메뉴 건너뛰기




Volumn 64, Issue 1, 2009, Pages 12-15

Applications of novel technologies in processing of functional foods

Author keywords

[No Author keywords available]

Indexed keywords


EID: 63749094297     PISSN: 00049433     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Conference Paper
Times cited : (21)

References (52)
  • 1
    • 0031905287 scopus 로고    scopus 로고
    • Specificity of the human IgE response to the different caseins in allergy to cow's milk proteins
    • Bernard, H., Creminon, C., Yvon, M. and Wal J.M. (1998), Specificity of the human IgE response to the different caseins in allergy to cow's milk proteins, Int. Arch. Allergy Immunol. 115, 235-244.
    • (1998) Int. Arch. Allergy Immunol , vol.115 , pp. 235-244
    • Bernard, H.1    Creminon, C.2    Yvon, M.3    Wal, J.M.4
  • 5
    • 0036424566 scopus 로고    scopus 로고
    • Identification of sequential IgE-binding epitopes on bovine alpha(s2)-casein in cow's milk allergic patients
    • Busse, P.J., Jarvinen, K.M., Vila, L., Beyer, K. and Sampson, H.A. (2002), Identification of sequential IgE-binding epitopes on bovine alpha(s2)-casein in cow's milk allergic patients. Int. Arch. of Allergy Immunol. 129, 93-96.
    • (2002) Int. Arch. of Allergy Immunol , vol.129 , pp. 93-96
    • Busse, P.J.1    Jarvinen, K.M.2    Vila, L.3    Beyer, K.4    Sampson, H.A.5
  • 6
    • 63749124072 scopus 로고    scopus 로고
    • Pressure treating foods to reduce spoilage.
    • International Patent WO 2004/032655
    • Carroll, T., Chen, P., Harnett, M. and Harnett, J. (2004), Pressure treating foods to reduce spoilage. International Patent WO 2004/032655.
    • (2004)
    • Carroll, T.1    Chen, P.2    Harnett, M.3    Harnett, J.4
  • 8
    • 0035724636 scopus 로고    scopus 로고
    • Identification of IgE and IgG binding epitopes on beta- and kappa-casein in cow's milk allergic patients
    • Chatchatee, P., Jarvinen, K.M., Bardina, L., Vila, L., Beyer, K. and Sampson, H.A. (2001), Identification of IgE and IgG binding epitopes on beta- and kappa-casein in cow's milk allergic patients. Clin. Exp. Allergy 31, 1256-1262.
    • (2001) Clin. Exp. 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
  • 9
    • 46949094923 scopus 로고    scopus 로고
    • Hydrolysis under pressure as a means to reduce the binding of β-Lactoglobulin to immunoglobulin E from human sera
    • Chicon, R., Bellque, J., Alonso, E., Martin-Alvarez, P.J. and Lopez-Fandino, R. (2008), Hydrolysis under pressure as a means to reduce the binding of β-Lactoglobulin to immunoglobulin E from human sera. J. Food Protect. 71, 453-1459.
    • (2008) J. Food Protect , vol.71 , pp. 453-1459
    • Chicon, R.1    Bellque, J.2    Alonso, E.3    Martin-Alvarez, P.J.4    Lopez-Fandino, R.5
  • 10
    • 33645760729 scopus 로고    scopus 로고
    • Changes in chymotrypsin hydrolysis of β-Lactoglobulin A induced by high hydrostatic pressure
    • Chicon, R., Lopez-Fandino, R., Quiros, A. and Bellque, J. (2006), Changes in chymotrypsin hydrolysis of β-Lactoglobulin A induced by high hydrostatic pressure. J. Agric. Food Chem. 54, 2333-2341.
    • (2006) J. Agric. Food Chem , vol.54 , pp. 2333-2341
    • Chicon, R.1    Lopez-Fandino, R.2    Quiros, A.3    Bellque, J.4
  • 12
    • 0028950420 scopus 로고
    • Hydrolysis of β-lactoglobulin by thermolysin and pepsin under high hydrostatic pressure
    • Dufour, E., Herve, G. and Heartle, T. (1995), Hydrolysis of β-lactoglobulin by thermolysin and pepsin under high hydrostatic pressure. Biopolymers 35, 475-483.
    • (1995) Biopolymers , vol.35 , pp. 475-483
    • Dufour, E.1    Herve, G.2    Heartle, T.3
  • 13
    • 1542286920 scopus 로고    scopus 로고
    • Modification of IgE-binding during heat processing of the cow's milk allergen β-lactoglobulin
    • Ehn, B., Ekstrand, B., Bengtsson, U. and Ahlsted, S. (2004), Modification of IgE-binding during heat processing of the cow's milk allergen β-lactoglobulin, J. Agric. Food Chem. 52, 1398-1403.
    • (2004) J. Agric. Food Chem , vol.52 , pp. 1398-1403
    • Ehn, B.1    Ekstrand, B.2    Bengtsson, U.3    Ahlsted, S.4
  • 14
    • 0029790266 scopus 로고    scopus 로고
    • The lipocalin family: Structure and function
    • Flower, D.R. (1996), The lipocalin family: Structure and function, Biochem. J 318, 1-14.
    • (1996) Biochem. J , vol.318 , pp. 1-14
    • Flower, D.R.1
  • 15
    • 0018675107 scopus 로고
    • IgE antibodies to peptic and peptic-tryptic digests of β-Lg: Significance in food hypersensitivity
    • Haddad, Z.H., Kalra, V. and Verma, S. (1979), IgE antibodies to peptic and peptic-tryptic digests of β-Lg: significance in food hypersensitivity, Ann. Allergy 42, 368-371.
    • (1979) Ann. Allergy , vol.42 , pp. 368-371
    • Haddad, Z.H.1    Kalra, V.2    Verma, S.3
  • 16
    • 13944261678 scopus 로고    scopus 로고
    • Potential applications of high pressure homogenisation in processing of liquid milk
    • Hayes, M.G., Fox, P.F., and Kelly, A.L. (2005), Potential applications of high pressure homogenisation in processing of liquid milk. J Dairy Res. 72, 25-33.
    • (2005) J Dairy Res , vol.72 , pp. 25-33
    • Hayes, M.G.1    Fox, P.F.2    Kelly, A.L.3
  • 18
    • 33645975504 scopus 로고    scopus 로고
    • High pressure-induced changes in bovine milk proteins: A review
    • Huppertz, T., Fox, P.F., De Kruif, C.G. and Kelly, A.L. (2006b), High pressure-induced changes in bovine milk proteins: a review. Biochim Biophys. Acta, 1764, 593-598.
    • (2006) Biochim Biophys. Acta , vol.1764 , pp. 593-598
    • Huppertz, T.1    Fox, P.F.2    De Kruif, C.G.3    Kelly, A.L.4
  • 19
    • 39149126312 scopus 로고    scopus 로고
    • Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor
    • Indyk, H.E., Williams, J. W. and Patel, H.A. (2008), Analysis of denaturation of bovine IgG by heat and high pressure using an optical biosensor. Int. Dairy J 18, 359-366.
    • (2008) Int. Dairy J , vol.18 , pp. 359-366
    • Indyk, H.E.1    Williams, J.W.2    Patel, H.A.3
  • 20
    • 0035208510 scopus 로고    scopus 로고
    • IgE and IgG binding epitopes on alpha Lactalbumin and β-Lg in cow's milk allergy
    • Jarvenin, K.M., Chatchatee, P., Bardina L., et al. (2001), IgE and IgG binding epitopes on alpha Lactalbumin and β-Lg in cow's milk allergy. Int. Arch. Allergy Immunol. 126, 111-118.
    • (2001) Int. Arch. Allergy Immunol , vol.126 , pp. 111-118
    • Jarvenin, K.M.1    Chatchatee, P.2    Bardina, L.3
  • 21
    • 33846785047 scopus 로고    scopus 로고
    • Antigenic response of bovine beta-lactoglobulin influenced by ultra-high pressure treatment and temperature
    • Kleber, N., Maier, S. and Hinrichs, J. (2007), Antigenic response of bovine beta-lactoglobulin influenced by ultra-high pressure treatment and temperature. Inn. Food Sci. Emerg. Technol. 8, 39-45.
    • (2007) Inn. Food Sci. Emerg. Technol , vol.8 , pp. 39-45
    • Kleber, N.1    Maier, S.2    Hinrichs, J.3
  • 22
    • 21044455900 scopus 로고    scopus 로고
    • The antigenic response of beta-lactoglobulin is mediated by thermally induced aggregation
    • Kleber, N., Krause, I., Illgner, S. and Hinricks, J. (2004), The antigenic response of beta-lactoglobulin is mediated by thermally induced aggregation. Eur. Food Res. Tech. 219, 105-110.
    • (2004) Eur. Food Res. Tech , vol.219 , pp. 105-110
    • Kleber, N.1    Krause, I.2    Illgner, S.3    Hinricks, J.4
  • 23
    • 0038528585 scopus 로고    scopus 로고
    • Effects of pulsed electric fields and thermal processing on the stability of bovine immunoglobulin G (IgG) in enriched soymilk
    • Li, S.Q., Zhang, Q.H., Lee, Y.Z. and Pham, T,V. (2003), Effects of pulsed electric fields and thermal processing on the stability of bovine immunoglobulin G (IgG) in enriched soymilk. J. Food Sci. 68, 1201-1207.
    • (2003) J. Food Sci , vol.68 , pp. 1201-1207
    • Li, S.Q.1    Zhang, Q.H.2    Lee, Y.Z.3    Pham, T.V.4
  • 24
    • 13244259221 scopus 로고    scopus 로고
    • Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G
    • Li, S.Q., Boser, J.A. and Zhang, Q.H. (2005), Effects of pulsed electric fields and heat treatment on stability and secondary structure of bovine immunoglobulin G. J. Agric. Food Chem. 53, 663-670.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 663-670
    • Li, S.Q.1    Boser, J.A.2    Zhang, Q.H.3
  • 25
    • 2542490246 scopus 로고    scopus 로고
    • Food processing effects on allergenicity
    • Maleki, S.J. (2004), Food processing effects on allergenicity. Curr. Opin. Allergy Clin. Immunol. 4, 241-245.
    • (2004) Curr. Opin. Allergy Clin. Immunol , vol.4 , pp. 241-245
    • Maleki, S.J.1
  • 27
    • 0031999039 scopus 로고    scopus 로고
    • Effect of high-pressure treatment on the tryptic hydrolysis of bovine β-lactoglobulin AB
    • Maynard, F., Weingand, A., Hau, J. and Jost, R. (1998), Effect of high-pressure treatment on the tryptic hydrolysis of bovine β-lactoglobulin AB. Int. Dairy J. 8, 125-133.
    • (1998) Int. Dairy J , vol.8 , pp. 125-133
    • Maynard, F.1    Weingand, A.2    Hau, J.3    Jost, R.4
  • 28
    • 0030849219 scopus 로고    scopus 로고
    • Human IgE binding capacity of tryptic peptides from bovine alpha-lactalbumin
    • Maynard, F., Jost, R., and Wal, J.M. (1997), Human IgE binding capacity of tryptic peptides from bovine alpha-lactalbumin. Int. Arch. Allergy Immunol. 113, 478-88.
    • (1997) Int. Arch. Allergy Immunol , vol.113 , pp. 478-488
    • Maynard, F.1    Jost, R.2    Wal, J.M.3
  • 29
    • 0024351478 scopus 로고
    • Chemical characterization of bioactive peptides from in vivo digests of casein
    • Meisel, H. and Frister, H. (1989), Chemical characterization of bioactive peptides from in vivo digests of casein. J. Dairy Sci. 56, 343-349.
    • (1989) J. Dairy Sci , vol.56 , pp. 343-349
    • Meisel, H.1    Frister, H.2
  • 32
    • 63749114846 scopus 로고    scopus 로고
    • High pressure processing of metal ion lactoferrin.
    • International Patent WO 2006/096073
    • Palmano, K.P., Patel, H.A., Carroll, T.J., Elgar, D.F. and Gonzalez-Martin, M.A. (2006), High pressure processing of metal ion lactoferrin. International Patent WO 2006/096073.
    • (2006)
    • Palmano, K.P.1    Patel, H.A.2    Carroll, T.J.3    Elgar, D.F.4    Gonzalez-Martin, M.A.5
  • 33
    • 57049105497 scopus 로고    scopus 로고
    • New dairy processing technologies
    • Eds. Chandan, R.C, Kilara, A. and Shah, N.R, Elsevier, London, pp
    • Patel, H., Carroll, T. and Kelly, A.L. (2008), New dairy processing technologies. In: Dairy Processing Technology and Quality Assurance (Eds. Chandan, R.C., Kilara, A. and Shah, N.R). Elsevier, London, pp. 465-482.
    • (2008) Dairy Processing Technology and Quality Assurance , pp. 465-482
    • Patel, H.1    Carroll, T.2    Kelly, A.L.3
  • 34
    • 28944443945 scopus 로고    scopus 로고
    • Pressure-induced unfolding and aggregation of the proteins in whey protein concentrate solutions
    • Patel, H.A., Singh, H., Havea, P., Considine, T. and Creamer, L.K. (2005), Pressure-induced unfolding and aggregation of the proteins in whey protein concentrate solutions. J. Agric. Food Chem. 53, 9590-9601.
    • (2005) J. Agric. Food Chem , vol.53 , pp. 9590-9601
    • Patel, H.A.1    Singh, H.2    Havea, P.3    Considine, T.4    Creamer, L.K.5
  • 35
    • 33646693647 scopus 로고    scopus 로고
    • High pressure can reduce the antigenicity of bovine whey hydrolysates
    • Penas, E., Snell, H., Floris, R., Prestamo, G. and Gomez, R. (2006), High pressure can reduce the antigenicity of bovine whey hydrolysates. Int. Dairy J. 16, 969-975.
    • (2006) Int. Dairy J , vol.16 , pp. 969-975
    • Penas, E.1    Snell, H.2    Floris, R.3    Prestamo, G.4    Gomez, R.5
  • 36
    • 34249318078 scopus 로고    scopus 로고
    • Rivas, A., Rodrigo, D., Company, B., Sampedro, F. and Rodrigo, M. (2007), Effects of pulsed electric fields on water-soluble vitamins and ACE inhibitory peptides added to a mixed orange juice and milk beverage. Food Chem. 104, 1550-1559.
    • Rivas, A., Rodrigo, D., Company, B., Sampedro, F. and Rodrigo, M. (2007), Effects of pulsed electric fields on water-soluble vitamins and ACE inhibitory peptides added to a mixed orange juice and milk beverage. Food Chem. 104, 1550-1559.
  • 40
    • 34047183005 scopus 로고    scopus 로고
    • Acid coagulation properties and suitability for yogurt production of cows' milk treated by high-pressure homogenisation
    • Serra, M., Trujillo, A.J., Quevedo, J.M., Guamis, B. and Ferragut, V. (2007), Acid coagulation properties and suitability for yogurt production of cows' milk treated by high-pressure homogenisation. Int. Dairy J. 17, 782-790.
    • (2007) Int. Dairy J , vol.17 , pp. 782-790
    • Serra, M.1    Trujillo, A.J.2    Quevedo, J.M.3    Guamis, B.4    Ferragut, V.5
  • 41
    • 0000552061 scopus 로고
    • Tryptic and chymotryptic hydrolysis of β-lactoglobulin-A, β-lactoglobulin-B and β-lactoglobulin-AB at ambient and high pressure
    • Van Willige, R.W.G. and Fitzgerald, R.J. (1995), Tryptic and chymotryptic hydrolysis of β-lactoglobulin-A, β-lactoglobulin-B and β-lactoglobulin-AB at ambient and high pressure. Milchwissenschaft 50, 183-186.
    • (1995) Milchwissenschaft , vol.50 , pp. 183-186
    • Van Willige, R.W.G.1    Fitzgerald, R.J.2
  • 42
    • 0037048746 scopus 로고    scopus 로고
    • Rheological properties of yoghurt made with milk submitted to manothermosonication
    • Vercet, A., Oria, R., Marquina, P., Crelier, S. and Lopez-Buesa, P. (2002), Rheological properties of yoghurt made with milk submitted to manothermosonication. J. Agric. Food Chem. 50, 6165-6171.
    • (2002) J. Agric. Food Chem , vol.50 , pp. 6165-6171
    • Vercet, A.1    Oria, R.2    Marquina, P.3    Crelier, S.4    Lopez-Buesa, P.5
  • 43
    • 0034795756 scopus 로고    scopus 로고
    • Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy
    • Vila, L., Beyer, K., Jarvinen, K.M., Chatchatee, P., Bardina, L. and Sampson, H.A. (2001), Role of conformational and linear epitopes in the achievement of tolerance in cow's milk allergy. Clin. Exp. Allergy 31, 1599-1606.
    • (2001) Clin. Exp. Allergy , vol.31 , pp. 1599-1606
    • Vila, L.1    Beyer, K.2    Jarvinen, K.M.3    Chatchatee, P.4    Bardina, L.5    Sampson, H.A.6
  • 44
    • 33845276210 scopus 로고    scopus 로고
    • High hydrostatic pressure enhances whey protein digestibility to generate whey peptides that improve glutathione status in CTFR-deficient epithelial cells
    • Vilela, R.M., Lands, L.C., Chan, H.M., Azadi, B. and Kubow, S. (2006), High hydrostatic pressure enhances whey protein digestibility to generate whey peptides that improve glutathione status in CTFR-deficient epithelial cells. Mol. Nutr. Food Res. 11 1013-1029.
    • (2006) Mol. Nutr. Food Res , vol.11 , pp. 1013-1029
    • Vilela, R.M.1    Lands, L.C.2    Chan, H.M.3    Azadi, B.4    Kubow, S.5
  • 45
    • 0033483846 scopus 로고    scopus 로고
    • Effect of ultrasound processing on the quality of dairy products
    • Villamiel, M., van Hamersveld, E.H. and de Jong, P. (1999), Effect of ultrasound processing on the quality of dairy products. Milchwissenschaft 54, 69-73.
    • (1999) Milchwissenschaft , vol.54 , pp. 69-73
    • Villamiel, M.1    van Hamersveld, E.H.2    de Jong, P.3
  • 46
    • 0034974942 scopus 로고    scopus 로고
    • Structure and function of milk allergens
    • Wal, J.M. (2001), Structure and function of milk allergens. Allergy, 56, 35-38.
    • (2001) Allergy , vol.56 , pp. 35-38
    • Wal, J.M.1
  • 49
    • 34548285780 scopus 로고    scopus 로고
    • Heat treatment of bovine alpha lactalbumin results in partially folded disulfide bond shuffled states with enhanced surface activity
    • Wejishina-Bettoni, R., Gao, C., Jenkins, J.A., Mackie, A.R., Wilde, P.J., Mills, E.N.C. and Smith, L.J. (2007), Heat treatment of bovine alpha lactalbumin results in partially folded disulfide bond shuffled states with enhanced surface activity. Biochem. 46, 9774-9784.
    • (2007) Biochem , vol.46 , pp. 9774-9784
    • Wejishina-Bettoni, R.1    Gao, C.2    Jenkins, J.A.3    Mackie, A.R.4    Wilde, P.J.5    Mills, E.N.C.6    Smith, L.J.7
  • 51
    • 63749092721 scopus 로고    scopus 로고
    • Zhang, H.P., Deligelsang, Guo, J. and Mu, Z.S. (1998), Denaturation of bovine milk IgG at high pressure and its stability. Food Sci. China 19(4), 10-12.
    • Zhang, H.P., Deligelsang, Guo, J. and Mu, Z.S. (1998), Denaturation of bovine milk IgG at high pressure and its stability. Food Sci. China 19(4), 10-12.
  • 52
    • 36348936097 scopus 로고    scopus 로고
    • Effect of high pressure treatment on in vitro digestibility of β-Lactoglobulin
    • Zeece, M., Huppretz, T. and Kelly, A.L. (2008), Effect of high pressure treatment on in vitro digestibility of β-Lactoglobulin. Inn. Food Sci. Emerg. Technol. 9, 62-69.
    • (2008) Inn. Food Sci. Emerg. Technol , vol.9 , pp. 62-69
    • Zeece, M.1    Huppretz, T.2    Kelly, A.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.