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Volumn 27, Issue 5, 2016, Pages 604-623

Comparative study of four physical approaches about allergenicity of soybean protein isolate for infant formula

Author keywords

allergenicity; high hydrostatic pressure; high intensity ultrasound; high pressure homogenization; Microwaving; SPI for infant formula

Indexed keywords


EID: 84953279795     PISSN: 09540105     EISSN: 14653443     Source Type: Journal    
DOI: 10.1080/09540105.2015.1129602     Document Type: Article
Times cited : (49)

References (54)
  • 1
    • 80054951068 scopus 로고    scopus 로고
    • Comparative study of high intensity ultrasound effects on food proteins functionality
    • C.Arzeni, K.Martinez, P.Zema, A.Arias, O.E.Pérez, & A.M.R.Pilosof, (2012). Comparative study of high intensity ultrasound effects on food proteins functionality. Journal of Food Engineering, 108, 463–472. doi:10.1016/j.jfoodeng.2011.08.018
    • (2012) Journal of Food Engineering , vol.108 , pp. 463-472
    • Arzeni, C.1    Martinez, K.2    Zema, P.3    Arias, A.4    Pérez, O.E.5    Pilosof, A.M.R.6
  • 2
    • 85032119438 scopus 로고
    • Determination of SH- and SS-groups in some food proteins using Ellman's reagent
    • T.Beveridge, S.J.Toma, & S.Nakai, (1974). Determination of SH- and SS-groups in some food proteins using Ellman's reagent. Journal of Food Science, 39, 49–51. doi:10.1111/j.1365-2621.1974.tb00984.x
    • (1974) Journal of Food Science , vol.39 , pp. 49-51
    • Beveridge, T.1    Toma, S.J.2    Nakai, S.3
  • 3
    • 44449105160 scopus 로고    scopus 로고
    • The Committee on Nutrition. Use of soy protein-based formulas in infant feeding
    • J.Bhatia, & F.Greer, (2008). The Committee on Nutrition. Use of soy protein-based formulas in infant feeding. Pediatrics, 121, 1062–1068. doi:10.1542/peds.2008-0564
    • (2008) Pediatrics , vol.121 , pp. 1062-1068
    • Bhatia, J.1    Greer, F.2
  • 4
    • 30344478568 scopus 로고    scopus 로고
    • Functional properties of whey proteins as affected by dynamic high-pressure treatment
    • H.Bouaouina, A.Desrumaux, C.Loisel, & J.Legrand, (2006). Functional properties of whey proteins as affected by dynamic high-pressure treatment. International Dairy Journal, 16, 275–284. doi:10.1016/j.idairyj.2005.05.004
    • (2006) International Dairy Journal , vol.16 , pp. 275-284
    • Bouaouina, H.1    Desrumaux, A.2    Loisel, C.3    Legrand, J.4
  • 5
    • 0017184389 scopus 로고
    • A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein–dye binding
    • M.M.Bradford, (1976). A rapid and sensitive method for quantitation of microgram quantities of protein utilizing the principle of protein–dye binding. Analytical Biochemistry, 72, 248–254. doi:10.1016/0003-2697(76)90527-3
    • (1976) Analytical Biochemistry , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 6
    • 2342525840 scopus 로고    scopus 로고
    • Classification of plant food allergens molecular mechanisms in allergy and clinical immunology
    • H.Breiteneder, & C.A.Radauer, (2004). Classification of plant food allergens molecular mechanisms in allergy and clinical immunology. Journal of Allergy and Clinical Immunology, 113, 821–830. doi:10.1016/j.jaci.2004.01.779
    • (2004) Journal of Allergy and Clinical Immunology , vol.113 , pp. 821-830
    • Breiteneder, H.1    Radauer, C.A.2
  • 7
    • 79956344900 scopus 로고    scopus 로고
    • Effects of ultrasound on the thermal and structural characteristics of proteins
    • J.Chandrapala, B.Zisu, M.Palmer, S.Kentish, & M.Ashokkumar, (2011). Effects of ultrasound on the thermal and structural characteristics of proteins. Ultrasonics Sonochemistry, 18, 951–957. doi:10.1016/j.ultsonch.2010.12.016
    • (2011) Ultrasonics Sonochemistry , vol.18 , pp. 951-957
    • Chandrapala, J.1    Zisu, B.2    Palmer, M.3    Kentish, S.4    Ashokkumar, M.5
  • 9
    • 33846850537 scopus 로고    scopus 로고
    • The challenge of cow milk protein allergy
    • E.I.El-Agamy, (2007). The challenge of cow milk protein allergy. Small Ruminant Research, 68, 64–72. doi:10.1016/j.smallrumres.2006.09.016
    • (2007) Small Ruminant Research , vol.68 , pp. 64-72
    • El-Agamy, E.I.1
  • 10
    • 0036868068 scopus 로고    scopus 로고
    • Effect of ultra-high pressure homogenization on structure and on rheological properties of soy protein stabilized emulsions
    • J.Floury, A.Desrumaux, & J.Legrand, (2002). Effect of ultra-high pressure homogenization on structure and on rheological properties of soy protein stabilized emulsions. Journal of Food Science, 67, 3388–3395. doi:10.1111/j.1365-2621.2002.tb09595.x
    • (2002) Journal of Food Science , vol.67 , pp. 3388-3395
    • Floury, J.1    Desrumaux, A.2    Legrand, J.3
  • 11
    • 0026060563 scopus 로고
    • Flexibility of globular proteins in water as revealed by compressibility
    • Levine H., Sla D.L., (eds), New York, NY: Plenum Press
    • K.Gekko, (1991). Flexibility of globular proteins in water as revealed by compressibility. In H.Levine, & D.L.Slade L. (Eds.), Water relationships in foods (pp. 753–771). New York, NY:Plenum Press.
    • (1991) Water relationships in foods , pp. 753-771
    • Gekko, K.1
  • 12
    • 70349980260 scopus 로고    scopus 로고
    • Microwave irradiation under different pH conditions induced a decrease in β-lactoglobulin antigenicity
    • H.Grar, H.Kaddouri, H.Gourine, H.Negaoui, O.Kheroua, & D.Saïdi, (2009). Microwave irradiation under different pH conditions induced a decrease in β-lactoglobulin antigenicity. European Food Research and Technology, 229, 779–783. doi:10.1007/s00217-009-1114-0
    • (2009) European Food Research and Technology , vol.229 , pp. 779-783
    • Grar, H.1    Kaddouri, H.2    Gourine, H.3    Negaoui, H.4    Kheroua, O.5    Saïdi, D.6
  • 13
    • 80054679001 scopus 로고    scopus 로고
    • Mechanism of microwave-accelerated soyprotein isolate–saccharide graft reactions
    • J.J.Guan, T.B.Zhang, M.Hui, H.C.Yin, A.Y.Qiu, & X.Y.Liu, (2011). Mechanism of microwave-accelerated soyprotein isolate–saccharide graft reactions. Food Research International, 44, 2647–2654. doi:10.1016/j.foodres.2011.05.015
    • (2011) Food Research International , vol.44 , pp. 2647-2654
    • Guan, J.J.1    Zhang, T.B.2    Hui, M.3    Yin, H.C.4    Qiu, A.Y.5    Liu, X.Y.6
  • 16
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • U.K.Laemmli, (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature, 227, 680–685. doi:10.1038/227680a0
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 17
    • 81255195782 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure on some functional and nutritional properties of soy protein isolate for infant formula
    • H.J.Li, K.X.Zhu, H.M.Zhou, & W.Peng, (2011). Effects of high hydrostatic pressure on some functional and nutritional properties of soy protein isolate for infant formula. Journal of Agricultural and Food Chemistry, 59, 12028–12036. doi:10.1021/jf203390e
    • (2011) Journal of Agricultural and Food Chemistry , vol.59 , pp. 12028-12036
    • Li, H.J.1    Zhu, K.X.2    Zhou, H.M.3    Peng, W.4
  • 18
    • 84855674654 scopus 로고    scopus 로고
    • Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula
    • H.J.Li, K.X.Zhu, H.M.Zhou, & W.Peng, (2012). Effects of high hydrostatic pressure treatment on allergenicity and structural properties of soybean protein isolate for infant formula. Food Chemistry, 132, 808–814. doi:10.1016/j.foodchem.2011.11.040
    • (2012) Food Chemistry , vol.132 , pp. 808-814
    • Li, H.J.1    Zhu, K.X.2    Zhou, H.M.3    Peng, W.4
  • 19
    • 34247211578 scopus 로고    scopus 로고
    • Effects of pulsed electric fields on physicochemical properties of soybean protein isolates
    • Y.Q.Li, Z.X.Chen, & H.Z.Mo, (2007). Effects of pulsed electric fields on physicochemical properties of soybean protein isolates. LWT – Food Science and Technology, 40, 1167–1175. doi:10.1016/j.lwt.2006.08.015
    • (2007) LWT – Food Science and Technology , vol.40 , pp. 1167-1175
    • Li, Y.Q.1    Chen, Z.X.2    Mo, H.Z.3
  • 20
    • 33746873662 scopus 로고    scopus 로고
    • Reduction of allergenic properties of shrimp (Penaeus vannamei) allergens by high intensity ultrasound
    • Z.X.Li, L.Caolimin, & K.Jamil, (2006). Reduction of allergenic properties of shrimp (Penaeus vannamei) allergens by high intensity ultrasound. European Food Research and Technology, 223, 639–644. doi:10.1007/s00217-005-0246-0
    • (2006) European Food Research and Technology , vol.223 , pp. 639-644
    • Li, Z.X.1    Caolimin, L.2    Jamil, K.3
  • 21
    • 60149099551 scopus 로고    scopus 로고
    • Activation and conformational changes of mushroom polyphenoloxidase by high pressure microfluidization treatment
    • W.Liu, J.H.Liu, C.M.Liu, Y.J.Zhong, W.L.Liu, & J.Wan, (2009). Activation and conformational changes of mushroom polyphenoloxidase by high pressure microfluidization treatment. Innovative Food Science & Emerging Technologies, 10, 142–147. doi:10.1016/j.ifset.2008.11.009
    • (2009) Innovative Food Science & Emerging Technologies , vol.10 , pp. 142-147
    • Liu, W.1    Liu, J.H.2    Liu, C.M.3    Zhong, Y.J.4    Liu, W.L.5    Wan, J.6
  • 23
    • 0031127640 scopus 로고    scopus 로고
    • The use of high pressure to modify the functionality of food proteins
    • W.Messens, J.Van Camp, & A.Huyghebaert, (1997). The use of high pressure to modify the functionality of food proteins. Trends in Food Science & Technology, 8, 107–112. doi:10.1016/S0924-2244(97)01015-7
    • (1997) Trends in Food Science & Technology , vol.8 , pp. 107-112
    • Messens, W.1    Van Camp, J.2    Huyghebaert, A.3
  • 24
    • 0037723037 scopus 로고    scopus 로고
    • Food allergens of plant origin – their molecular and evolutionary relationships
    • E.N.C.Mills, C.Madsen, P.R.Shewry, & H.J.Wichers, (2003). Food allergens of plant origin – their molecular and evolutionary relationships. Trends in Food Science & Technology, 14, 145–156. doi:10.1016/S0924-2244(03)00026-8
    • (2003) Trends in Food Science & Technology , vol.14 , pp. 145-156
    • Mills, E.N.C.1    Madsen, C.2    Shewry, P.R.3    Wichers, H.J.4
  • 25
    • 0035021485 scopus 로고    scopus 로고
    • Emulsifying properties of high pressure treated soy protein isolates and 7S and 11S globulins
    • E.Molina, A.Papadopoulou, & D.A.Ledward, (2001). Emulsifying properties of high pressure treated soy protein isolates and 7S and 11S globulins. Food Hydrocolloids, 15, 263–269. doi:10.1016/S0268-005X(01)00023-6
    • (2001) Food Hydrocolloids , vol.15 , pp. 263-269
    • Molina, E.1    Papadopoulou, A.2    Ledward, D.A.3
  • 27
    • 0028961335 scopus 로고
    • SCOP: A structural classification of proteins database for the investigation of sequences and structures
    • A.G.Murzin, S.E.Brenner, T.Hubbard, & C.Chothia, (1995). SCOP:A structural classification of proteins database for the investigation of sequences and structures. Journal of Molecular Biology, 247, 536–540.
    • (1995) Journal of Molecular Biology , vol.247 , pp. 536-540
    • Murzin, A.G.1    Brenner, S.E.2    Hubbard, T.3    Chothia, C.4
  • 29
    • 78049446254 scopus 로고    scopus 로고
    • High hydrostatic pressure effects on immunoreactivity and nutritional quality of soybean products
    • E.Peñas, R.Gomez, J.Frias, M.L.Baeza, & C.Vidal-Valverde, (2011). High hydrostatic pressure effects on immunoreactivity and nutritional quality of soybean products. Food Chemistry, 125, 423–429. doi:10.1016/j.foodchem.2010.09.023
    • (2011) Food Chemistry , vol.125 , pp. 423-429
    • Peñas, E.1    Gomez, R.2    Frias, J.3    Baeza, M.L.4    Vidal-Valverde, C.5
  • 30
    • 33646696127 scopus 로고    scopus 로고
    • Enzymatic proteolysis, under high pressure of soybean whey: Analysis of peptides and the allergen Gly m 1 in the hydrolysates
    • E.Peñas, G.Préstamo, F.Polo, & R.Gomez, (2006). Enzymatic proteolysis, under high pressure of soybean whey:Analysis of peptides and the allergen Gly m 1 in the hydrolysates. Food Chemistry, 99, 569–573. doi:10.1016/j.foodchem.2005.08.028
    • (2006) Food Chemistry , vol.99 , pp. 569-573
    • Peñas, E.1    Préstamo, G.2    Polo, F.3    Gomez, R.4
  • 31
    • 0001420837 scopus 로고
    • Unexpected frequency effects on the rate of oxidative processes induced by ultrasound
    • C.Petrier, A.Jeunet, J.L.Luche, & G.Reverdy, (1992). Unexpected frequency effects on the rate of oxidative processes induced by ultrasound. Journal of the American Chemical Society, 114, 3148–3150. doi:10.1021/ja00034a077
    • (1992) Journal of the American Chemical Society , vol.114 , pp. 3148-3150
    • Petrier, C.1    Jeunet, A.2    Luche, J.L.3    Reverdy, G.4
  • 33
    • 84980544615 scopus 로고    scopus 로고
    • Structure, allergenicity, and cross-reactivity of plant allergens
    • Falus A., (ed), New York, NY: Springer
    • C.Radauer, & H.Breiteneder, (2004). Structure, allergenicity, and cross-reactivity of plant allergens. In A.Falus (Ed.), Clinical applications of immunomics – immunomics reviews (pp. 127–151). New York, NY:Springer.
    • (2004) Clinical applications of immunomics – immunomics reviews , pp. 127-151
    • Radauer, C.1    Breiteneder, H.2
  • 34
    • 44649142111 scopus 로고    scopus 로고
    • Food allergy overview in children
    • S.Ramesh, (2008). Food allergy overview in children. Clinical Reviews in Allergy & Immunology, 34, 217–230. doi:10.1007/s12016-007-8034-1
    • (2008) Clinical Reviews in Allergy & Immunology , vol.34 , pp. 217-230
    • Ramesh, S.1
  • 37
    • 84859152164 scopus 로고    scopus 로고
    • Microfluidization as a potential technique to modify surface properties of soyprotein isolate
    • L.Shen, & C.H.Tang, (2012). Microfluidization as a potential technique to modify surface properties of soyprotein isolate. Food Research International, 48, 108–118. doi:10.1016/j.foodres.2012.03.006
    • (2012) Food Research International , vol.48 , pp. 108-118
    • Shen, L.1    Tang, C.H.2
  • 38
    • 79952489287 scopus 로고    scopus 로고
    • Thermal and nonthermal methods for food allergen control
    • S.K.Shriver, & W.W.Yang, (2011). Thermal and nonthermal methods for food allergen control. Food Engineering Reviews, 3, 26–43. doi:10.1007/s12393-011-9033-9
    • (2011) Food Engineering Reviews , vol.3 , pp. 26-43
    • Shriver, S.K.1    Yang, W.W.2
  • 40
    • 77954083367 scopus 로고    scopus 로고
    • Effect of ultrasound on the technological properties and bioactivity of food: A review
    • A.C.Soria, & M.Villamiel, (2010). Effect of ultrasound on the technological properties and bioactivity of food:A review. Trends in Food Science & Technology, 21, 323–331. doi:10.1016/j.tifs.2010.04.003
    • (2010) Trends in Food Science & Technology , vol.21 , pp. 323-331
    • Soria, A.C.1    Villamiel, M.2
  • 41
    • 1242265596 scopus 로고    scopus 로고
    • Effect of different denaturing methods on lipid-protein complex formation
    • F.S.Taha, & S.S.Mohamed, (2004). Effect of different denaturing methods on lipid-protein complex formation. LWT – Food Science and Technology, 37, 99–104. doi:10.1016/S0023-6438(03)00140-3
    • (2004) LWT – Food Science and Technology , vol.37 , pp. 99-104
    • Taha, F.S.1    Mohamed, S.S.2
  • 42
    • 84879783447 scopus 로고    scopus 로고
    • Determining the effect of UV-C, high intensity ultrasound and nonthermal atmospheric plasma treatments on reducing the allergenicity of α-casein and whey proteins
    • C.V.R.K.Tammineedi, R.Choudhary, G.C.Perez-Alvarado, & D.G.Watson, (2013). Determining the effect of UV-C, high intensity ultrasound and nonthermal atmospheric plasma treatments on reducing the allergenicity of α-casein and whey proteins. LWT – Food Science and Technology, 54, 35–41. doi:10.1016/j.lwt.2013.05.020
    • (2013) LWT – Food Science and Technology , vol.54 , pp. 35-41
    • Tammineedi, C.V.R.K.1    Choudhary, R.2    Perez-Alvarado, G.C.3    Watson, D.G.4
  • 43
    • 33847300425 scopus 로고    scopus 로고
    • Epitope peptides and immunotherapy
    • S.Tanabe, (2007). Epitope peptides and immunotherapy. Current Protein & Peptide Science, 8, 109–118. doi:10.2174/138920307779941569
    • (2007) Current Protein & Peptide Science , vol.8 , pp. 109-118
    • Tanabe, S.1
  • 44
    • 77957783907 scopus 로고    scopus 로고
    • Comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes: Implications for the structure–function relationship
    • C.H.Tang, & X.A.Sun, (2011). Comparative study of physicochemical and conformational properties in three vicilins from Phaseolus legumes:Implications for the structure–function relationship. Food Hydrocolloids, 25, 313–324.
    • (2011) Food Hydrocolloids , vol.25 , pp. 313-324
    • Tang, C.H.1    Sun, X.A.2
  • 45
    • 84980601228 scopus 로고    scopus 로고
    • Improvement of protein properties through dynamic high pressure micro-fluidization treatment and preliminary study on its mechanism (PhD dissertation). Nanchang University, Nanchang, People's Republic of China, pp 185–189
    • Z.C.Tu, (2007). Improvement of protein properties through dynamic high pressure micro-fluidization treatment and preliminary study on its mechanism (PhD dissertation). Nanchang University, Nanchang, People's Republic of China, pp 185–189.
    • (2007)
    • Tu, Z.C.1
  • 47
    • 38849139630 scopus 로고    scopus 로고
    • Effects of high pressure treatment on some physicochemical and functional properties of soy protein isolates
    • X.S.Wang, C.H.Tang, B.S.Li, X.Q.Yang, L.Li, & C.Y.Ma, (2008). Effects of high pressure treatment on some physicochemical and functional properties of soy protein isolates. Food Hydrocolloids, 22, 560–567. doi:10.1016/j.foodhyd.2007.01.027
    • (2008) Food Hydrocolloids , vol.22 , pp. 560-567
    • Wang, X.S.1    Tang, C.H.2    Li, B.S.3    Yang, X.Q.4    Li, L.5    Ma, C.Y.6
  • 48
    • 78349306782 scopus 로고    scopus 로고
    • Effects of high pressure homogenization on rheological properties of flaxseedgum
    • Y.Wang, D.Li, L.J.Wang, & J.Xue, (2011). Effects of high pressure homogenization on rheological properties of flaxseedgum. Carbohydrate Polymers, 83, 489–494. doi:10.1016/j.carbpol.2010.08.015
    • (2011) Carbohydrate Polymers , vol.83 , pp. 489-494
    • Wang, Y.1    Li, D.2    Wang, L.J.3    Xue, J.4
  • 49
    • 3242877618 scopus 로고    scopus 로고
    • DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data
    • L.Whitmore, & B.A.Wallace, (2004). DICHROWEB, an online server for protein secondary structure analyses from circular dichroism spectroscopic data. Nucleic Acids Research, 32, W668–W673. doi:10.1093/nar/gkh371
    • (2004) Nucleic Acids Research , vol.32 , pp. W668-W673
    • Whitmore, L.1    Wallace, B.A.2
  • 52
    • 84856035282 scopus 로고    scopus 로고
    • Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate
    • B.E.Yuan, J.Y.Ren, M.M.Zhao, D.H.Luo, & L.J.Gu, (2012). Effects of limited enzymatic hydrolysis with pepsin and high-pressure homogenization on the functional properties of soybean protein isolate. LWT – Food Science and Technology, 46, 453–459. doi:10.1016/j.lwt.2011.12.001
    • (2012) LWT – Food Science and Technology , vol.46 , pp. 453-459
    • Yuan, B.E.1    Ren, J.Y.2    Zhao, M.M.3    Luo, D.H.4    Gu, L.J.5
  • 54
    • 79959302375 scopus 로고    scopus 로고
    • Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin
    • J.Z.Zhong, C.M.Liu, W.Liu, X.F.Cai, Z.C.Tu, & J.Wan, (2011). Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin. European Food Research and Technology, 233, 95–102. doi:10.1007/s00217-011-1500-2
    • (2011) European Food Research and Technology , vol.233 , pp. 95-102
    • Zhong, J.Z.1    Liu, C.M.2    Liu, W.3    Cai, X.F.4    Tu, Z.C.5    Wan, J.6


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