메뉴 건너뛰기




Volumn 27, Issue 3, 2016, Pages 401-413

Effects of heat treatment on the antigenicity of four milk proteins in milk protein concentrates

Author keywords

antigenicity; heat treatment; Milk protein concentrates; potential allergenicity

Indexed keywords


EID: 84959910820     PISSN: 09540105     EISSN: 14653443     Source Type: Journal    
DOI: 10.1080/09540105.2015.1117059     Document Type: Article
Times cited : (42)

References (35)
  • 2
    • 70350044740 scopus 로고    scopus 로고
    • Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology
    • G.H.Bu,, J.Lu,, Z.Zheng,, & Y.K.Luo, (2009). Influence of Maillard reaction conditions on the antigenicity of bovine α-lactalbumin using response surface methodology. Journal of the Science of Food and Agriculture, 89(14), 2428–2434. doi: 10.1002/jsfa.3741
    • (2009) Journal of the Science of Food and Agriculture , vol.89 , Issue.14 , pp. 2428-2434
    • Bu, G.H.1    Lu, J.2    Zheng, Z.3    Luo, Y.K.4
  • 3
    • 77955939723 scopus 로고    scopus 로고
    • Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins
    • G.H.Bu,, Y.K.Luo,, Y.Zhang,, & F.S.Chen, (2010). Effects of fermentation by lactic acid bacteria on the antigenicity of bovine whey proteins. Journal of the Science of Food and Agriculture, 90(12), 2015–2020.
    • (2010) Journal of the Science of Food and Agriculture , vol.90 , Issue.12 , pp. 2015-2020
    • Bu, G.H.1    Luo, Y.K.2    Zhang, Y.3    Chen, F.S.4
  • 4
    • 70449410078 scopus 로고    scopus 로고
    • Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate
    • G.H.Bu,, Y.K.Luo,, Z.Zheng,, & H.Zheng, (2009). Effect of heat treatment on the antigenicity of bovine α-lactalbumin and β-lactoglobulin in whey protein isolate. Food and Agricultural Immunology, 20(3), 195–206. doi: 10.1080/09540100903026116
    • (2009) Food and Agricultural Immunology , vol.20 , Issue.3 , pp. 195-206
    • Bu, G.H.1    Luo, Y.K.2    Zheng, Z.3    Zheng, H.4
  • 5
    • 33745005553 scopus 로고    scopus 로고
    • A novel conformation-dependent monoclonal antibody specific to the native structure of β-Lactoglobulin and Its application
    • W.L.Chen,, W.T.Liu,, M.C.Yang,, M.T.Hwang,, J.H.Tsao,, & S.J.T.Mao, (2006). A novel conformation-dependent monoclonal antibody specific to the native structure of β-Lactoglobulin and Its application. Journal of Dairy Science, 89(3), 912–921. doi: 10.3168/jds.S0022-0302(06)72156-7
    • (2006) Journal of Dairy Science , vol.89 , Issue.3 , pp. 912-921
    • Chen, W.L.1    Liu, W.T.2    Yang, M.C.3    Hwang, M.T.4    Tsao, J.H.5    Mao, S.J.T.6
  • 6
    • 0036852998 scopus 로고    scopus 로고
    • Kinetics of alkaline phosphatase and lactoperoxidase inactivation, and of β-lactoglobulin denaturation in milk with different fat content
    • W.L.Claeys,, A.M.Van Loey,, & M.E.Hendrickx, (2002). Kinetics of alkaline phosphatase and lactoperoxidase inactivation, and of β-lactoglobulin denaturation in milk with different fat content. Journal of Dairy Research, 69(4), 541–553. doi: 10.1017/S0022029902005721
    • (2002) Journal of Dairy Research , vol.69 , Issue.4 , pp. 541-553
    • Claeys, W.L.1    Van Loey, A.M.2    Hendrickx, M.E.3
  • 8
    • 0031758168 scopus 로고    scopus 로고
    • Protein modification by thermal processing
    • P.Davis,, & S.Williams, (1998). Protein modification by thermal processing. Allergy, 53(s46), 102–105. doi: 10.1111/j.1398-9995.1998.tb04975.x
    • (1998) Allergy , vol.53 , Issue.s46 , pp. 102-105
    • Davis, P.1    Williams, S.2
  • 9
    • 84875398710 scopus 로고    scopus 로고
    • Assessing the heat induced changes in major cow and non-cow whey proteins conformation on kinetic and thermodynamic basis
    • L.Dumitraşcu,, E.Moschopoulou,, I.Aprodu,, S.Stanciu,, G.Râpeanu,, & N.Stănciuc, (2013). Assessing the heat induced changes in major cow and non-cow whey proteins conformation on kinetic and thermodynamic basis. Small Ruminant Research, 111(1–3), 129–138. doi: 10.1016/j.smallrumres.2012.12.019
    • (2013) Small Ruminant Research , vol.111 , Issue.1-3 , pp. 129-138
    • Dumitraşcu, L.1    Moschopoulou, E.2    Aprodu, I.3    Stanciu, S.4    Râpeanu, G.5    Stănciuc, N.6
  • 10
    • 79953831690 scopus 로고    scopus 로고
    • Heat treatment of milk during powder manufacture increases casein resistance to simulated infant digestion
    • D.Dupont,, R.Boutrou,, O.Menard,, J.Jardin,, G.Tanguy,, P.Schuck,, … J.Leonil,. (2010). Heat treatment of milk during powder manufacture increases casein resistance to simulated infant digestion. Food Digestion, 1(1–2), 28–39. doi: 10.1007/s13228-010-0003-0
    • (2010) Food Digestion , vol.1 , Issue.1-2 , pp. 28-39
    • Dupont, D.1    Boutrou, R.2    Menard, O.3    Jardin, J.4    Tanguy, G.5    Schuck, P.6    Leonil, J.7
  • 11
    • 1542286920 scopus 로고    scopus 로고
    • Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin
    • B.-M.Ehn,, B.Ekstrand,, U.Bengtsson,, & S.Ahlstedt, (2004). Modification of IgE binding during heat processing of the cow's milk allergen β-lactoglobulin. Journal of Agricultural and Food Chemistry, 52(5), 1398–1403. doi: 10.1021/jf0304371
    • (2004) Journal of Agricultural and Food Chemistry , vol.52 , Issue.5 , pp. 1398-1403
    • Ehn, B.-M.1    Ekstrand, B.2    Bengtsson, U.3    Ahlstedt, S.4
  • 12
    • 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(1–2), 64–72. doi: 10.1016/j.smallrumres.2006.09.016
    • (2007) Small Ruminant Research , vol.68 , Issue.1-2 , pp. 64-72
    • El-Agamy, E.I.1
  • 13
    • 84865964632 scopus 로고    scopus 로고
    • Molecular dynamics simulation of the effect of heat on the conformation of bovine β-lactoglobulin A: A comparison of conventional and accelerated methods
    • S.R.Euston, (2013). Molecular dynamics simulation of the effect of heat on the conformation of bovine β-lactoglobulin A: A comparison of conventional and accelerated methods. Food Hydrocolloids, 30(2), 519–530. doi: 10.1016/j.foodhyd.2012.07.016
    • (2013) Food Hydrocolloids , vol.30 , Issue.2 , pp. 519-530
    • Euston, S.R.1
  • 14
    • 0036704306 scopus 로고    scopus 로고
    • Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins
    • M.A.de la Fuente,, H.Singh,, & Y.Hemar, (2002). Recent advances in the characterisation of heat-induced aggregates and intermediates of whey proteins. Trends in Food Science & Technology, 13(8), 262–274. doi: 10.1016/S0924-2244(02)00133-4
    • (2002) Trends in Food Science & Technology , vol.13 , Issue.8 , pp. 262-274
    • de la Fuente, M.A.1    Singh, H.2    Hemar, Y.3
  • 15
    • 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(5), 779–783. doi: 10.1007/s00217-009-1114-0
    • (2009) European Food Research and Technology , vol.229 , Issue.5 , pp. 779-783
    • Grar, H.1    Kaddouri, H.2    Gourine, H.3    Negaoui, H.4    Kheroua, O.5    Saïdi, D.6
  • 16
    • 79953703693 scopus 로고    scopus 로고
    • High-pressure microfluidisation-induced changes in the antigenicity and conformation of allergen Ara h 2 purified from Chinese peanut
    • C.Q.Hu,, H.B.Chen,, J.Y.Gao,, C.P.Luo,, X.J.Ma,, & P.Tong, (2011). High-pressure microfluidisation-induced changes in the antigenicity and conformation of allergen Ara h 2 purified from Chinese peanut. Journal of the Science of Food and Agriculture, 91(7), 1304–1309. doi: 10.1002/jsfa.4318
    • (2011) Journal of the Science of Food and Agriculture , vol.91 , Issue.7 , pp. 1304-1309
    • Hu, C.Q.1    Chen, H.B.2    Gao, J.Y.3    Luo, C.P.4    Ma, X.J.5    Tong, P.6
  • 17
    • 84865485855 scopus 로고    scopus 로고
    • Effect of thermal processing and gamma-irradiation on allergenicity of legume proteins
    • R.Kasera,, A.B.Singh,, R.Kumar,, S.Lavasa,, K.N.Prasad,, & N.Arora, (2012). Effect of thermal processing and gamma-irradiation on allergenicity of legume proteins. Food and Chemical Toxicology, 50(10), 3456–3461. doi: 10.1016/j.fct.2012.07.031
    • (2012) Food and Chemical Toxicology , vol.50 , Issue.10 , pp. 3456-3461
    • Kasera, R.1    Singh, A.B.2    Kumar, R.3    Lavasa, S.4    Prasad, K.N.5    Arora, N.6
  • 18
    • 21044455900 scopus 로고    scopus 로고
    • The antigenic response of ?-lactoglobulin is modulated by thermally induced aggregation
    • N.Kleber,, I.Krause,, S.Illgner,, & J.R.Hinrichs, (2004). The antigenic response of ?-lactoglobulin is modulated by thermally induced aggregation. European Food Research and Technology, 219(2), 105–110. doi: 10.1007/s00217-004-0924-3
    • (2004) European Food Research and Technology , vol.219 , Issue.2 , pp. 105-110
    • Kleber, N.1    Krause, I.2    Illgner, S.3    Hinrichs, J.R.4
  • 19
    • 33846785047 scopus 로고    scopus 로고
    • Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature
    • N.Kleber,, S.Maier,, & J.Hinrichs, (2007). Antigenic response of bovine β-lactoglobulin influenced by ultra-high pressure treatment and temperature. Innovative Food Science & Emerging Technologies, 8(1), 39–45. doi: 10.1016/j.ifset.2006.05.001
    • (2007) Innovative Food Science & Emerging Technologies , vol.8 , Issue.1 , pp. 39-45
    • Kleber, N.1    Maier, S.2    Hinrichs, J.3
  • 20
    • 33746733581 scopus 로고    scopus 로고
    • Screening for lactic acid bacteria with potential to reduce antigenic response of β-lactoglobulin in bovine skim milk and sweet whey
    • N.Kleber,, U.Weyrich,, & J.Hinrichs, (2006). Screening for lactic acid bacteria with potential to reduce antigenic response of β-lactoglobulin in bovine skim milk and sweet whey. Innovative Food Science & Emerging Technologies, 7(3), 233–238. doi: 10.1016/j.ifset.2005.12.005
    • (2006) Innovative Food Science & Emerging Technologies , vol.7 , Issue.3 , pp. 233-238
    • Kleber, N.1    Weyrich, U.2    Hinrichs, J.3
  • 21
    • 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
    • Z.Li,, Y.K.Luo,, & L.G.Feng, (2011). Effects of Maillard reaction conditions on the antigenicity of α-lactalbumin and β-lactoglobulin in whey protein conjugated with maltose. European Food Research and Technology, 233(3), 387–394. doi: 10.1007/s00217-011-1532-7
    • (2011) European Food Research and Technology , vol.233 , Issue.3 , pp. 387-394
    • Li, Z.1    Luo, Y.K.2    Feng, L.G.3
  • 22
    • 84863152868 scopus 로고    scopus 로고
    • Effects of pH, temperature, enzyme-to-substrate ratio and reaction time on the antigenicity of casein hydrolysates prepared by papain
    • X.Y.Liu,, Y.K.Luo,, & Z.Li, (2012). Effects of pH, temperature, enzyme-to-substrate ratio and reaction time on the antigenicity of casein hydrolysates prepared by papain. Food and Agricultural Immunology, 23(1), 69–82. doi: 10.1080/09540105.2011.604770
    • (2012) Food and Agricultural Immunology , vol.23 , Issue.1 , pp. 69-82
    • Liu, X.Y.1    Luo, Y.K.2    Li, Z.3
  • 23
  • 24
    • 33646049733 scopus 로고    scopus 로고
    • Functional milk proteins: production and utilization
    • P. F. Fox & P. L. H. McSweeney (Eds.), New York: Springer
    • D.Mulvihill,, & M.Ennis, (2003). Functional milk proteins: production and utilization. In P. F. Fox & P. L. H. McSweeney (Eds.), Advanced dairy chemistry—1 Proteins (pp. 1175–1228). New York: Springer.
    • (2003) Advanced dairy chemistry—1 Proteins , pp. 1175-1228
    • Mulvihill, D.1    Ennis, M.2
  • 25
    • 0033668026 scopus 로고    scopus 로고
    • Heat-induced interactions of β-lactoglobulin and α-lactalbumin with the casein micelle in pH-adjusted skim milk
    • D.J.Oldfield,, H.Singh,, M.W.Taylor,, & K.N.Pearce, (2000). Heat-induced interactions of β-lactoglobulin and α-lactalbumin with the casein micelle in pH-adjusted skim milk. International Dairy Journal, 10(8), 509–518. doi: 10.1016/S0958-6946(00)00087-X
    • (2000) International Dairy Journal , vol.10 , Issue.8 , pp. 509-518
    • Oldfield, D.J.1    Singh, H.2    Taylor, M.W.3    Pearce, K.N.4
  • 26
    • 33646693647 scopus 로고    scopus 로고
    • High pressure can reduce the antigenicity of bovine whey protein hydrolysates
    • E.Peñas,, H.Snel,, R.Floris,, G.Préstamo,, & R.Gomez, (2006). High pressure can reduce the antigenicity of bovine whey protein hydrolysates. International Dairy Journal, 16(9), 969–975. doi: 10.1016/j.idairyj.2005.09.010
    • (2006) International Dairy Journal , vol.16 , Issue.9 , pp. 969-975
    • Peñas, E.1    Snel, H.2    Floris, R.3    Préstamo, G.4    Gomez, R.5
  • 27
    • 0032344471 scopus 로고    scopus 로고
    • Influence of the lactose concentration on the denaturation kinetics of whey proteins in concentrated sweet whey
    • J.Plock,, T.Spiegel,, & H.Kessler, (1998). Influence of the lactose concentration on the denaturation kinetics of whey proteins in concentrated sweet whey. Milchwissenschaft, 53(7), 389–393.
    • (1998) Milchwissenschaft , vol.53 , Issue.7 , pp. 389-393
    • Plock, J.1    Spiegel, T.2    Kessler, H.3
  • 28
    • 84878730992 scopus 로고    scopus 로고
    • Effect of thermal processing of cow and buffalo milk on the allergenic response to caseins and whey proteins in mice
    • U.K.Shandilya,, R.Kapila,, R.M.Haq,, S.Kapila,, & V.K.Kansal, (2013). Effect of thermal processing of cow and buffalo milk on the allergenic response to caseins and whey proteins in mice. Journal of the Science of Food and Agriculture, 93(9), 2287–2292. doi: 10.1002/jsfa.6041
    • (2013) Journal of the Science of Food and Agriculture , vol.93 , Issue.9 , pp. 2287-2292
    • Shandilya, U.K.1    Kapila, R.2    Haq, R.M.3    Kapila, S.4    Kansal, V.K.5
  • 30
    • 84888095981 scopus 로고    scopus 로고
    • Effects of fermentation by Lactobacillus casei on the antigenicity and allergenicity of four bovine milk proteins
    • J.Shi,, Y.K.Luo,, Y.Xiao,, Z.Li,, Q.Xu,, & M.J.Yao, (2014). Effects of fermentation by Lactobacillus casei on the antigenicity and allergenicity of four bovine milk proteins. International Dairy Journal, 35(1), 75–80. doi: 10.1016/j.idairyj.2013.10.010
    • (2014) International Dairy Journal , vol.35 , Issue.1 , pp. 75-80
    • Shi, J.1    Luo, Y.K.2    Xiao, Y.3    Li, Z.4    Xu, Q.5    Yao, M.J.6
  • 31
    • 67049174179 scopus 로고    scopus 로고
    • Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients
    • A.Taheri-Kafrani,, J.-C.Gaudin,, H.Rabesona,, C.Nioi,, D.Agarwal,, M.Drouet,, (2009). Effects of heating and glycation of β-lactoglobulin on its recognition by IgE of sera from cow milk allergy patients. Journal of Agricultural and Food Chemistry, 57(11), 4974–4982. doi: 10.1021/jf804038t
    • (2009) Journal of Agricultural and Food Chemistry , vol.57 , Issue.11 , pp. 4974-4982
    • Taheri-Kafrani, A.1    Gaudin, J.-C.2    Rabesona, H.3    Nioi, C.4    Agarwal, D.5    Drouet, M.6
  • 33
    • 8644235852 scopus 로고    scopus 로고
    • Bovine milk allergenicity
    • J.-M.Wal, (2004). Bovine milk allergenicity. Annals of Allergy, Asthma & Immunology, 93(5), S2–S11. doi: 10.1016/S1081-1206(10)61726-7
    • (2004) Annals of Allergy, Asthma & Immunology , vol.93 , Issue.5 , pp. S2-S11
    • Wal, J.-M.1
  • 34
    • 84924853575 scopus 로고    scopus 로고
    • Study on reducing antigenic response and IgE-binding inhibitions of four milk proteins of Lactobacillus casei 1134
    • M.J.Yao,, Q.Xu,, Y.K.Luo,, J.Shi,, & Z.Li, (2015). Study on reducing antigenic response and IgE-binding inhibitions of four milk proteins of Lactobacillus casei 1134. Journal of the Science of Food and Agriculture, 95(6), 1303–1312. doi: 10.1002/jsfa.6823
    • (2015) Journal of the Science of Food and Agriculture , vol.95 , Issue.6 , pp. 1303-1312
    • Yao, M.J.1    Xu, Q.2    Luo, Y.K.3    Shi, J.4    Li, Z.5
  • 35
    • 1542575981 scopus 로고    scopus 로고
    • Kinetics of heat-induced association of β-lactoglobulin and α-lactalbumin with milk fat globule membrane in whole milk
    • A.Ye,, H.Singh,, D.James Oldfield,, & S.Anema, (2004). Kinetics of heat-induced association of β-lactoglobulin and α-lactalbumin with milk fat globule membrane in whole milk. International Dairy Journal, 14(5), 389–398. doi: 10.1016/j.idairyj.2003.09.004
    • (2004) International Dairy Journal , vol.14 , Issue.5 , pp. 389-398
    • Ye, A.1    Singh, H.2    James Oldfield, D.3    Anema, S.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.