.foodhyd.2014.09.001.
    • (2015) Food Hydrocolloids , vol.44 , pp. 12-22
    • Pelgrom, P.J.M.1    Boom, R.M.2    Schutyser, M.A.I.3
  • 23
    • 0043286245 scopus 로고    scopus 로고
    • Sustainability of meat-based and plant-based diets and the environment
    • Pimentel, D., Pimentel, M., Sustainability of meat-based and plant-based diets and the environment. American Journal of Clinical Nutrition 78 (2003), 660S–663S.
    • (2003) American Journal of Clinical Nutrition , vol.78 , pp. 660S-663S
    • Pimentel, D.1    Pimentel, M.2
  • 24
    • 0043065429 scopus 로고    scopus 로고
    • Molecular mechanisms of Fe2+-induced β-lactoglobulin cold gelation
    • Remondetto, G.E., Subirade, M., Molecular mechanisms of Fe2+-induced β-lactoglobulin cold gelation. Biopolymers 69 (2003), 461–469.
    • (2003) Biopolymers , vol.69 , pp. 461-469
    • Remondetto, G.E.1    Subirade, M.2
  • 25
    • 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, 10.1021/jf048870d.
    • (2005) Journal of Agricultural and Food Chemistry , vol.53 , pp. 3476-3482
    • Roesch, R.R.1    Corredig, M.2
  • 26
  • 27
    • 84903853228 scopus 로고    scopus 로고
    • Sustainability of plant-based diets: Back to the future
    • Sabate, J., Soret, S., Sustainability of plant-based diets: Back to the future. American Journal of Clinical Nutrition 100 (2014), 476S–482S, 10.3945/ajcn.113.071522.
    • (2014) American Journal of Clinical Nutrition , vol.100 , pp. 476S-482S
    • Sabate, J.1    Soret, S.2
  • 28
    • 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, 10.1016/j.foodchem.2006.06.060.
    • (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
  • 29
    • 36148929800 scopus 로고    scopus 로고
    • Transglutaminase treatment of pea proteins: Effect on physicochemical and rheological properties of heat-induced protein gels
    • Shand, P.J., Ya, H., Pietrasik, Z., Wanasundara, P.K.J.P.D., Transglutaminase treatment of pea proteins: Effect on physicochemical and rheological properties of heat-induced protein gels. Food Chemistry 107 (2008), 692–699, 10.1016/j.foodchem.2007.08.095.
    • (2008) Food Chemistry , vol.107 , pp. 692-699
    • Shand, P.J.1    Ya, H.2    Pietrasik, Z.3    Wanasundara, P.K.J.P.D.4
  • 30
    • 75149183532 scopus 로고    scopus 로고
    • Gelation properties of salt-extracted pea protein induced by heat treatment
    • Sun, X.D., Arntfield, S.D., Gelation properties of salt-extracted pea protein induced by heat treatment. Food Research International 43 (2010), 509–515, 10.1016/j.foodres.2009.09.039.
    • (2010) Food Research International , vol.43 , pp. 509-515
    • Sun, X.D.1    Arntfield, S.D.2
  • 31
    • 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, 10.1016/j.foodchem.2010.07.063.
    • (2011) Food Chemistry , vol.124 , pp. 1011-1016
    • Sun, X.D.1    Arntfield, S.D.2
  • 32
    • 77957774479 scopus 로고    scopus 로고
    • Gelation properties of salt-extracted pea protein isolate catalyzed by microbial transglutaminase cross-linking
    • Sun, X.D., Arntfield, S.D., Gelation properties of salt-extracted pea protein isolate catalyzed by microbial transglutaminase cross-linking. Food Hydrocolloids 25 (2011), 25–31, 10.1016/j.foodhyd.2010.05.002.
    • (2011) Food Hydrocolloids , vol.25 , pp. 25-31
    • Sun, X.D.1    Arntfield, S.D.2
  • 33
    • 84863252501 scopus 로고    scopus 로고
    • Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels
    • Sun, X.D., Arntfield, S.D., Molecular forces involved in heat-induced pea protein gelation: Effects of various reagents on the rheological properties of salt-extracted pea protein gels. Food Hydrocolloids 28 (2012), 325–332, 10.1016/j.foodhyd.2011.12.014.
    • (2012) Food Hydrocolloids , vol.28 , pp. 325-332
    • Sun, X.D.1    Arntfield, S.D.2
  • 34
    • 84934907445 scopus 로고    scopus 로고
    • Interaction of selected volatile flavour compounds and salt-extracted pea proteins: Effect on protein structure and thermal-induced gelation properties
    • Wang, K., Arntfield, S.D., Interaction of selected volatile flavour compounds and salt-extracted pea proteins: Effect on protein structure and thermal-induced gelation properties. Food Hydrocolloids 51 (2015), 383–394, 10.1016/j.foodhyd.2015.05.044.
    • (2015) Food Hydrocolloids , vol.51 , pp. 383-394
    • Wang, K.1    Arntfield, S.D.2
  • 35
    • 84884601077 scopus 로고    scopus 로고
    • Synergistic enhancement in the co-gelation of salt-soluble pea proteins and whey proteins
    • Wong, D., Vasanthan, T., Ozimek, L., Synergistic enhancement in the co-gelation of salt-soluble pea proteins and whey proteins. Food Chemistry 141 (2013), 3913–3919, 10.1016/j.foodchem.2013.05.082.
    • (2013) Food Chemistry , vol.141 , pp. 3913-3919
    • Wong, D.1    Vasanthan, T.2    Ozimek, L.3
  • 36
    • 84959896140 scopus 로고    scopus 로고
    • Fermentation of cow milk and/or pea milk mixtures by different starter cultures: Physico-chemical and sensorial properties
    • Yousseef, M., Lafarge, C., Valentin, D., Lubbers, S., Husson, F., Fermentation of cow milk and/or pea milk mixtures by different starter cultures: Physico-chemical and sensorial properties. LWT - Food Science and Technology 69 (2016), 430–437, 10.1016/j.lwt.2016.01.060.
    • (2016) LWT - Food Science and Technology , vol.69 , pp. 430-437
    • Yousseef, M.1    Lafarge, C.2    Valentin, D.3    Lubbers, S.4    Husson, F.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.