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Volumn 17, Issue 1, 2018, Pages 137-164

Bovine Milk Allergens: A Comprehensive Review

Author keywords

allergen; cross reactivity; detection; food processing; milk proteins

Indexed keywords

ALLERGENS; ALLERGIES; BAKERY PRODUCTS; COMPLIANCE CONTROL; ERROR DETECTION; FOOD PROCESSING; FOOD PRODUCTS; MASS SPECTROMETRY; POLYMERASE CHAIN REACTION; PROCESSED FOODS; PROTEINS;

EID: 85033685661     PISSN: None     EISSN: 15414337     Source Type: Journal    
DOI: 10.1111/1541-4337.12318     Document Type: Review
Times cited : (178)

References (262)
  • 1
    • 33847199653 scopus 로고    scopus 로고
    • Assessment of allergen cross-reactivity
    • Aalberse R. 2007. Assessment of allergen cross-reactivity. Clin Mol Allergy 5:2.
    • (2007) Clin Mol Allergy , vol.5 , pp. 2
    • Aalberse, R.1
  • 2
    • 0026072947 scopus 로고
    • Human IgE-binding synthetic peptides of bovine β-lactoglobulin and α-lactalbumin. In vitro cross-reactivity of the allergens
    • Adams S, Barnett D, Walsh B, Pearce R, Hill D, Howden M. 1991. Human IgE-binding synthetic peptides of bovine β-lactoglobulin and α-lactalbumin. In vitro cross-reactivity of the allergens. Immunol Cell Biol 69:191–7.
    • (1991) Immunol Cell Biol , vol.69 , pp. 191-197
    • Adams, S.1    Barnett, D.2    Walsh, B.3    Pearce, R.4    Hill, D.5    Howden, M.6
  • 3
    • 17644408352 scopus 로고    scopus 로고
    • Peanut- and cow's milk-specific IgE, Th2 cells and local anaphylactic reaction are induced in Balb/c mice orally sensitized with cholera toxin
    • Adel-Patient K, Bernard H, Ah-Leung S, Créminon C, Wal JM. 2005. Peanut- and cow's milk-specific IgE, Th2 cells and local anaphylactic reaction are induced in Balb/c mice orally sensitized with cholera toxin. Allergy 60:658–64.
    • (2005) Allergy , vol.60 , pp. 658-664
    • Adel-Patient, K.1    Bernard, H.2    Ah-Leung, S.3    Créminon, C.4    Wal, J.M.5
  • 7
    • 36249018405 scopus 로고    scopus 로고
    • Efficacy of donkey's milk in treating cow's milk allergic children: major concerns
    • Alessandri C, Mari A. 2007. Efficacy of donkey's milk in treating cow's milk allergic children: major concerns. Pediatr Allergy Immunol 18:625–6.
    • (2007) Pediatr Allergy Immunol , vol.18 , pp. 625-626
    • Alessandri, C.1    Mari, A.2
  • 11
    • 79251620332 scopus 로고    scopus 로고
    • Selection of possible marker peptides for the detection of major ruminant milk proteins in food by liquid chromatography-tandem mass spectrometry
    • Ansari P, Stoppacher N, Rudolf J, Schuhmacher R, Baumgartner S. 2011. Selection of possible marker peptides for the detection of major ruminant milk proteins in food by liquid chromatography-tandem mass spectrometry. Anal Bioanal Chem 399:1105–15.
    • (2011) Anal Bioanal Chem , vol.399 , pp. 1105-1115
    • Ansari, P.1    Stoppacher, N.2    Rudolf, J.3    Schuhmacher, R.4    Baumgartner, S.5
  • 14
    • 0017122325 scopus 로고
    • Immunochemistry of serum albumin-II: Isolation and characterization of a fragment from the first third bovine serum albumin carrying almost all the antigenic reactivity of the protein
    • Atassi MS, Habeeb AFSA, Lee C-L. 1976. Immunochemistry of serum albumin-II: Isolation and characterization of a fragment from the first third bovine serum albumin carrying almost all the antigenic reactivity of the protein. Immunochem 13:547–55.
    • (1976) Immunochem , vol.13 , pp. 547-555
    • Atassi, M.S.1    Habeeb, A.F.S.A.2    Lee, C.-L.3
  • 15
    • 0028086287 scopus 로고
    • A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding
    • Ball G, Shelton M, Walsh B, Hill D, Hosking C, Howden M. 1994. A major continuous allergenic epitope of bovine β-lactoglobulin recognized by human IgE binding. Clin Exp Allergy 24:758–64.
    • (1994) Clin Exp Allergy , vol.24 , pp. 758-764
    • Ball, G.1    Shelton, M.2    Walsh, B.3    Hill, D.4    Hosking, C.5    Howden, M.6
  • 17
    • 84883251337 scopus 로고    scopus 로고
    • In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides
    • Benedé S, López-Expósito I, Giménez G, Grishina G, Bardina L, Sampson HA, Molina E, López-Fandiño R. 2014. In vitro digestibility of bovine β-casein with simulated and human oral and gastrointestinal fluids. Identification and IgE-reactivity of the resultant peptides. Food Chem 143:514–21.
    • (2014) Food Chem , vol.143 , pp. 514-521
    • Benedé, S.1    López-Expósito, I.2    Giménez, G.3    Grishina, G.4    Bardina, L.5    Sampson, H.A.6    Molina, E.7    López-Fandiño, R.8
  • 19
    • 0031905287 scopus 로고    scopus 로고
    • Specificity of the human IgE response to the different purified caseins in allergy to cow's milk proteins
    • Bernard H, Créminon C, Yvon M, Wal JM. 1998. Specificity of the human IgE response to the different purified caseins in allergy to cow's milk proteins. Intl Arch Allergy Immunol 115:235–44.
    • (1998) Intl Arch Allergy Immunol , vol.115 , pp. 235-244
    • Bernard, H.1    Créminon, C.2    Yvon, M.3    Wal, J.M.4
  • 20
    • 0033962437 scopus 로고    scopus 로고
    • Post-translational phosphorylation affects the IgE binding capacity of caseins
    • Bernard H, Meisel H, Creminon C, Wal JM. 2000a. Post-translational phosphorylation affects the IgE binding capacity of caseins. FEBS Lett 467:239–44.
    • (2000) FEBS Lett , vol.467 , pp. 239-244
    • Bernard, H.1    Meisel, H.2    Creminon, C.3    Wal, J.M.4
  • 24
    • 71649085277 scopus 로고    scopus 로고
    • Simultaneous, quantitative detection of five whey proteins in multiple samples by surface plasmon resonance
    • Billakanti JM, Fee CJ, Lane FR, Kash AS, Fredericks R. 2010. Simultaneous, quantitative detection of five whey proteins in multiple samples by surface plasmon resonance. Intl Dairy J 20:96–105.
    • (2010) Intl Dairy J , vol.20 , pp. 96-105
    • Billakanti, J.M.1    Fee, C.J.2    Lane, F.R.3    Kash, A.S.4    Fredericks, R.5
  • 27
    • 84975137981 scopus 로고    scopus 로고
    • Food allergens: is there a correlation between stability to digestion and allergenicity
    • Bøgh KL, Madsen CB. 2016. Food allergens: is there a correlation between stability to digestion and allergenicity? Crit Rev Food Sci Nutr 56:1545–67.
    • (2016) Crit Rev Food Sci Nutr , vol.56 , pp. 1545-1567
    • Bøgh, K.L.1    Madsen, C.B.2
  • 28
    • 0037227420 scopus 로고    scopus 로고
    • A multiplex polymerase chain reaction for the identification of cows', goats' and sheeps' milk in dairy products
    • Bottero MT, Civera T, Nucera D, Rosati S, Sacchi P, Turi RM. 2003. A multiplex polymerase chain reaction for the identification of cows', goats' and sheeps' milk in dairy products. Intl Dairy J 13:277–82.
    • (2003) Intl Dairy J , vol.13 , pp. 277-282
    • Bottero, M.T.1    Civera, T.2    Nucera, D.3    Rosati, S.4    Sacchi, P.5    Turi, R.M.6
  • 31
    • 52649097972 scopus 로고    scopus 로고
    • Glycosylations of κ-casein-derived caseinomacropeptide reduce its accessibility to endo- but not exointestinal brush border membrane peptidases
    • Boutrou R, Jardin J, Blais A, Tomé D, Léonil J. 2008. Glycosylations of κ-casein-derived caseinomacropeptide reduce its accessibility to endo- but not exointestinal brush border membrane peptidases. J Agric Food Chem 56:8166–73.
    • (2008) J Agric Food Chem , vol.56 , pp. 8166-8173
    • Boutrou, R.1    Jardin, J.2    Blais, A.3    Tomé, D.4    Léonil, J.5
  • 34
    • 70350044740 scopus 로고    scopus 로고
    • Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology
    • Bu G, Lu J, Zheng Z, Luo Y. 2009a. Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology. J Sci Food Agric 89:2428–34.
    • (2009) J Sci Food Agric , vol.89 , pp. 2428-2434
    • Bu, G.1    Lu, J.2    Zheng, Z.3    Luo, Y.4
  • 35
    • 70449410078 scopus 로고    scopus 로고
    • Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate
    • Bu G, Luo Y, Zheng Z, Zheng H. 2009b. Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate. Food Agric Immunol 20:195–206.
    • (2009) Food Agric Immunol , vol.20 , pp. 195-206
    • Bu, G.1    Luo, Y.2    Zheng, Z.3    Zheng, H.4
  • 36
    • 77952216642 scopus 로고    scopus 로고
    • Reduced antigenicity of β-lactoglobulin by conjugation with glucose through controlled Maillard reaction conditions
    • Bu G, Luo Y, Lu J, Zhang Y. 2010a. Reduced antigenicity of β-lactoglobulin by conjugation with glucose through controlled Maillard reaction conditions. Food Agric Immunol 21:143–56.
    • (2010) Food Agric Immunol , vol.21 , pp. 143-156
    • Bu, G.1    Luo, Y.2    Lu, J.3    Zhang, Y.4
  • 37
    • 77955939723 scopus 로고    scopus 로고
    • Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins
    • Bu G, Luo Y, Zhang Y, Chen F. 2010b. Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins. J Sci Food Agric 90:2015–20.
    • (2010) J Sci Food Agric , vol.90 , pp. 2015-2020
    • Bu, G.1    Luo, Y.2    Zhang, Y.3    Chen, F.4
  • 38
    • 84883010738 scopus 로고    scopus 로고
    • Milk processing as a tool to reduce cow's milk allergenicity: a mini-review
    • Bu G, Luo Y, Chen F, Liu K, Zhu T. 2013. Milk processing as a tool to reduce cow's milk allergenicity: a mini-review. Dairy Sci Technol 93:211–23.
    • (2013) Dairy Sci Technol , vol.93 , pp. 211-223
    • Bu, G.1    Luo, Y.2    Chen, F.3    Liu, K.4    Zhu, T.5
  • 41
    • 0036124875 scopus 로고    scopus 로고
    • Application of gamma irradiation for inhibition of food allergy
    • Byun MW, Lee JW, Yook HS, Jo C, Kim HY. 2002. Application of gamma irradiation for inhibition of food allergy. Radiat Phys Chem 63:369–70.
    • (2002) Radiat Phys Chem , vol.63 , pp. 369-370
    • Byun, M.W.1    Lee, J.W.2    Yook, H.S.3    Jo, C.4    Kim, H.Y.5
  • 42
    • 15644365219 scopus 로고    scopus 로고
    • Anaphylaxis to sheep's milk cheese in a child unaffected by cow's milk protein allergy
    • Calvani Jr M, Alessandri C, Calvani M. 1998. Anaphylaxis to sheep's milk cheese in a child unaffected by cow's milk protein allergy. Eur J Pediatr 157:17–9.
    • (1998) Eur J Pediatr , vol.157 , pp. 17-19
    • Calvani, M.1    Alessandri, C.2    Calvani, M.3
  • 44
    • 84959213281 scopus 로고    scopus 로고
    • The major soybean allergen Gly m Bd 28K induces hypersensitivity reactions in mice sensitized to cow's milk proteins
    • Candreva AM, Smaldini PL, Curciarello R, Fossati CA, Docena GH, Petruccelli S. 2016. The major soybean allergen Gly m Bd 28K induces hypersensitivity reactions in mice sensitized to cow's milk proteins. J Agric Food Chem 64:1590–9.
    • (2016) J Agric Food Chem , vol.64 , pp. 1590-1599
    • Candreva, A.M.1    Smaldini, P.L.2    Curciarello, R.3    Fossati, C.A.4    Docena, G.H.5    Petruccelli, S.6
  • 45
    • 79952816253 scopus 로고    scopus 로고
    • Electrochemical immunosensor for casein based on gold nanoparticles and poly(l-Arginine)/multi-walled carbon nanotubes composite film functionalized interface
    • Cao Q, Zhao H, Yang Y, He Y, Ding N, Wang J, Wu Z, Xiang K, Wang G. 2011. Electrochemical immunosensor for casein based on gold nanoparticles and poly(l-Arginine)/multi-walled carbon nanotubes composite film functionalized interface. Biosens Bioelectron 26:3469–74.
    • (2011) Biosens Bioelectron , vol.26 , pp. 3469-3474
    • Cao, Q.1    Zhao, H.2    Yang, Y.3    He, Y.4    Ding, N.5    Wang, J.6    Wu, Z.7    Xiang, K.8    Wang, G.9
  • 49
    • 0035724636 scopus 로고    scopus 로고
    • Identification of IgE and IgG binding epitopes on β- and κ-casein in cow's milk allergic patients
    • Chatchatee P, Jarvinen KM, Bardina L, Vila L, Beyer K, Sampson HA. 2001b. Identification of IgE and IgG binding epitopes on β- and κ-casein in cow's milk allergic patients. Clin Exper Allergy 31:1256–62.
    • (2001) Clin Exper Allergy , vol.31 , pp. 1256-1262
    • Chatchatee, P.1    Jarvinen, K.M.2    Bardina, L.3    Vila, L.4    Beyer, K.5    Sampson, H.A.6
  • 50
    • 84920143733 scopus 로고    scopus 로고
    • Quantification of bovine β-casein allergen in baked foodstuffs based on ultra-performance liquid chromatography with tandem mass spectrometry
    • Chen Q, Zhang J, Ke X, Lai S, Tao B, Yang J, Mo W, Ren Y. 2015. Quantification of bovine β-casein allergen in baked foodstuffs based on ultra-performance liquid chromatography with tandem mass spectrometry. Food Addit Contam Part A 32:25–34.
    • (2015) Food Addit Contam Part A , vol.32 , pp. 25-34
    • Chen, Q.1    Zhang, J.2    Ke, X.3    Lai, S.4    Tao, B.5    Yang, J.6    Mo, W.7    Ren, Y.8
  • 51
    • 54049110349 scopus 로고    scopus 로고
    • Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure
    • Chicon R, Belloque J, Alonso E, Lopez-Fandino R. 2009. Antibody binding and functional properties of whey protein hydrolysates obtained under high pressure. Food Hydrocolloids 23:593–9.
    • (2009) Food Hydrocolloids , vol.23 , pp. 593-599
    • Chicon, R.1    Belloque, J.2    Alonso, E.3    Lopez-Fandino, R.4
  • 55
    • 77955510256 scopus 로고    scopus 로고
    • Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin
    • Corzo-Martínez M, Soria AC, Belloque J, Villamiel M, Moreno FJ. 2010. Effect of glycation on the gastrointestinal digestibility and immunoreactivity of bovine β-lactoglobulin. Intl Dairy J 20:742–52.
    • (2010) Intl Dairy J , vol.20 , pp. 742-752
    • Corzo-Martínez, M.1    Soria, A.C.2    Belloque, J.3    Villamiel, M.4    Moreno, F.J.5
  • 56
    • 84856831464 scopus 로고    scopus 로고
    • Almond allergens: molecular characterization, detection, and clinical relevance
    • Costa J, Mafra I, Carrapatoso I, Oliveira MBPP. 2012. Almond allergens: molecular characterization, detection, and clinical relevance. J Agric Food Chem 60:1337–49.
    • (2012) J Agric Food Chem , vol.60 , pp. 1337-1349
    • Costa, J.1    Mafra, I.2    Carrapatoso, I.3    Oliveira, M.B.P.P.4
  • 57
    • 84894271730 scopus 로고    scopus 로고
    • Walnut allergens: molecular characterization, detection and clinical relevance
    • Costa J, Carrapatoso I, Oliveira MBPP, Mafra I. 2014. Walnut allergens: molecular characterization, detection and clinical relevance. Clin Exp Allergy 44:319–41.
    • (2014) Clin Exp Allergy , vol.44 , pp. 319-341
    • Costa, J.1    Carrapatoso, I.2    Oliveira, M.B.P.P.3    Mafra, I.4
  • 58
    • 84987677775 scopus 로고    scopus 로고
    • Hazelnut allergens: molecular characterisation, detection and clinical relevance
    • Costa J, Mafra I, Carrapatoso I, Oliveira MBPP. 2015. Hazelnut allergens: molecular characterisation, detection and clinical relevance. Crit Rev Food Sci Nutr 56:2579–605.
    • (2015) Crit Rev Food Sci Nutr , vol.56 , pp. 2579-2605
    • Costa, J.1    Mafra, I.2    Carrapatoso, I.3    Oliveira, M.B.P.P.4
  • 60
    • 84990059628 scopus 로고    scopus 로고
    • Evaluation of commercial milk-specific lateral flow devices
    • Courtney RC, Taylor SL, Baumert JL. 2016. Evaluation of commercial milk-specific lateral flow devices. J Food Prot 79:1767–74.
    • (2016) J Food Prot , vol.79 , pp. 1767-1774
    • Courtney, R.C.1    Taylor, S.L.2    Baumert, J.L.3
  • 61
    • 84857025302 scopus 로고    scopus 로고
    • MALDI based identification of whey protein derived tryptic marker peptides that resist protein glycation
    • Cucu T, De Meulenaer B, Kerkaert B, Vandenberghe I, Devreese B. 2012. MALDI based identification of whey protein derived tryptic marker peptides that resist protein glycation. Food Res Intl 47:23–30.
    • (2012) Food Res Intl , vol.47 , pp. 23-30
    • Cucu, T.1    De Meulenaer, B.2    Kerkaert, B.3    Vandenberghe, I.4    Devreese, B.5
  • 64
    • 77955277013 scopus 로고    scopus 로고
    • Simultaneous detection of cow and buffalo milk in mozzarella cheese by real-time PCR assay
    • Dalmasso A, Civera T, La Neve F, Bottero MT. 2011. Simultaneous detection of cow and buffalo milk in mozzarella cheese by real-time PCR assay. Food Chem 124:362–6.
    • (2011) Food Chem , vol.124 , pp. 362-366
    • Dalmasso, A.1    Civera, T.2    La Neve, F.3    Bottero, M.T.4
  • 65
    • 85020260508 scopus 로고    scopus 로고
    • A two-step enzymatic modification method to reduce immuno-reactivity of milk proteins
    • Damodaran S, Li Y. 2017. A two-step enzymatic modification method to reduce immuno-reactivity of milk proteins. Food Chem 237:724–32.
    • (2017) Food Chem , vol.237 , pp. 724-732
    • Damodaran, S.1    Li, Y.2
  • 66
    • 60849087668 scopus 로고    scopus 로고
    • Development and evaluation of two ELISA formats for the detection of β-lactoglobulin in model processed and commercial foods
    • de Luis R, Lavilla M, Sánchez L, Calvo M, Pérez MD. 2009. Development and evaluation of two ELISA formats for the detection of β-lactoglobulin in model processed and commercial foods. Food Control 20:643–7.
    • (2009) Food Control , vol.20 , pp. 643-647
    • de Luis, R.1    Lavilla, M.2    Sánchez, L.3    Calvo, M.4    Pérez, M.D.5
  • 68
    • 84864669034 scopus 로고    scopus 로고
    • Undeclared allergenic ingredients in foods from animal origin: survey of an Italian region's food market, 2007–2009
    • Decastelli L, Gallina S, Manila Bianchi D, Fragassi S, Restani P. 2012. Undeclared allergenic ingredients in foods from animal origin: survey of an Italian region's food market, 2007–2009. Food Addit Contam Part B-Surveill 5:160–4.
    • (2012) Food Addit Contam Part B-Surveill , vol.5 , pp. 160-164
    • Decastelli, L.1    Gallina, S.2    Manila Bianchi, D.3    Fragassi, S.4    Restani, P.5
  • 70
    • 34447536145 scopus 로고    scopus 로고
    • Detecting dairy and egg residues in food
    • In, Koppelman SJ, Hefle SL, editors., Cambridge, Woodhead Publishing, p
    • Demeulemester C, Giovannacci I, Leduc V. 2006. Detecting dairy and egg residues in food. In: Koppelman SJ, Hefle SL, editors. Detecting allergens in food. Cambridge: Woodhead Publishing. p 219–43.
    • (2006) Detecting allergens in food , pp. 219-243
    • Demeulemester, C.1    Giovannacci, I.2    Leduc, V.3
  • 72
    • 84930965771 scopus 로고    scopus 로고
    • In vitro digestibility and immunoreactivity of bovine milk proteins
    • Do AB, Williams K, Toomer OT. 2016. In vitro digestibility and immunoreactivity of bovine milk proteins. Food Chem 190:581–7.
    • (2016) Food Chem , vol.190 , pp. 581-587
    • Do, A.B.1    Williams, K.2    Toomer, O.T.3
  • 73
    • 77956636375 scopus 로고    scopus 로고
    • Effects of thermal processing on the enzyme-linked immunosorbent assay (ELISA) detection of milk residues in a model food matrix
    • Downs ML, Taylor SL. 2010. Effects of thermal processing on the enzyme-linked immunosorbent assay (ELISA) detection of milk residues in a model food matrix. J Agric Food Chem 58:10085–91.
    • (2010) J Agric Food Chem , vol.58 , pp. 10085-10091
    • Downs, M.L.1    Taylor, S.L.2
  • 74
    • 84903121146 scopus 로고    scopus 로고
    • Effects of enzymatic hydrolysis on the allergenicity of whey protein concentrates
    • Duan C, Yang L, Li A, Zhao R, Huo G. 2014. Effects of enzymatic hydrolysis on the allergenicity of whey protein concentrates. Iran J Allergy Asthma Immunol 13:231–9.
    • (2014) Iran J Allergy Asthma Immunol , vol.13 , pp. 231-239
    • Duan, C.1    Yang, L.2    Li, A.3    Zhao, R.4    Huo, G.5
  • 76
    • 1542286920 scopus 로고    scopus 로고
    • Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin
    • Ehn BM, Ekstrand B, Bengtsson U, Ahlstedt S. 2004. Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin. J Agric Food Chem 52:1398–403.
    • (2004) J Agric Food Chem , vol.52 , pp. 1398-1403
    • Ehn, B.M.1    Ekstrand, B.2    Bengtsson, U.3    Ahlstedt, S.4
  • 77
    • 84864395861 scopus 로고    scopus 로고
    • Electrochemical immunosensor for the milk allergen β-lactoglobulin based on electrografting of organic film on graphene modified screen-printed carbon electrodes
    • Eissa S, Tlili C, L'Hocine L, Zourob M. 2012. Electrochemical immunosensor for the milk allergen β-lactoglobulin based on electrografting of organic film on graphene modified screen-printed carbon electrodes. Biosens Bioelectron 38:308–13.
    • (2012) Biosens Bioelectron , vol.38 , pp. 308-313
    • Eissa, S.1    Tlili, C.2    L'Hocine, L.3    Zourob, M.4
  • 78
    • 33846850537 scopus 로고    scopus 로고
    • The challenge of cow milk protein allergy
    • El-Agamy EI. 2007. The challenge of cow milk protein allergy. Small Ruminant Res 68:64–72.
    • (2007) Small Ruminant Res , vol.68 , pp. 64-72
    • El-Agamy, E.I.1
  • 81
    • 85039933919 scopus 로고    scopus 로고
    • Available from, Accessed 2017 September 12
    • Eurostat. 2017. Milk and milk product statistics. Available from: http://ec.europa.eu/eurostat/statistics-explained/index.php/Milk_and_milk_product_statistics#Milk_products. Accessed 2017 September 12.
    • (2017) Milk and milk product statistics
  • 82
    • 85039932468 scopus 로고    scopus 로고
    • Available from, Accessed 2017 June 23
    • FAO. 2017. Bi-annual market reports, June 2017. Available from: http://www.fao.org/fileadmin/templates/est/COMM_MARKETS_MONITORING/Dairy/Documents/Food_Outlook_June_2017__Dairy_.pdf. Accessed 2017 June 23.
    • (2017) Bi-annual market reports, June 2017
  • 86
    • 84921283296 scopus 로고    scopus 로고
    • Immunoreactivity of lactic acid-treated mare's milk after simulated digestion
    • Fotschki J, Szyc A, Wróblewska B. 2015. Immunoreactivity of lactic acid-treated mare's milk after simulated digestion. J Dairy Res 82:78–85.
    • (2015) J Dairy Res , vol.82 , pp. 78-85
    • Fotschki, J.1    Szyc, A.2    Wróblewska, B.3
  • 87
    • 0041495395 scopus 로고    scopus 로고
    • Milk proteins as food ingredients
    • Fox P. 2001. Milk proteins as food ingredients. Intl J Dairy Technol 54:41–55.
    • (2001) Intl J Dairy Technol , vol.54 , pp. 41-55
    • Fox, P.1
  • 89
    • 84861203680 scopus 로고    scopus 로고
    • Comparison of international food allergen labeling regulations
    • Gendel SM. 2012. Comparison of international food allergen labeling regulations. Regul Toxicol Pharmacol 63:279–85.
    • (2012) Regul Toxicol Pharmacol , vol.63 , pp. 279-285
    • Gendel, S.M.1
  • 90
    • 85039963642 scopus 로고    scopus 로고
    • Introduction to dairy science and technology: milk history, consumption, production, and composition
    • In, Guelph, Canada, University of Guelph, Available from
    • Goff HD. 2016. Introduction to dairy science and technology: milk history, consumption, production, and composition. In: The Dairy Science and Technology eBook. Guelph, Canada: University of Guelph. Available from: https://www.uoguelph.ca/foodscience/book-page/dairy-science-and-technology-ebook.
    • (2016) The Dairy Science and Technology eBook
    • Goff, H.D.1
  • 91
    • 84929334481 scopus 로고    scopus 로고
    • Impact of irradiation and thermal processing on the immunochemical detection of milk and egg allergens in foods
    • Gomaa A, Boye J. 2015a. Impact of irradiation and thermal processing on the immunochemical detection of milk and egg allergens in foods. Food Res Intl 74:275–83.
    • (2015) Food Res Intl , vol.74 , pp. 275-283
    • Gomaa, A.1    Boye, J.2
  • 92
    • 84919629422 scopus 로고    scopus 로고
    • Simultaneous detection of multi-allergens in an incurred food matrix using ELISA, multiplex flow cytometry and liquid chromatography mass spectrometry (LC–MS)
    • Gomaa A, Boye J. 2015b. Simultaneous detection of multi-allergens in an incurred food matrix using ELISA, multiplex flow cytometry and liquid chromatography mass spectrometry (LC–MS). Food Chem 175:585–92.
    • (2015) Food Chem , vol.175 , pp. 585-592
    • Gomaa, A.1    Boye, J.2
  • 93
    • 56349088466 scopus 로고    scopus 로고
    • Irradiation effect on α-and β-caseins of milk and Queso Blanco cheese determined by capillary electrophoresis
    • Ham J, Jeong S, Lee S, Han G, Chae H, Yoo Y, Kim D, Lee W, Jo C. 2009. Irradiation effect on α-and β-caseins of milk and Queso Blanco cheese determined by capillary electrophoresis. Radiat Phys Chem 78:158–63.
    • (2009) Radiat Phys Chem , vol.78 , pp. 158-163
    • Ham, J.1    Jeong, S.2    Lee, S.3    Han, G.4    Chae, H.5    Yoo, Y.6    Kim, D.7    Lee, W.8    Jo, C.9
  • 94
    • 37749015567 scopus 로고    scopus 로고
    • Identification of amino acids critical for IgE-binding to sequential epitopes of bovine κ-casein and the similarity of these epitopes to the corresponding human κ-casein sequence
    • Han N, Järvinen K, Cocco R, Busse P, Sampson H, Beyer K. 2008. Identification of amino acids critical for IgE-binding to sequential epitopes of bovine κ-casein and the similarity of these epitopes to the corresponding human κ-casein sequence. Allergy 63:198–204.
    • (2008) Allergy , vol.63 , pp. 198-204
    • Han, N.1    Järvinen, K.2    Cocco, R.3    Busse, P.4    Sampson, H.5    Beyer, K.6
  • 96
    • 80054820101 scopus 로고    scopus 로고
    • Application of a liquid chromatography tandem mass spectrometry method for the simultaneous detection of seven allergenic foods in flour and bread and comparison of the method with commercially available ELISA test kits
    • Heick J, Fischer M, Kerbach S, Tamm U, Popping B. 2011a. Application of a liquid chromatography tandem mass spectrometry method for the simultaneous detection of seven allergenic foods in flour and bread and comparison of the method with commercially available ELISA test kits. J AOAC Intl 94:1060–8.
    • (2011) J AOAC Intl , vol.94 , pp. 1060-1068
    • Heick, J.1    Fischer, M.2    Kerbach, S.3    Tamm, U.4    Popping, B.5
  • 97
    • 78751702838 scopus 로고    scopus 로고
    • First screening method for the simultaneous detection of seven allergens by liquid chromatography mass spectrometry
    • Heick J, Fischer M, Popping B. 2011b. First screening method for the simultaneous detection of seven allergens by liquid chromatography mass spectrometry. J Chromatogr A 1218:938–43.
    • (2011) J Chromatogr A , vol.1218 , pp. 938-943
    • Heick, J.1    Fischer, M.2    Popping, B.3
  • 98
    • 0033456204 scopus 로고    scopus 로고
    • The recognition pattern of sequential B cell epitopes of β-lactoglobulin does not vary with the clinical manifestations of cow's milk allergy
    • Heinzmann A, Blattmann S, Spuergin P, Forster J, Deichmann KA. 1999. The recognition pattern of sequential B cell epitopes of β-lactoglobulin does not vary with the clinical manifestations of cow's milk allergy. Intl Arch Allergy Immunol 120:280–6.
    • (1999) Intl Arch Allergy Immunol , vol.120 , pp. 280-286
    • Heinzmann, A.1    Blattmann, S.2    Spuergin, P.3    Forster, J.4    Deichmann, K.A.5
  • 100
    • 84860195220 scopus 로고    scopus 로고
    • Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk
    • Hinz K, O'Connor PM, Huppertz T, Ross RP, Kelly AL. 2012. Comparison of the principal proteins in bovine, caprine, buffalo, equine and camel milk. J Dairy Res 79:185–91.
    • (2012) J Dairy Res , vol.79 , pp. 185-191
    • Hinz, K.1    O'Connor, P.M.2    Huppertz, T.3    Ross, R.P.4    Kelly, A.L.5
  • 102
    • 84896707250 scopus 로고    scopus 로고
    • Cow's milk allergy: from allergens to new forms of diagnosis, therapy and prevention
    • Hochwallner H, Schulmeister U, Swoboda I, Spitzauer S, Valenta R. 2014. Cow's milk allergy: from allergens to new forms of diagnosis, therapy and prevention. Methods 66:22–33.
    • (2014) Methods , vol.66 , pp. 22-33
    • Hochwallner, H.1    Schulmeister, U.2    Swoboda, I.3    Spitzauer, S.4    Valenta, R.5
  • 103
    • 34347371983 scopus 로고    scopus 로고
    • A ‘gold cluster-linked immunosorbent assay’: optical near-field biosensor chip for the detection of allergenic β-lactoglobulin in processed milk matrices
    • Hohensinner V, Maier I, Pittner F. 2007. A ‘gold cluster-linked immunosorbent assay’: optical near-field biosensor chip for the detection of allergenic β-lactoglobulin in processed milk matrices. J Biotechnol 130:385–8.
    • (2007) J Biotechnol , vol.130 , pp. 385-388
    • Hohensinner, V.1    Maier, I.2    Pittner, F.3
  • 104
    • 84884353426 scopus 로고    scopus 로고
    • Invited review: caseins and the casein micelle: their biological functions, structures, and behavior in foods
    • Holt C, Carver JA, Ecroyd H, Thorn DC. 2013. Invited review: caseins and the casein micelle: their biological functions, structures, and behavior in foods. J Dairy Sci 96:6127–46.
    • (2013) J Dairy Sci , vol.96 , pp. 6127-6146
    • Holt, C.1    Carver, J.A.2    Ecroyd, H.3    Thorn, D.C.4
  • 105
    • 0019907229 scopus 로고
    • Immunochemical studies on α-lactalbumin
    • Hopp TP, Woods KR. 1982. Immunochemical studies on α-lactalbumin. Mol Immunol 19:1453–63.
    • (1982) Mol Immunol , vol.19 , pp. 1453-1463
    • Hopp, T.P.1    Woods, K.R.2
  • 106
    • 84958984713 scopus 로고    scopus 로고
    • Structure and IgE-binding properties of α-casein treated by high hydrostatic pressure, UV-C, and far-IR radiations
    • Hu G, Zheng Y, Liu Z, Deng Y, Zhao Y. 2016. Structure and IgE-binding properties of α-casein treated by high hydrostatic pressure, UV-C, and far-IR radiations. Food Chem 204:46–55.
    • (2016) Food Chem , vol.204 , pp. 46-55
    • Hu, G.1    Zheng, Y.2    Liu, Z.3    Deng, Y.4    Zhao, Y.5
  • 107
    • 84890526289 scopus 로고    scopus 로고
    • Potential utility of high-pressure processing to address the risk of food allergen concerns
    • Huang HW, Hsu CP, Yang BB, Wang CY. 2014. Potential utility of high-pressure processing to address the risk of food allergen concerns. Compr Rev Food Sci Food Saf 13:78–90.
    • (2014) Compr Rev Food Sci Food Saf , vol.13 , pp. 78-90
    • Huang, H.W.1    Hsu, C.P.2    Yang, B.B.3    Wang, C.Y.4
  • 108
    • 54149112723 scopus 로고    scopus 로고
    • Development and application of an optical biosensor immunoassay for α-lactalbumin in bovine milk
    • Indyk HE. 2009. Development and application of an optical biosensor immunoassay for α-lactalbumin in bovine milk. Intl Dairy J 19:36–42.
    • (2009) Intl Dairy J , vol.19 , pp. 36-42
    • Indyk, H.E.1
  • 109
    • 16244409271 scopus 로고    scopus 로고
    • Determination of lactoferrin in bovine milk, colostrum and infant formulas by optical biosensor analysis
    • Indyk HE, Filonzi EL. 2005. Determination of lactoferrin in bovine milk, colostrum and infant formulas by optical biosensor analysis. Intl Dairy J 15:429–38.
    • (2005) Intl Dairy J , vol.15 , pp. 429-438
    • Indyk, H.E.1    Filonzi, E.L.2
  • 110
    • 47649096420 scopus 로고    scopus 로고
    • Effects of combined microwave and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins
    • Izquierdo FJ, Peñas E, Baeza ML, Gomez R. 2008. Effects of combined microwave and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins. Intl Dairy J 18:918–22.
    • (2008) Intl Dairy J , vol.18 , pp. 918-922
    • Izquierdo, F.J.1    Peñas, E.2    Baeza, M.L.3    Gomez, R.4
  • 111
    • 68049142071 scopus 로고    scopus 로고
    • Mammalian milk allergy: clinical suspicion, cross-reactivities and diagnosis
    • Jarvinen KM, Chatchatee P. 2009. Mammalian milk allergy: clinical suspicion, cross-reactivities and diagnosis. Curr Opin Allergy Clin Immunol 9:251–8.
    • (2009) Curr Opin Allergy Clin Immunol , vol.9 , pp. 251-258
    • Jarvinen, K.M.1    Chatchatee, P.2
  • 113
    • 84864393750 scopus 로고    scopus 로고
    • Diagnostic oral food challenges: procedures and biomarkers
    • Järvinen KM, Sicherer SH. 2012. Diagnostic oral food challenges: procedures and biomarkers. J Immunol Methods 383:30–8.
    • (2012) J Immunol Methods , vol.383 , pp. 30-38
    • Järvinen, K.M.1    Sicherer, S.H.2
  • 114
    • 85006778545 scopus 로고    scopus 로고
    • Development of a liquid chromatography-tandem mass spectrometry method for simultaneous detection of the main milk allergens
    • Ji J, Zhu P, Pi F, Sun C, Sun J, Jia M, Ying C, Zhang Y, Sun X. 2017. Development of a liquid chromatography-tandem mass spectrometry method for simultaneous detection of the main milk allergens. Food Control 74:79–88.
    • (2017) Food Control , vol.74 , pp. 79-88
    • Ji, J.1    Zhu, P.2    Pi, F.3    Sun, C.4    Sun, J.5    Jia, M.6    Ying, C.7    Zhang, Y.8    Sun, X.9
  • 115
    • 84979035990 scopus 로고    scopus 로고
    • HPLC-MS/MS—detection of caseins and whey proteins in meat products
    • Jira W, Schwägele F. 2015. HPLC-MS/MS—detection of caseins and whey proteins in meat products. Procedia Food Sci 5:129–32.
    • (2015) Procedia Food Sci , vol.5 , pp. 129-132
    • Jira, W.1    Schwägele, F.2
  • 121
    • 84955287328 scopus 로고    scopus 로고
    • β-lactoglobulin mutation Ala86Gln improves its ligand binding and reduces its immunoreactivity
    • Kazem-Farzandi N, Taheri-Kafrani A, Haertlé T. 2015. β-lactoglobulin mutation Ala86Gln improves its ligand binding and reduces its immunoreactivity. Intl J Biol Macromol 81:340–8.
    • (2015) Intl J Biol Macromol , vol.81 , pp. 340-348
    • Kazem-Farzandi, N.1    Taheri-Kafrani, A.2    Haertlé, T.3
  • 122
    • 84860473202 scopus 로고    scopus 로고
    • Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: dark chocolate
    • Khuda S, Slate A, Pereira M, Al-Taher F, Jackson L, Diaz-Amigo C, Bigley EC, Whitaker T, Williams K. 2012a. Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: dark chocolate. J Agric Food Chem 60:4204–11.
    • (2012) J Agric Food Chem , vol.60 , pp. 4204-4211
    • Khuda, S.1    Slate, A.2    Pereira, M.3    Al-Taher, F.4    Jackson, L.5    Diaz-Amigo, C.6    Bigley, E.C.7    Whitaker, T.8    Williams, K.9
  • 123
    • 84860473202 scopus 로고    scopus 로고
    • Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: sugar cookies
    • Khuda S, Slate A, Pereira M, Al-Taher F, Jackson L, Diaz-Amigo C, Bigley EC, Whitaker T, Williams KM. 2012b. Effect of processing on recovery and variability associated with immunochemical analytical methods for multiple allergens in a single matrix: sugar cookies. J Agric Food Chem 60:4195–203.
    • (2012) J Agric Food Chem , vol.60 , pp. 4195-4203
    • Khuda, S.1    Slate, A.2    Pereira, M.3    Al-Taher, F.4    Jackson, L.5    Diaz-Amigo, C.6    Bigley, E.C.7    Whitaker, T.8    Williams, K.M.9
  • 125
    • 34247172857 scopus 로고    scopus 로고
    • Antigenic response of β-lactoglobulin in thermally treated bovine skim milk and sweet whey
    • Kleber N, Hinrichs J. 2007. Antigenic response of β-lactoglobulin in thermally treated bovine skim milk and sweet whey. Milchwiss-Milk Sci Intl 62:121–4.
    • (2007) Milchwiss-Milk Sci Intl , vol.62 , pp. 121-124
    • Kleber, N.1    Hinrichs, J.2
  • 126
    • 33846785047 scopus 로고    scopus 로고
    • Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature
    • Kleber N, Maier S, Hinrichs J. 2007. Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature. Innov Food Sci Emerg Technol 8:39–45.
    • (2007) Innov Food Sci Emerg Technol , vol.8 , pp. 39-45
    • Kleber, N.1    Maier, S.2    Hinrichs, J.3
  • 128
    • 0035117504 scopus 로고    scopus 로고
    • Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight
    • Kobayashi K, Hirano A, Ohta A, Yoshida T, Takahashi K, Hattori M. 2001. Reduced immunogenicity of β-lactoglobulin by conjugation with carboxymethyl dextran differing in molecular weight. J Agric Food Chem 49:823–31.
    • (2001) J Agric Food Chem , vol.49 , pp. 823-831
    • Kobayashi, K.1    Hirano, A.2    Ohta, A.3    Yoshida, T.4    Takahashi, K.5    Hattori, M.6
  • 130
    • 84867737688 scopus 로고    scopus 로고
    • Two quantitative hexaplex real-time PCR systems for the detection and quantification of DNA from twelve allergens in food
    • Köppel R, Velsen-Zimmerli F, Bucher T. 2012. Two quantitative hexaplex real-time PCR systems for the detection and quantification of DNA from twelve allergens in food. Eur Food Res Technol 235:843–52.
    • (2012) Eur Food Res Technol , vol.235 , pp. 843-852
    • Köppel, R.1    Velsen-Zimmerli, F.2    Bucher, T.3
  • 134
  • 137
    • 84978712221 scopus 로고    scopus 로고
    • Identification of IgE and IgG epitopes on native Bos d 4 allergen specific to allergic children
    • Li X, Yuan S, Huang M, Gao J, Wu Z, Tong P, Yang A, Chen H. 2016. Identification of IgE and IgG epitopes on native Bos d 4 allergen specific to allergic children. Food Funct 7:2996–3005.
    • (2016) Food Funct , vol.7 , pp. 2996-3005
    • Li, X.1    Yuan, S.2    Huang, M.3    Gao, J.4    Wu, Z.5    Tong, P.6    Yang, A.7    Chen, H.8
  • 138
    • 84860395576 scopus 로고    scopus 로고
    • Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose
    • Li Z, Luo Y, Feng L. 2011. Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose. Eur Food Res Technol 233:387–94.
    • (2011) Eur Food Res Technol , vol.233 , pp. 387-394
    • Li, Z.1    Luo, Y.2    Feng, L.3
  • 139
    • 84889038227 scopus 로고    scopus 로고
    • Effect of Maillard reaction conditions on antigenicity of β-lactoglobulin and the properties of glycated whey protein during simulated gastric digestion
    • Li Z, Luo Y, Feng L, Liao P. 2013. Effect of Maillard reaction conditions on antigenicity of β-lactoglobulin and the properties of glycated whey protein during simulated gastric digestion. Food Agric Immunol 24:433–43.
    • (2013) Food Agric Immunol , vol.24 , pp. 433-443
    • Li, Z.1    Luo, Y.2    Feng, L.3    Liao, P.4
  • 140
    • 33645981010 scopus 로고    scopus 로고
    • Effect of high intensity ultrasound on the allergenicity of shrimp
    • Li ZX, Lin H, Cao LM, Jameel K. 2006. Effect of high intensity ultrasound on the allergenicity of shrimp. J Zhejiang Univ Sci B 7:251–6.
    • (2006) J Zhejiang Univ Sci B , vol.7 , pp. 251-256
    • Li, Z.X.1    Lin, H.2    Cao, L.M.3    Jameel, K.4
  • 141
    • 84956651497 scopus 로고    scopus 로고
    • The decrease in the IgG-binding capacity of intensively dry heated whey proteins is associated with intense Maillard reaction, structural changes of the proteins and formation of RAGE-ligands
    • Liu F, Teodorowicz M, van Boekel MAJS, Wichers HJ, Hettinga KA. 2016. The decrease in the IgG-binding capacity of intensively dry heated whey proteins is associated with intense Maillard reaction, structural changes of the proteins and formation of RAGE-ligands. Food Funct 7:239–49.
    • (2016) Food Funct , vol.7 , pp. 239-249
    • Liu, F.1    Teodorowicz, M.2    van Boekel, M.A.J.S.3    Wichers, H.J.4    Hettinga, K.A.5
  • 144
    • 84856150284 scopus 로고    scopus 로고
    • In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of β-lactoglobulin are immunologically inert
    • López-Expósito I, Chicón R, Belloque J, López-Fandiño R, Berin M. 2012. In vivo methods for testing allergenicity show that high hydrostatic pressure hydrolysates of β-lactoglobulin are immunologically inert. J Dairy Sci 95:541–8.
    • (2012) J Dairy Sci , vol.95 , pp. 541-548
    • López-Expósito, I.1    Chicón, R.2    Belloque, J.3    López-Fandiño, R.4    Berin, M.5
  • 145
    • 84890675459 scopus 로고    scopus 로고
    • Development of a method for the quantification of caseinate traces in italian commercial white wines based on liquid chromatography-electrospray ionization-ion trap-mass spectrometry
    • Losito I, Introna B, Monaci L, Minella S, Palmisano F. 2013. Development of a method for the quantification of caseinate traces in italian commercial white wines based on liquid chromatography-electrospray ionization-ion trap-mass spectrometry. J Agric Food Chem 61:12436–44.
    • (2013) J Agric Food Chem , vol.61 , pp. 12436-12444
    • Losito, I.1    Introna, B.2    Monaci, L.3    Minella, S.4    Palmisano, F.5
  • 146
    • 4043106251 scopus 로고    scopus 로고
    • A novel approach to the quantification of bovine milk in ovine cheeses using a duplex polymerase chain reaction method
    • Mafra I, Ferreira IMPLVO, Faria MA, Oliveira BPP. 2004. A novel approach to the quantification of bovine milk in ovine cheeses using a duplex polymerase chain reaction method. J Agric Food Chem 52:4943–7.
    • (2004) J Agric Food Chem , vol.52 , pp. 4943-4947
    • Mafra, I.1    Ferreira, I.M.P.L.V.O.2    Faria, M.A.3    Oliveira, B.P.P.4
  • 148
    • 68249159575 scopus 로고    scopus 로고
    • Antigenicity of heat-treated and trypsin-digested milk samples studied by an optical immunochip biosensor
    • Maier I, Lindner W, Pittner F. 2009. Antigenicity of heat-treated and trypsin-digested milk samples studied by an optical immunochip biosensor. Monatsh Chem 140:921–9.
    • (2009) Monatsh Chem , vol.140 , pp. 921-929
    • Maier, I.1    Lindner, W.2    Pittner, F.3
  • 150
    • 0036980025 scopus 로고    scopus 로고
    • Beef allergy in children with cow's milk allergy; cow's milk allergy in children with beef allergy
    • Martelli A, De Chiara A, Corvo M, Restani P, Fiocchi A. 2002. Beef allergy in children with cow's milk allergy; cow's milk allergy in children with beef allergy. Ann Allergy Asthma Immunol 89:38–43.
    • (2002) Ann Allergy Asthma Immunol , vol.89 , pp. 38-43
    • Martelli, A.1    De Chiara, C.M.2    Restani, P.3    Fiocchi, A.4
  • 152
    • 84944172687 scopus 로고    scopus 로고
    • Common food allergens and their IgE-binding epitopes
    • Matsuo H, Yokooji T, Taogoshi T. 2015. Common food allergens and their IgE-binding epitopes. Allergol Intl 64:332–43.
    • (2015) Allergol Intl , vol.64 , pp. 332-343
    • Matsuo, H.1    Yokooji, T.2    Taogoshi, T.3
  • 153
    • 84886656208 scopus 로고    scopus 로고
    • Investigation of different sample pre-treatment routes for liquid chromatography-tandem mass spectrometry detection of caseins and ovalbumin in fortified red wine
    • Mattarozzi M, Milioli M, Bignardi C, Elviri L, Corradini C, Careri M. 2014. Investigation of different sample pre-treatment routes for liquid chromatography-tandem mass spectrometry detection of caseins and ovalbumin in fortified red wine. Food Control 38:82–7.
    • (2014) Food Control , vol.38 , pp. 82-87
    • Mattarozzi, M.1    Milioli, M.2    Bignardi, C.3    Elviri, L.4    Corradini, C.5    Careri, M.6
  • 154
    • 0030849219 scopus 로고    scopus 로고
    • Human IgE binding capacity of tryptic peptides from bovine α-lactalbumin
    • Maynard F, Jost R, Wal JM. 1997. Human IgE binding capacity of tryptic peptides from bovine α-lactalbumin. Intl Arch Allergy Immunol 113:478–88.
    • (1997) Intl Arch Allergy Immunol , vol.113 , pp. 478-488
    • Maynard, F.1    Jost, R.2    Wal, J.M.3
  • 155
    • 85008721431 scopus 로고    scopus 로고
    • Characterization of the potential allergenicity of irradiated bovine α-lactalbumin in a BALB/c mouse model
    • Meng X, Li X, Gao J, Chen H. 2016a. Characterization of the potential allergenicity of irradiated bovine α-lactalbumin in a BALB/c mouse model. Food Chem Toxicol 97:402–10.
    • (2016) Food Chem Toxicol , vol.97 , pp. 402-410
    • Meng, X.1    Li, X.2    Gao, J.3    Chen, H.4
  • 156
    • 84978731531 scopus 로고    scopus 로고
    • Potential allergenicity response to structural modification of irradiated bovine α-lactalbumin
    • Meng X, Li X, Wang X, Gao J, Yang H, Chen H. 2016b. Potential allergenicity response to structural modification of irradiated bovine α-lactalbumin. Food Funct 7:3102–10.
    • (2016) Food Funct , vol.7 , pp. 3102-3110
    • Meng, X.1    Li, X.2    Wang, X.3    Gao, J.4    Yang, H.5    Chen, H.6
  • 159
    • 84958180103 scopus 로고    scopus 로고
    • Identification and quantification of bovine protein lactosylation sites in different milk products
    • Milkovska-Stamenova S, Hoffmann R. 2016. Identification and quantification of bovine protein lactosylation sites in different milk products. J Proteom 134:112–26.
    • (2016) J Proteom , vol.134 , pp. 112-126
    • Milkovska-Stamenova, S.1    Hoffmann, R.2
  • 160
    • 42649101981 scopus 로고    scopus 로고
    • Development of a method for the quantification of whey allergen traces in mixed-fruit juices based on liquid chromatography with mass spectrometric detection
    • Monaci L, van Hengel AJ. 2008. Development of a method for the quantification of whey allergen traces in mixed-fruit juices based on liquid chromatography with mass spectrometric detection. J Chromatogr A 1192:113–20.
    • (2008) J Chromatogr A , vol.1192 , pp. 113-120
    • Monaci, L.1    van Hengel, A.J.2
  • 161
    • 67349171915 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics methods for analysis of food allergens
    • Monaci L, Visconti A. 2009. Mass spectrometry-based proteomics methods for analysis of food allergens. Trends Anal Chem 28:581–91.
    • (2009) Trends Anal Chem , vol.28 , pp. 581-591
    • Monaci, L.1    Visconti, A.2
  • 162
    • 33646798420 scopus 로고    scopus 로고
    • Milk allergens, their characteristics and their detection in food: a review
    • Monaci L, Tregoat V, van Hengel AJ, Anklam E. 2006. Milk allergens, their characteristics and their detection in food: a review. Eur Food Res Technol 223:149–79.
    • (2006) Eur Food Res Technol , vol.223 , pp. 149-179
    • Monaci, L.1    Tregoat, V.2    van Hengel, A.J.3    Anklam, E.4
  • 163
    • 77953542946 scopus 로고    scopus 로고
    • Identification of allergenic milk proteins markers in fined white wines by capillary liquid chromatography-electrospray ionization-tandem mass spectrometry
    • Monaci L, Losito I, Palmisano F, Visconti A. 2010a. Identification of allergenic milk proteins markers in fined white wines by capillary liquid chromatography-electrospray ionization-tandem mass spectrometry. J Chromatogr A 1217:4300–5.
    • (2010) J Chromatogr A , vol.1217 , pp. 4300-4305
    • Monaci, L.1    Losito, I.2    Palmisano, F.3    Visconti, A.4
  • 164
    • 77954895196 scopus 로고    scopus 로고
    • Feasibility of a capillary LC/ESI-Q-TOF MS method for the detection of milk allergens in an incurred model food matrix
    • Monaci L, Nørgaard JV, van Hengel AJ. 2010b. Feasibility of a capillary LC/ESI-Q-TOF MS method for the detection of milk allergens in an incurred model food matrix. Anal Methods 2:967–72.
    • (2010) Anal Methods , vol.2 , pp. 967-972
    • Monaci, L.1    Nørgaard, J.V.2    van Hengel, A.J.3
  • 165
    • 80054812208 scopus 로고    scopus 로고
    • Reliable detection of milk allergens in food using a high-resolution, stand-alone mass spectrometer
    • Monaci L, Losito I, Palmisano F, Visconti A. 2011. Reliable detection of milk allergens in food using a high-resolution, stand-alone mass spectrometer. J AOAC Intl 94:1034–42.
    • (2011) J AOAC Intl , vol.94 , pp. 1034-1042
    • Monaci, L.1    Losito, I.2    Palmisano, F.3    Visconti, A.4
  • 166
    • 84905722171 scopus 로고    scopus 로고
    • Multi-allergen detection in food by micro high-performance liquid chromatography coupled to a dual cell linear ion trap mass spectrometry
    • Monaci L, Pilolli R, De Angelis E, Godula M, Visconti A. 2014. Multi-allergen detection in food by micro high-performance liquid chromatography coupled to a dual cell linear ion trap mass spectrometry. J Chromatogr A 1358:136–44.
    • (2014) J Chromatogr A , vol.1358 , pp. 136-144
    • Monaci, L.1    Pilolli, R.2    De Angelis, G.M.3    Visconti, A.4
  • 169
    • 0041620647 scopus 로고    scopus 로고
    • Thresholds of clinical reactivity to milk, egg, peanut and sesame in immunoglobulin E-dependent allergies: evaluation by double-blind or single-blind placebo-controlled oral challenges
    • Morisset M, Moneret-Vautrin DA, Kanny G, Guénard L, Beaudouin E, Flabbée J, Hatahet R. 2003. Thresholds of clinical reactivity to milk, egg, peanut and sesame in immunoglobulin E-dependent allergies: evaluation by double-blind or single-blind placebo-controlled oral challenges. Clin Exp Allergy 33:1046–51.
    • (2003) Clin Exp Allergy , vol.33 , pp. 1046-1051
    • Morisset, M.1    Moneret-Vautrin, D.A.2    Kanny, G.3    Guénard, L.4    Beaudouin, E.5    Flabbée, J.6    Hatahet, R.7
  • 170
    • 82655171680 scopus 로고    scopus 로고
    • Immunology in the clinic review series; focus on allergies: immunotherapy for food allergy
    • Mousallem T, Burks AW. 2012. Immunology in the clinic review series; focus on allergies: immunotherapy for food allergy. Clin Exp Immunol 167:26–31.
    • (2012) Clin Exp Immunol , vol.167 , pp. 26-31
    • Mousallem, T.1    Burks, A.W.2
  • 175
    • 84879407082 scopus 로고    scopus 로고
    • Quantification of allergenic bovine milk αs1-casein in baked goods using an intact 15N-labeled protein internal standard
    • Newsome GA, Scholl PF. 2012. Quantification of allergenic bovine milk αs1-casein in baked goods using an intact 15N-labeled protein internal standard. J Agric Food Chem 61:5659–68.
    • (2012) J Agric Food Chem , vol.61 , pp. 5659-5668
    • Newsome, G.A.1    Scholl, P.F.2
  • 177
    • 68049123064 scopus 로고    scopus 로고
    • Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity
    • Nowak-Wegrzyn A, Fiocchi A. 2009. Rare, medium, or well done? The effect of heating and food matrix on food protein allergenicity. Curr Opin Allergy Clin Immunol 9:234–7.
    • (2009) Curr Opin Allergy Clin Immunol , vol.9 , pp. 234-237
    • Nowak-Wegrzyn, A.1    Fiocchi, A.2
  • 180
    • 0001581744 scopus 로고
    • Antigenic activities of some peptides derived from residues 1–93
    • Otani H, Mine Y, Hosono A. 1987. Antigenic activities of some peptides derived from residues 1–93. Milchwissenchaft 42:505–8.
    • (1987) Milchwissenchaft , vol.42 , pp. 505-508
    • Otani, H.1    Mine, Y.2    Hosono, A.3
  • 181
    • 33646494005 scopus 로고    scopus 로고
    • Effects of combined high pressure and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins
    • Peñas E, Préstamo G, Luisa Baeza M, Martínez-Molero MI, Gomez R. 2006. Effects of combined high pressure and enzymatic treatments on the hydrolysis and immunoreactivity of dairy whey proteins. Intl Dairy J 16:831–9.
    • (2006) Intl Dairy J , vol.16 , pp. 831-839
    • Peñas, E.1    Préstamo, G.2    Luisa Baeza, M.3    Martínez-Molero, M.I.4    Gomez, R.5
  • 182
    • 84871608855 scopus 로고    scopus 로고
    • In vitro gastric digestion of heat-induced aggregates of β-lactoglobulin
    • Peram MR, Loveday SM, Ye A, Singh H. 2013. In vitro gastric digestion of heat-induced aggregates of β-lactoglobulin. J Dairy Sci 96:63–74.
    • (2013) J Dairy Sci , vol.96 , pp. 63-74
    • Peram, M.R.1    Loveday, S.M.2    Ye, A.3    Singh, H.4
  • 183
    • 79952314454 scopus 로고    scopus 로고
    • Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin
    • Pescuma M, Hébert EM, Rabesona H, Drouet M, Choiset Y, Haertlé T, Mozzi F, De Valdez GF, Chobert JM. 2011. Proteolytic action of Lactobacillus delbrueckii subsp. bulgaricus CRL 656 reduces antigenic response to bovine β-lactoglobulin. Food Chem 127:487–92.
    • (2011) Food Chem , vol.127 , pp. 487-492
    • Pescuma, M.1    Hébert, E.M.2    Rabesona, H.3    Drouet, M.4    Choiset, Y.5    Haertlé, T.6    Mozzi, F.7    De Valdez, C.J.M.8
  • 184
    • 84960089723 scopus 로고    scopus 로고
    • Whey protein isolate hydrolysates obtained with free and immobilized alcalase: Characterization and detection of residual allergens
    • Pessato TB, Carvalho NC, Tavano OL, Fernandes LGR, Zollner RL, Netto FM. 2016. Whey protein isolate hydrolysates obtained with free and immobilized alcalase: Characterization and detection of residual allergens. Food Res Intl 83:112–120.
    • (2016) Food Res Intl , vol.83 , pp. 112-120
    • Pessato, T.B.1    Carvalho, N.C.2    Tavano, O.L.3    Fernandes, L.G.R.4    Zollner, R.L.5    Netto, F.M.6
  • 185
    • 0017694018 scopus 로고
    • Immunochemical studies of fragments of bovine serum albumin
    • Peters T, Feldhoff RC, Reed RG. 1977. Immunochemical studies of fragments of bovine serum albumin. J Biol Chem 252:8464–8.
    • (1977) J Biol Chem , vol.252 , pp. 8464-8468
    • Peters, T.1    Feldhoff, R.C.2    Reed, R.G.3
  • 186
    • 43049141557 scopus 로고    scopus 로고
    • Identification of proteolytic bacteria from thai traditional fermented foods and their allergenic reducing potentials
    • Phromraksa P, Nagano H, Boonmars T, Kamboonruang C. 2008. Identification of proteolytic bacteria from thai traditional fermented foods and their allergenic reducing potentials. J Food Sci 73:M189–95.
    • (2008) J Food Sci , vol.73 , pp. M189-M195
    • Phromraksa, P.1    Nagano, H.2    Boonmars, T.3    Kamboonruang, C.4
  • 187
    • 74049126072 scopus 로고    scopus 로고
    • Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications
    • Picariello G, Ferranti P, Fierro O, Mamone G, Caira S, Di Luccia A, Monica S, Addeo F. 2010. Peptides surviving the simulated gastrointestinal digestion of milk proteins: Biological and toxicological implications. J Chrom B 878:295–308.
    • (2010) J Chrom B , vol.878 , pp. 295-308
    • Picariello, G.1    Ferranti, P.2    Fierro, O.3    Mamone, G.4    Caira, S.5    Di Luccia, A.6    Monica, S.7    Addeo, F.8
  • 188
    • 80053304692 scopus 로고    scopus 로고
    • The frontiers of mass spectrometry-based techniques in food allergenomics
    • Picariello G, Mamone G, Addeo F, Ferranti P. 2011. The frontiers of mass spectrometry-based techniques in food allergenomics. J Chromatogr A 1218:7386–98.
    • (2011) J Chromatogr A , vol.1218 , pp. 7386-7398
    • Picariello, G.1    Mamone, G.2    Addeo, F.3    Ferranti, P.4
  • 190
    • 84915782420 scopus 로고    scopus 로고
    • Orbitrap monostage MS versus hybrid linear ion trap MS: application to multi-allergen screening in wine
    • Pilolli R, De Angelis E, Godula M, Visconti A, Monaci L. 2014. Orbitrap monostage MS versus hybrid linear ion trap MS: application to multi-allergen screening in wine. J Mass Spectrom 49:1254–63.
    • (2014) J Mass Spectrom , vol.49 , pp. 1254-1263
    • Pilolli, R.1    De Angelis, G.M.2    Visconti, A.3    Monaci, L.4
  • 191
    • 0141703210 scopus 로고    scopus 로고
    • Use of goat's milk in patients with cow's milk allergy
    • Pina ID, Tormo Carnice R, Conde Zandueta M. 2003. Use of goat's milk in patients with cow's milk allergy. An Pediatr 59:138–42.
    • (2003) An Pediatr , vol.59 , pp. 138-142
    • Pina, I.D.1    Tormo Carnice, R.2    Conde Zandueta, M.3
  • 192
    • 84991051636 scopus 로고    scopus 로고
    • Advances in ultra-high performance liquid chromatography coupled to tandem mass spectrometry for sensitive detection of several food allergens in complex and processed foodstuffs
    • Planque M, Arnould T, Dieu M, Delahaut P, Renard P, Gillard N. 2016. Advances in ultra-high performance liquid chromatography coupled to tandem mass spectrometry for sensitive detection of several food allergens in complex and processed foodstuffs. J Chromatogr A 1464:115–23.
    • (2016) J Chromatogr A , vol.1464 , pp. 115-123
    • Planque, M.1    Arnould, T.2    Dieu, M.3    Delahaut, P.4    Renard, P.5    Gillard, N.6
  • 193
    • 1142287446 scopus 로고    scopus 로고
    • Methods for allergen analysis in food: a review
    • Poms RE, Klein CL, Anklam E. 2004. Methods for allergen analysis in food: a review. Food Addit Contam 21:1–31.
    • (2004) Food Addit Contam , vol.21 , pp. 1-31
    • Poms, R.E.1    Klein, C.L.2    Anklam, E.3
  • 195
    • 1642316967 scopus 로고    scopus 로고
    • Stimulation of interleukin-10 production by acidic β-lactoglobulin-derived peptides hydrolyzed with Lactobacillus paracasei NCC2461 peptidases
    • Prioult G, Pecquet S, Fliss I. 2004. Stimulation of interleukin-10 production by acidic β-lactoglobulin-derived peptides hydrolyzed with Lactobacillus paracasei NCC2461 peptidases. Clin Diagn Lab Immunol 11:266–71.
    • (2004) Clin Diagn Lab Immunol , vol.11 , pp. 266-271
    • Prioult, G.1    Pecquet, S.2    Fliss, I.3
  • 196
    • 16244416867 scopus 로고    scopus 로고
    • Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes
    • Prioult G, Pecquet S, Fliss I. 2005. Allergenicity of acidic peptides from bovine β-lactoglobulin is reduced by hydrolysis with Bifidobacterium lactis NCC362 enzymes. Intl Dairy J 15:439–48.
    • (2005) Intl Dairy J , vol.15 , pp. 439-448
    • Prioult, G.1    Pecquet, S.2    Fliss, I.3
  • 197
    • 85018333748 scopus 로고    scopus 로고
    • Reduction of whey protein concentrate antigenicity by using a combined enzymatic digestion and ultrafiltration approach
    • Quintieri L, Monaci L, Baruzzi F, Giuffrida MG, de Candia S, Caputo L. 2017. Reduction of whey protein concentrate antigenicity by using a combined enzymatic digestion and ultrafiltration approach. J Food Sci Technol 54:1910–6.
    • (2017) J Food Sci Technol , vol.54 , pp. 1910-1916
    • Quintieri, L.1    Monaci, L.2    Baruzzi, F.3    Giuffrida, M.G.4    de Candia, S.5    Caputo, L.6
  • 198
    • 84957889521 scopus 로고    scopus 로고
    • Effect of processing on conformational changes of food proteins related to allergenicity
    • Rahaman T, Vasiljevic T, Ramchandran L. 2016. Effect of processing on conformational changes of food proteins related to allergenicity. Trends Food Sci Technol 49:24–34.
    • (2016) Trends Food Sci Technol , vol.49 , pp. 24-34
    • Rahaman, T.1    Vasiljevic, T.2    Ramchandran, L.3
  • 199
    • 77958027429 scopus 로고    scopus 로고
    • Food allergens profiling with an imaging surface plasmon resonance-based biosensor
    • Raz SR, Liu H, Norde W, Bremer MGEG. 2010. Food allergens profiling with an imaging surface plasmon resonance-based biosensor. Anal Chem 82:8485–91.
    • (2010) Anal Chem , vol.82 , pp. 8485-8491
    • Raz, S.R.1    Liu, H.2    Norde, W.3    Bremer, M.G.E.G.4
  • 200
    • 85013196607 scopus 로고    scopus 로고
    • Potential applications of milk fractions and valorization of dairy by-products: a review of the state-of-the-art available data, outlining the innovation potential from a bigger data standpoint
    • Rebouillat S, Ortega-Requena S. 2015. Potential applications of milk fractions and valorization of dairy by-products: a review of the state-of-the-art available data, outlining the innovation potential from a bigger data standpoint. J Biomater Nanobiotechnol 6:176–203.
    • (2015) J Biomater Nanobiotechnol , vol.6 , pp. 176-203
    • Rebouillat, S.1    Ortega-Requena, S.2
  • 202
    • 84885172572 scopus 로고    scopus 로고
    • Detection of allergenic parvalbumin of Atlantic and Pacific herrings in fish products by PCR
    • Rencova E, Kostelnikova D, Tremlova B. 2013. Detection of allergenic parvalbumin of Atlantic and Pacific herrings in fish products by PCR. Food Addit Contam Part A-Chem 30:1679–83.
    • (2013) Food Addit Contam Part A-Chem , vol.30 , pp. 1679-1683
    • Rencova, E.1    Kostelnikova, D.2    Tremlova, B.3
  • 205
    • 3442890649 scopus 로고    scopus 로고
    • Characterization of bovine serum albumin epitopes and their role in allergic reactions
    • Restani P, Ballabio C, Cattaneo A, Isoardi P, Terracciano L, Fiocchi A. 2004. Characterization of bovine serum albumin epitopes and their role in allergic reactions. Allergy 59:21–4.
    • (2004) Allergy , vol.59 , pp. 21-24
    • Restani, P.1    Ballabio, C.2    Cattaneo, A.3    Isoardi, P.4    Terracciano, L.5    Fiocchi, A.6
  • 207
    • 0036378387 scopus 로고    scopus 로고
    • Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk
    • Rozenfeld P, Docena GH, Fossati MCA. 2002. Detection and identification of a soy protein component that cross-reacts with caseins from cow's milk. Clin Exp Immunol 130:49–58.
    • (2002) Clin Exp Immunol , vol.130 , pp. 49-58
    • Rozenfeld, P.1    Docena, G.H.2    Fossati, M.C.A.3
  • 210
    • 85021686257 scopus 로고    scopus 로고
    • Protein degradation and peptide release from milk proteins in human jejunum. Comparison with in vitro gastrointestinal simulation
    • Sanchón J, Fernández-Tomé S, Miralles B, Hernández-Ledesma B, Tomé D, Gaudichon C, Recio I. 2018. Protein degradation and peptide release from milk proteins in human jejunum. Comparison with in vitro gastrointestinal simulation. Food Chem 239:486–94.
    • (2018) Food Chem , vol.239 , pp. 486-494
    • Sanchón, J.1    Fernández-Tomé, S.2    Miralles, B.3    Hernández-Ledesma, B.4    Tomé, D.5    Gaudichon, C.6    Recio, I.7
  • 212
    • 84885156681 scopus 로고    scopus 로고
    • Changes in functional properties of milk protein powders: effects of vacuum concentration and drying
    • Schuck P, le Floch-Fouere C, Jeantet R. 2013. Changes in functional properties of milk protein powders: effects of vacuum concentration and drying. Drying Technol 31:1578–91.
    • (2013) Drying Technol , vol.31 , pp. 1578-1591
    • Schuck, P.1    le Floch-Fouere, C.2    Jeantet, R.3
  • 213
  • 216
    • 84888095981 scopus 로고    scopus 로고
    • Effects of fermentation by Lactobacillus casei on the antigenicity and allergenicity of four bovine milk proteins
    • Shi J, Luo Y, Xiao Y, Li Z, Xu Q, Yao M. 2014. Effects of fermentation by Lactobacillus casei on the antigenicity and allergenicity of four bovine milk proteins. Intl Dairy J 35:75–80.
    • (2014) Intl Dairy J , vol.35 , pp. 75-80
    • Shi, J.1    Luo, Y.2    Xiao, Y.3    Li, Z.4    Xu, Q.5    Yao, M.6
  • 219
    • 49749107597 scopus 로고    scopus 로고
    • Differential influence of the degree of processing on immunogenicity following proteolysis of casein and β-lactoglobulin
    • Sletten GBG, Holden L, Egaas E, Faeste CK. 2008. Differential influence of the degree of processing on immunogenicity following proteolysis of casein and β-lactoglobulin. Food Agric Immunol 19:213–28.
    • (2008) Food Agric Immunol , vol.19 , pp. 213-228
    • Sletten, G.B.G.1    Holden, L.2    Egaas, E.3    Faeste, C.K.4
  • 221
    • 2442637545 scopus 로고    scopus 로고
    • A biological perspective on the structure and function of caseins and casein micelles
    • Smyth E, Clegg RA, Holt C. 2004. A biological perspective on the structure and function of caseins and casein micelles. Intl J Dairy Technol 57:121–6.
    • (2004) Intl J Dairy Technol , vol.57 , pp. 121-126
    • Smyth, E.1    Clegg, R.A.2    Holt, C.3
  • 228
    • 84942058308 scopus 로고    scopus 로고
    • β-Lactoglobulin mutant Lys69Asn has attenuated IgE and increased retinol binding activity
    • Taheri-Kafrani A, Koupaie NT, Haertlé T. 2015. β-Lactoglobulin mutant Lys69Asn has attenuated IgE and increased retinol binding activity. J Biotechnol 212:181–8.
    • (2015) J Biotechnol , vol.212 , pp. 181-188
    • Taheri-Kafrani, A.1    Koupaie, N.T.2    Haertlé, T.3
  • 229
    • 85039943810 scopus 로고    scopus 로고
    • Recent advances in processing for reducing dairy and food allergenicity
    • Tammineedi CV, Choudhary R. 2014. Recent advances in processing for reducing dairy and food allergenicity. Intl J Food Sci Nutr Eng 4:36–42.
    • (2014) Intl J Food Sci Nutr Eng , vol.4 , pp. 36-42
    • Tammineedi, C.V.1    Choudhary, R.2
  • 230
    • 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
    • Tammineedi CVRK, Choudhary R, Perez-Alvarado GC, Watson DG. 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 Sci Technol 54:35–41.
    • (2013) LWT - Food Sci Technol , vol.54 , pp. 35-41
    • Tammineedi, C.V.R.K.1    Choudhary, R.2    Perez-Alvarado, G.C.3    Watson, D.G.4
  • 232
    • 84930147195 scopus 로고    scopus 로고
    • Worldwide food allergy labeling and detection of allergens in processed foods
    • In, Ebisawa M, Ballmer-Weber BK, Vieths S, Wood RA, editors., Basel, Karger Publishers, p
    • Taylor SL, Baumert JL. 2015. Worldwide food allergy labeling and detection of allergens in processed foods. In: Ebisawa M, Ballmer-Weber BK, Vieths S, Wood RA, editors. Food allergy: molecular basis and clinical practice. Basel: Karger Publishers. p 227–34.
    • (2015) Food allergy: molecular basis and clinical practice , pp. 227-234
    • Taylor, S.L.1    Baumert, J.L.2
  • 235
    • 84911985348 scopus 로고    scopus 로고
    • Investigation of incurred single- and multi-component model food matrices for determination of food proteins triggering allergy and coeliac disease
    • Török K, Horváth V, Horváth Á, Hajas L, Bugyi Z, Tömösközi S. 2014. Investigation of incurred single- and multi-component model food matrices for determination of food proteins triggering allergy and coeliac disease. Eur Food Res Technol 239:923–32.
    • (2014) Eur Food Res Technol , vol.239 , pp. 923-932
    • Török, K.1    Horváth, V.2    Horváth, Á.3    Hajas, L.4    Bugyi, Z.5    Tömösközi, S.6
  • 244
    • 0034974942 scopus 로고    scopus 로고
    • Structure and function of milk allergens
    • Wal J. 2001. Structure and function of milk allergens. Allergy 56:35–8.
    • (2001) Allergy , vol.56 , pp. 35-38
    • Wal, J.1
  • 245
    • 8644235852 scopus 로고    scopus 로고
    • Bovine milk allergenicity
    • Wal J. 2004. Bovine milk allergenicity. Ann Allergy Asthma Immunol 93:S2–11.
    • (2004) Ann Allergy Asthma Immunol , vol.93 , pp. S2-11
    • Wal, J.1
  • 246
    • 0032199537 scopus 로고    scopus 로고
    • Cow's milk allergens
    • Wal JM. 1998. Cow's milk allergens. Allergy 53:1013–22.
    • (1998) Allergy , vol.53 , pp. 1013-1022
    • Wal, J.M.1
  • 247
    • 0036977345 scopus 로고    scopus 로고
    • Cow's milk proteins/allergens
    • Wal JM. 2002. Cow's milk proteins/allergens. Ann Allergy Asthma Immunol 89:3–10.
    • (2002) Ann Allergy Asthma Immunol , vol.89 , pp. 3-10
    • Wal, J.M.1
  • 248
    • 3342965285 scopus 로고    scopus 로고
    • Lactoferrin: role in iron homeostasis and host defense against microbial infection
    • Ward PP, Conneely OM. 2004. Lactoferrin: role in iron homeostasis and host defense against microbial infection. Biometals 17:203–8.
    • (2004) Biometals , vol.17 , pp. 203-208
    • Ward, P.P.1    Conneely, O.M.2
  • 249
    • 0031817073 scopus 로고    scopus 로고
    • Identification of epitopes within β-lactoglobulin recognised by polyclonal antibodies using phage display and PEPSCAN
    • Williams S, Badley R, Davis P, Puijk W, Meloen R. 1998. Identification of epitopes within β-lactoglobulin recognised by polyclonal antibodies using phage display and PEPSCAN. J Immunol Methods 213:1–17.
    • (1998) J Immunol Methods , vol.213 , pp. 1-17
    • Williams, S.1    Badley, R.2    Davis, P.3    Puijk, W.4    Meloen, R.5
  • 250
    • 84959325791 scopus 로고    scopus 로고
    • Lactobacillus casei LcY decreases milk protein immunoreactivity of fermented buttermilk but also contains IgE-reactive proteins
    • Wróblewska B, Markiewicz LH, Szyc AM, Dietrich MA, Szymkiewicz A, Fotschki J. 2016. Lactobacillus casei LcY decreases milk protein immunoreactivity of fermented buttermilk but also contains IgE-reactive proteins. Food Res Intl 83:95–101.
    • (2016) Food Res Intl , vol.83 , pp. 95-101
    • Wróblewska, B.1    Markiewicz, L.H.2    Szyc, A.M.3    Dietrich, M.A.4    Szymkiewicz, A.5    Fotschki, J.6
  • 251
    • 84889022403 scopus 로고    scopus 로고
    • Conjugation of functional oligosaccharides reduced in vitro allergenicity of β-lactoglobulin
    • Wu X, Liu M, Xia L, Wu H, Liu Z, Xu X. 2013. Conjugation of functional oligosaccharides reduced in vitro allergenicity of β-lactoglobulin. Food Agric Immunol 24:379–91.
    • (2013) Food Agric Immunol , vol.24 , pp. 379-391
    • Wu, X.1    Liu, M.2    Xia, L.3    Wu, H.4    Liu, Z.5    Xu, X.6
  • 252
    • 0029081772 scopus 로고
    • Allergy to cheese produced from sheep's and goat's milk but not to cheese produced from cow's milk
    • Wüthrich B, Johansson SGO. 1995. Allergy to cheese produced from sheep's and goat's milk but not to cheese produced from cow's milk. J Allergy Clin Immunol 96:270–3.
    • (1995) J Allergy Clin Immunol , vol.96 , pp. 270-273
    • Wüthrich, B.1    Johansson, S.G.O.2
  • 253
    • 84957842379 scopus 로고    scopus 로고
    • Development of a real-time quantitative PCR assay using a TaqMan minor groove binder probe for the detection of α-lactalbumin in food
    • Xiao G, Qin C, Wenju Z, Qin C. 2016. Development of a real-time quantitative PCR assay using a TaqMan minor groove binder probe for the detection of α-lactalbumin in food. J Dairy Sci 99:1716–24.
    • (2016) J Dairy Sci , vol.99 , pp. 1716-1724
    • Xiao, G.1    Qin, C.2    Wenju, Z.3    Qin, C.4
  • 254
    • 84959910820 scopus 로고    scopus 로고
    • Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates
    • Xu Q, Shi J, Yao M, Jiang M, Luo Y. 2016. Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates. Food Agric Immunol 27:401–13.
    • (2016) Food Agric Immunol , vol.27 , pp. 401-413
    • Xu, Q.1    Shi, J.2    Yao, M.3    Jiang, M.4    Luo, Y.5
  • 255
    • 84926144492 scopus 로고    scopus 로고
    • Effects of fermentation by Lactobacillus rhamnosus GG on the antigenicity and allergenicity of four cows' milk proteins
    • Yao M, Luo Y, Shi J, Zhou Y, Xu Q, Li Z. 2014. Effects of fermentation by Lactobacillus rhamnosus GG on the antigenicity and allergenicity of four cows' milk proteins. Food Agric Immunol 25:545–55.
    • (2014) Food Agric Immunol , vol.25 , pp. 545-555
    • Yao, M.1    Luo, Y.2    Shi, J.3    Zhou, Y.4    Xu, Q.5    Li, Z.6
  • 256
    • 36348936097 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin
    • Zeece M, Huppertz T, Kelly A. 2008. Effect of high-pressure treatment on in-vitro digestibility of β-lactoglobulin. Innov Food Sci Emerg Technol 9:62–9.
    • (2008) Innov Food Sci Emerg Technol , vol.9 , pp. 62-69
    • Zeece, M.1    Huppertz, T.2    Kelly, A.3
  • 257
    • 33847343534 scopus 로고    scopus 로고
    • A TaqMan real-time PCR system for the identification and quantification of bovine DNA in meats, milks and cheeses
    • Zhang CL, Fowler MR, Scott NW, Lawson G, Slater A. 2007. A TaqMan real-time PCR system for the identification and quantification of bovine DNA in meats, milks and cheeses. Food Control 18:1149–58.
    • (2007) Food Control , vol.18 , pp. 1149-1158
    • Zhang, C.L.1    Fowler, M.R.2    Scott, N.W.3    Lawson, G.4    Slater, A.5
  • 258
    • 79959302375 scopus 로고    scopus 로고
    • Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin
    • Zhong J, Liu C, Liu W, Cai X, Tu Z, Wan J. 2011. Effect of dynamic high-pressure microfluidization at different temperatures on the antigenic response of bovine β-lactoglobulin. Eur Food Res Technol 233:95–102.
    • (2011) Eur Food Res Technol , vol.233 , pp. 95-102
    • Zhong, J.1    Liu, C.2    Liu, W.3    Cai, X.4    Tu, Z.5    Wan, J.6
  • 259
    • 84901738261 scopus 로고    scopus 로고
    • Steady-state kinetics of tryptic hydrolysis of β-lactoglobulin after dynamic high-pressure microfluidization treatment in relation to antigenicity
    • Zhong J, Luo S, Liu C, Liu W. 2014. Steady-state kinetics of tryptic hydrolysis of β-lactoglobulin after dynamic high-pressure microfluidization treatment in relation to antigenicity. Eur Food Res Technol 239:525–31.
    • (2014) Eur Food Res Technol , vol.239 , pp. 525-531
    • Zhong, J.1    Luo, S.2    Liu, C.3    Liu, W.4
  • 260
    • 84930216543 scopus 로고    scopus 로고
    • Comparative study on the effects of nystose and fructofuranosyl nystose in the glycation reaction on the antigenicity and conformation of β-lactoglobulin
    • Zhong J, Tu Y, Liu W, Luo S, Liu C. 2015. Comparative study on the effects of nystose and fructofuranosyl nystose in the glycation reaction on the antigenicity and conformation of β-lactoglobulin. Food Chem 188:658–63.
    • (2015) Food Chem , vol.188 , pp. 658-663
    • Zhong, J.1    Tu, Y.2    Liu, W.3    Luo, S.4    Liu, C.5
  • 261
    • 84954173432 scopus 로고    scopus 로고
    • Purification and conformational changes of bovine PEGylated β-lactoglobulin related to antigenicity
    • Zhong J, Cai X, Liu C, Liu W, Xu Y, Luo S. 2016. Purification and conformational changes of bovine PEGylated β-lactoglobulin related to antigenicity. Food Chem 199:387–92.
    • (2016) Food Chem , vol.199 , pp. 387-392
    • Zhong, J.1    Cai, X.2    Liu, C.3    Liu, W.4    Xu, Y.5    Luo, S.6
  • 262
    • 84876734132 scopus 로고    scopus 로고
    • Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes
    • Zhong JZ, Xu YJ, Liu W, Liu CM, Luo SJ, Tu ZC. 2013. Antigenicity and functional properties of β-lactoglobulin conjugated with fructo-oligosaccharides in relation to conformational changes. J Dairy Sci 96:2808–15.
    • (2013) J Dairy Sci , vol.96 , pp. 2808-2815
    • Zhong, J.Z.1    Xu, Y.J.2    Liu, W.3    Liu, C.M.4    Luo, S.J.5    Tu, Z.C.6


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